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dolichyl beta-D-mannosyl phosphate + biotin-Tyr-Leu-Ala-Val-NH2
?
-
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
dolichyl beta-D-mannosyl phosphate + synthetic peptide based on a mucin-like domain in alpha-dystroglycan
?
-
-
-
-
?
dolichyl D-mannosyl phosphate + YATAVK-Btn
dolichyl phosphate + O-D-mannosyl-YATAVK-Btn
photocross-linking reaction based on the peptide YATAVK-Btn that serves as in vitro mannosyl acceptor substrate of Pmt1p/Pmt2p and is O -mannosylated to a similar extent as the known acceptor peptide AcNH-YATAV-CONH2
-
-
?
dolichyl phosphate D-mannose + Ac-Ala-Thr-Ala-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Ala-Thr-Ala-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
dolichyl phosphate D-mannose + alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
-
in vitro asssay with both enzyme isoforms (RT and TW), 20 mM Tris, pH 8.0, mercaptoethanol, EDTA, n-octyl-beta-D-thioglucoside, sugar donor is tritium-labeled, alpha-dystroglycan isoform C contains mucin-type domain that is target of O-mannose modifications in mammals, high grade of O-mannosylation, A isoform without noticeable O-mannosylation, rabbit alpha-dystroglycan as positive control shows lower O-mannosylation
-
-
?
dolichyl phosphate D-mannose + alpha-dystroglycan glutathione-S-transferase fusion protein
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
sugar donor tritium-labeled
-
-
?
dolichyl phosphate D-mannose + Asn-Ala-Thr-Val-dinitrophenyl
dolichyl phosphate + O-D-mannosyl-Asn-Ala-Thr-Val-dinitrophenyl
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate D-mannose + biotin-Tyr-Pro-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Pro-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Gas1p
dolichyl phosphate + O-D-mannosyl-Gas1p
-
-
-
-
?
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl-[glucoamylase]
-
extracellular Aspergillus awamori protein as reporter for glycosylation measurements, underglycosylation upon AnpmtA, AnpmtB, and AnpmtC diruption
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
-
tritium-labeled sugar donor, 20 mM Tris-HCl, pH 8.0, 2-mercaptoethanol, EDTA, n-octyl-beta-D-thiogucoside, 22°C
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[glutathione-S-transferase fusion alpha-dystroglycan]
-
-
-
-
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
dolichyl phosphate D-mannose + Lys-Pro-Ser-Gly-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Ser-Gly-Tyr
-
-
-
?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Gly-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Gly-Tyr
-
-
-
?
dolichyl phosphate D-mannose + Lys-Pro-Thr-Pro-Tyr
dolichyl phosphate + O-D-mannosyl-Lys-Pro-Thr-Pro-Tyr
-
-
-
?
dolichyl phosphate D-mannose + N-acetyl-SSSSS
dolichyl phosphate + O-D-mannosyl-N-acetyl-SSSSS
-
worst substrate
-
-
?
dolichyl phosphate D-mannose + N-acetyl-YASAV
dolichyl phosphate + O-D-mannosyl-N-acetyl-YASAV
-
-
-
-
?
dolichyl phosphate D-mannose + N-acetyl-YATAV
dolichyl phosphate + O-D-mannosyl-N-acetyl-YATAV
-
best substrate
-
-
?
dolichyl phosphate D-mannose + N-acetyl-YATAVK-biotin
dolichyl phosphate + O-D-mannosyl-N-acetyl-YATAVK-biotin
-
N-acetyl-YATAVK-biotin preferentially reacts with isoform Pmt1p
-
-
?
dolichyl phosphate D-mannose + Pro-Thr-Val
dolichyl phosphate + O-D-mannosyl-Pro-Thr-Val
-
-
-
?
dolichyl phosphate D-mannose + Pro-Tyr-Thr-Val
dolichyl phosphate + O-D-mannosyl-Pro-Tyr-Thr-Val
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
dolichyl phosphate D-mannose + RSPSPSTQ
dolichyl phosphate + O-D-mannosyl-RSPSPSTQ
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
dolichyl phosphate D-mannose + Tyr-Asn-Leu-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Leu-Thr-Ser-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-alpha-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Leu-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Leu-Thr-Ala-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Pro-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Pro-Thr-Ala-Val
-
-
-
?
additional information
?
-
dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
substrates used are Dol-P-[3H]mannose and 3.5 mM acceptor peptide Ac-YATAV-NH2
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
substrates used are Dol-P-[3H]mannose and 3.5 mM acceptor peptide Ac-YATAV-NH2
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
recombinant yeast overproducing PMT1 and PMT2
-
ir
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
PMT1
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Ala-Thr-Ala-Val-NH2
-
PMT1 transfers preferably to the threonine and valine residues, the additional enzyme form prefers the serine residue, both depending on the sequence of the acceptor substrate peptide
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
?
dolichyl phosphate D-mannose + Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
dolichyl phosphate + O-D-mannosyl-Ac-Tyr-Asn-Pro-Thr-Ser-Val-NH2
-
-
-
ir
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
-
-
-
ir
dolichyl phosphate D-mannose + AcSSSSSNH2
dolichyl phosphate + O-D-mannosyl-AcSSSSSNH2
-
PMT1-3, PMT5, PMT6, not PMT4
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + biotin-Tyr-Ala-Thr-Ala-Val-NH2
dolichyl phosphate + O-D-mannosyl-N-biotinyl-Tyr-Ala-Thr-Ala-Val-NH2
-
-
-
?
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
-
-
-
?
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
the AaPmtA protein is involved in the formation of the normal cell wall. AaPmtA protein is responsible for the transfer of mannose to glucoamylase I
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-glutathione-S-transferase fusion alpha-dystroglycan
-
-
-
-
?
dolichyl phosphate D-mannose + glutathione-S-transferase fusion alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-glutathione-S-transferase fusion alpha-dystroglycan
-
-
-
-
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
-
whole protein or N-terminal dodecapeptide containing Trp7
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
-
C-mannosylation activity
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
-
no C-mannosylation activity of Trp7 when Trp10 is exchanged for Ala in the acceptor substrate
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + human ribonuclease 2
dolichyl phosphate + human ribonuclease 2-D-mannose
-
recombinant wild-type RNase from E. coli is no substrate
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
central role for Pmt4-mediated protein O-mannosylation in growth, cell wall integrity, and virulence of Cryptococcus neoformans
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
catalyzes the initial step of O-mannosyl glycan biosynthesis
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
synthetic peptides based on a mucin-like domain in alpha-dystroglycan. Thr414 of peptide 401-420 and Thr351 of peptide 336-355 are prominently modified by O-mannosylation
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
role of O-glycosylation in the control of folding of secretory proteins in the endoplasmic reticulum
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate: human-granulocyte-macrophage colony-stimulating-factor-derived peptide(4-11)
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
the enzyme transfers mannosyl residues to the hydroxyl of serine or threonine residues
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
preferred chain lengthin decreasing order: C100, C80, C55, C35
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
preferred chain lengthin decreasing order: C100, C80, C55, C35
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate specificity study
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
strictly stereospecific for the anomeric configuration of phosphoryl-linkage of the donor substrate, a saturated alpha-isoprene unit in the dolichyl moiety is required
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acidic amino acids strongly inhibit acceptor activity, as do glycine and proline residues as amino-terminal and carboxy-terminal neighbours
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate: HCl-treated cell wall mannoprotein from Saccharomyces cerevisiae
-
ir
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate specificities of PMT1-4,6
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential. ogm4D mutants differ morphologically from wild type and exhibit defects in sexual agglutination
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
protein O-mannosylation is crucial for cell wall integrity, septation and viability
-
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
i.e. small-agglutinin
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
activity is not affected by disruption mutations of PMT1-4
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
protein is located at the cell surface
-
-
?
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
the un-glycosylated 32 kDa protein is an ortholog of Wsc family proteins in Saccharomyces cerevisiae, these proteins serve as sensors of stress, such as high temperature and cell wall-perturbing chemicals
AN5660
-
?
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
the non-glycosylated 32 kDa protein is an ortholog of Wsc family proteins in Saccharomyces cerevisiae, these proteins serve as sensors of stress, such as high temperature and cell wall-perturbing chemicals, S-tagged AN5660 is hypo-glycosylated in the deltapmtA and deltapmtC deletion mutants (target for these isoforms), not in the deltapmtB deletion mutant (no target)
AN5660
-
?
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
-
triple-hemagglutin-tagged AN5660.3 protein is an ortholog of Wsc1 protein of Saccharomyces cerevisiae, a sensor for cell wall stress, underglycosylation upon AnpmtA and AnpmtC diruption not due to AnpmtB disruption
AN5660
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
-
PMT1 and PMT2, not PMT3 and PMT4
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
-
protein is located in the medium
-
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
PMT1
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
PMT1, PMT4, PMT6 and especially PMT2, not PMT3
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
protein is located in the cell wall and medium
-
-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
-
PMT4 and PMT6, not PMT1-3
-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
-
protein is located at the cell surface
-
-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
-
PMT4, not PMT1-3
-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
-
protein is located in the Golgi apparatus
-
-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
-
mainly PMT1 and PMT2, not PMT3 and PMT4
-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
-
protein is located in the Golgi apparatus
-
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
PMT1
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
PMT1, PMT2, and to some extent PMT4, not PMT3
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
protein is located in the medium
-
-
?
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
-
C-mannosylation activity
-
-
?
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
-
C-mannosylation activity
D-mannose is bound at Trp7 forming a C-C linkage
?
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
-
biosynthetic pathway
-
-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Ala-Thr-Ala-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Ala-Thr-Ala-Val
wild-type and mutants
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
-
-
-
?
dolichyl phosphate D-mannose + Tyr-Asn-Pro-Thr-Ser-Val
dolichyl phosphate + O-D-mannosyl-Tyr-Asn-Pro-Thr-Ser-Val
-
-
-
?
additional information
?
-
-
Afpmt1 acts as an O-mannosyltransferase. Characterization of the DELTAAfpmt1 mutant shows that a lack of AfPmt1p results in sensitivity to elevated temperature and defects in growth and cell wall integrity, thereby affecting cell morphology, conidium formation, and germination. In a mouse model, Afpmt1 is not required for the virulence of Aspergillus fumigatus
-
-
?
additional information
?
-
-
PMT2 is essential for growth
-
-
?
additional information
?
-
-
PMT4 is required for full virulence of Candida albicans
-
-
?
additional information
?
-
-
PMT5 does not make a significant contribution to virulence
-
-
?
additional information
?
-
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
-
protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
Drosophila sp. (in: flies)
-
protein O-mannosyltransferases 1 and 2 are required to maintain integrity of Drosophila larval muscles
-
-
?
additional information
?
-
-
O-mannosylation of specific secretory proteins of the bacterial pathogen Mycobacterium tuberculosis contributes significantly to virulence
-
-
?
additional information
?
-
-
although the improved secretion of the protein by suppression of O mannosylation might not be a general phenomenon, the suppression of O mannosylation could be beneficial for the production of proteins forming either homomeric or heteromeric complexes through their hydrophobic interaction in yeast
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
PMT3: no clearly determined dolichyl-phosphate-mannose-protein mannosyltransferase activity
-
-
?
additional information
?
-
-
PMT4 and PMT6 probably function as an active dimer
-
-
?
additional information
?
-
-
PMT1 and PMT2 function as a complex
-
-
?
additional information
?
-
-
PMT1 and PMT2 function as a complex
-
-
?
additional information
?
-
-
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
-
-
?
additional information
?
-
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
-
-
?
additional information
?
-
PMT3 behaves as a dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130
-
-
?
additional information
?
-
-
defective mutants are used to investigate the substrate specificities of PMT1-4,6 in vivo
-
-
?
additional information
?
-
disruption of the pmt1 gene decreased protein secretion but has no effect on glycosylation of secreted proteins. PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins
-
-
?
additional information
?
-
-
disruption of the pmt1 gene decreased protein secretion but has no effect on glycosylation of secreted proteins. PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins
-
-
?
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dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
dolichyl phosphate D-mannose + alpha-dystroglycan
dolichyl phosphate + O-D-mannosyl-[alpha-dystroglycan]
-
in vitro asssay with both enzyme isoforms (RT and TW), 20 mM Tris, pH 8.0, mercaptoethanol, EDTA, n-octyl-beta-D-thioglucoside, sugar donor is tritium-labeled, alpha-dystroglycan isoform C contains mucin-type domain that is target of O-mannose modifications in mammals, high grade of O-mannosylation, A isoform without noticeable O-mannosylation, rabbit alpha-dystroglycan as positive control shows lower O-mannosylation
-
-
?
dolichyl phosphate D-mannose + glucoamylase I
dolichyl phosphate + O-D-mannosyl glucoamylase I
the AaPmtA protein is involved in the formation of the normal cell wall. AaPmtA protein is responsible for the transfer of mannose to glucoamylase I
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
dolichyl phosphate D-mannose + protein AN5660
dolichyl phosphate + O-D-mannosylprotein
the un-glycosylated 32 kDa protein is an ortholog of Wsc family proteins in Saccharomyces cerevisiae, these proteins serve as sensors of stress, such as high temperature and cell wall-perturbing chemicals
AN5660
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
additional information
?
-
dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-seryl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-seryl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
-
-
-
?
dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein]
dolichyl phosphate + 3-O-(alpha-D-mannosyl)-L-threonyl-[protein]
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
central role for Pmt4-mediated protein O-mannosylation in growth, cell wall integrity, and virulence of Cryptococcus neoformans
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
catalyzes the initial step of O-mannosyl glycan biosynthesis
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
role of O-glycosylation in the control of folding of secretory proteins in the endoplasmic reticulum
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
-
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
acceptor substrate specificities of PMT1-4,6
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
acceptor substrates: secretory proteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
production of cell-wall mannoproteins
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential. ogm4D mutants differ morphologically from wild type and exhibit defects in sexual agglutination
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells
-
-
?
dolichyl phosphate D-mannose + protein
dolichyl phosphate + O-D-mannosylprotein
-
protein O-mannosylation is crucial for cell wall integrity, septation and viability
-
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
i.e. small-agglutinin
-
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
activity is not affected by disruption mutations of PMT1-4
-
-
?
dolichyl phosphate D-mannose + protein Aga2
dolichyl phosphate + O-D-mannosylprotein Aga2
-
protein is located at the cell surface
-
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
-
PMT1 and PMT2, not PMT3 and PMT4
-
-
?
dolichyl phosphate D-mannose + protein Bar1
dolichyl phosphate + O-D-mannosylprotein Bar1
-
protein is located in the medium
-
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
PMT1
-
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
PMT1, PMT4, PMT6 and especially PMT2, not PMT3
-
-
?
dolichyl phosphate D-mannose + protein chitinase 1
dolichyl phosphate + O-D-mannosylprotein chitinase 1
-
protein is located in the cell wall and medium
-
-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
-
PMT4 and PMT6, not PMT1-3
-
-
?
dolichyl phosphate D-mannose + protein Ggp1/Gas1
dolichyl phosphate + O-D-mannosylprotein Ggp1/Gas1
-
protein is located at the cell surface
-
-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
-
PMT4, not PMT1-3
-
-
?
dolichyl phosphate D-mannose + protein Kex2
dolichyl phosphate + O-D-mannosylprotein Kex2
-
protein is located in the Golgi apparatus
-
-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
-
mainly PMT1 and PMT2, not PMT3 and PMT4
-
-
?
dolichyl phosphate D-mannose + protein Kre9
dolichyl phosphate + O-D-mannosylprotein Kre9
-
protein is located in the Golgi apparatus
-
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
PMT1
-
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
PMT1, PMT2, and to some extent PMT4, not PMT3
-
-
?
dolichyl phosphate D-mannose + protein Pir2/hsp150
dolichyl phosphate + O-D-mannosylprotein Pir2/hsp150
-
protein is located in the medium
-
-
?
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
-
C-mannosylation activity
-
-
?
dolichyl phosphate D-mannose + ribonuclease 2
dolichyl phosphate + ribonuclease 2-D-mannose
-
biosynthetic pathway
-
-
?
additional information
?
-
-
Afpmt1 acts as an O-mannosyltransferase. Characterization of the DELTAAfpmt1 mutant shows that a lack of AfPmt1p results in sensitivity to elevated temperature and defects in growth and cell wall integrity, thereby affecting cell morphology, conidium formation, and germination. In a mouse model, Afpmt1 is not required for the virulence of Aspergillus fumigatus
-
-
?
additional information
?
-
-
PMT2 is essential for growth
-
-
?
additional information
?
-
-
PMT4 is required for full virulence of Candida albicans
-
-
?
additional information
?
-
-
PMT5 does not make a significant contribution to virulence
-
-
?
additional information
?
-
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
protein mannosyltransferases (Pmt proteins Pmt1p, Pmt2p, Pmt4p, Pmt5p, and Pmt6p) initiate O mannosylation of secretory proteins. Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases. The importance of individual Pmt isoforms may differ in specific host niches
-
-
?
additional information
?
-
-
protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
-
-
?
additional information
?
-
O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans contributes significantly to virulence. PMT2 is essential for growth. Loss of a single PMT2 allele already sufficed to significantly retarded growth
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additional information
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O-mannosylation of specific secretory proteins of the bacterial pathogen Mycobacterium tuberculosis contributes significantly to virulence
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additional information
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although the improved secretion of the protein by suppression of O mannosylation might not be a general phenomenon, the suppression of O mannosylation could be beneficial for the production of proteins forming either homomeric or heteromeric complexes through their hydrophobic interaction in yeast
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additional information
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defective mutants are used to investigate the substrate specificities of PMT1-4,6 in vivo
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additional information
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disruption of the pmt1 gene decreased protein secretion but has no effect on glycosylation of secreted proteins. PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins
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additional information
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disruption of the pmt1 gene decreased protein secretion but has no effect on glycosylation of secreted proteins. PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins
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evolution
PMT family members are conserved throughout the fungal and animal kingdoms. They are further subdivided into the PMT1, PMT2, and PMT4 subfamilies, which include transferases closely related to Saccharomyces cerevisiae Pmt1p, Pmt2p, and Pmt4p, respectively. In fungi, at least one member of each subfamily is present, whereas in animals only PMT2 and PMT4 subfamily members are conserved. In Saccharomyces, Pmt1p, Pmt2p, and Pmt4p account for the major transferase activities although at least six PMTs (Pmt1p-Pmt6p) are present
evolution
the enzyme is a member of the protein-O-mannosyltransferase (PMT) family. Pichia pastoris has five PMT genes. Based on sequence homology, the PMTs can be grouped into three subfamilies, with both PMT1 and PMT2 subfamilies possessing two members each (PMT1 and PMT5, and PMT2 and PMT6, respectively). The remaining subfamily, PMT4, has only one member, PMT4. PMT1 and PMT2 each play a significant role in O-glycosylation
evolution
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the enzyme is a member of the protein-O-mannosyltransferase (PMT) family. Pichia pastoris has five PMT genes. Based on sequence homology, the PMTs can be grouped into three subfamilies, with both PMT1 and PMT2 subfamilies possessing two members each (PMT1 and PMT5, and PMT2 and PMT6, respectively). The remaining subfamily, PMT4, has only one member, PMT4. PMT1 and PMT2 each play a significant role in O-glycosylation
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malfunction
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AnpmtA + AnpmtB double disruptant is viable but slow growing with morphological characteristics cumulative of single disruptants
malfunction
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AnpmtA + AnpmtB double disruptant is viable but slow growing with morphological characteristics cumulative of single disruptants, hyperglycosylation of specific target proteins
malfunction
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AnpmtB disruptant shows wild-type colony formation at 30°C, slightly repressed growth at 42°C, conidiation reduced to about 50%, hyperbranching of hyphae (defect in polarity maintenance)
malfunction
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defects in O-mannosylation are associated with muscular dystrophies (dystroglycanopathies)
malfunction
dystroglycanopathies (muscular dystrophy due to abnormal glycosylation of alpha-dystroglycan) such as the severe Walker-Warburg syndrome (brain and eye abnormalities, mild limb girdle muscular dystrophy)
malfunction
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loss of the O-mannosyltransferase is associated with a reduced formation frequency of the invasive structure, the appressorium, combined with a loss in the ability to penetrate the plant cuticle
malfunction
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mutation in either one of the complex forming enzymes can lead to Walker-Warburg syndrome, a congenital muscular dystrophy with abnormal neuronal migration
malfunction
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pmt4 deletion mutant with strong reduction in appressorium formation, the few formed appressoria lack the capacity to penetrate the plant cuticle, reduced pathogenicity, no effects on vegetative growth or mating, normal polar growth of infectious hyphae
malfunction
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pmtC disruptant with highest growth repression, swollen, frequently branched hyphae, no conidia formation, recovery of hyphal structures in the presence of osmotic stabilizers, enables conidiophore and conidia production (abnormal and fewer) at 42°C
malfunction
single enzyme deletion mutants are viable, at elevated temperatures they show cell wall-associated defects and increased sensitivity to cell wall-perturbing agents, and defects in developmental patterning, partial restoration of wild-type growth with the osmotic sorbitol
malfunction
virulence of the human fungal pathogen causing meningoencephalitis depends on extracellular factors including the O-glycosylation of proteins
malfunction
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virulence of the human fungal pathogen causing meningoencephalitis depends on extracellular factors including the O-glycosylation of proteins
malfunction
PMT2 knockout, and to a lesser extent a PMT1 knockout, in addition to a reduction in O-glycan site occupancy also leads to shortened O-glycan chain lengths
malfunction
the lack of C-terminal Pmt1 MIR-containing region affects transcriptomes, altering the transcription of genes involved in asexual development, e.g. transcription patterns of seven conidiation-associated genes flbA-flbD, fluG, hyd1, and hyd2. Loss of the enzyme's C-terminal Pmt1 MIR-containing region affects mannosylation of the cell wall proteins. The Pmt1DELTA311-902 cells show significant increases in lectin binding when probed with either the ConA or the JAL lectins as compared with the wild-type strain. Increased binding of the WGA lectin is also detected or Pmt1delta311-902 cells, but no obvious difference in reactivity with GNL between the wild-type and Pmt1delta311-902 cells. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion. Phenotypes, overview. Hyphal bodies isolated from insects infected with Pmt1DELTA311-902 cells are elongated and significantly longer than their wild-type counterparts. In addition, hyphal branching is seen in numerous cells, a phenomenon rarely detected in wild-type (and complemented strain) samples
malfunction
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PMT2 knockout, and to a lesser extent a PMT1 knockout, in addition to a reduction in O-glycan site occupancy also leads to shortened O-glycan chain lengths
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malfunction
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the lack of C-terminal Pmt1 MIR-containing region affects transcriptomes, altering the transcription of genes involved in asexual development, e.g. transcription patterns of seven conidiation-associated genes flbA-flbD, fluG, hyd1, and hyd2. Loss of the enzyme's C-terminal Pmt1 MIR-containing region affects mannosylation of the cell wall proteins. The Pmt1DELTA311-902 cells show significant increases in lectin binding when probed with either the ConA or the JAL lectins as compared with the wild-type strain. Increased binding of the WGA lectin is also detected or Pmt1delta311-902 cells, but no obvious difference in reactivity with GNL between the wild-type and Pmt1delta311-902 cells. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion. Phenotypes, overview. Hyphal bodies isolated from insects infected with Pmt1DELTA311-902 cells are elongated and significantly longer than their wild-type counterparts. In addition, hyphal branching is seen in numerous cells, a phenomenon rarely detected in wild-type (and complemented strain) samples
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metabolism
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a complex of protein O-mannosyltransferase 1 and 2 catalyzes the initial step of O-mannosyl glycan biosynthesis
metabolism
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isoforms POMT1 and POMT2 catalyze the initial step of O-mannosyl glycan biosynthesis
metabolism
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protein O-mannosyltransferase 1 (POMT1) and its homolog, POMT2, are responsible for the catalysis of the first step in O-mannosyl glycan synthesis
physiological function
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AnpmtB, hyphal development and differentiation, polarity maintenance
physiological function
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AnpmtC, hyphal development and differentiation, maintenance of cell wall integrity
physiological function
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fungal morphology and conidia formation
physiological function
O-glycosylation of proteins
physiological function
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O-glycosylation of proteins
physiological function
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O-mannosylation can modulate the ligand-binding activity of alpha-dystroglycan
physiological function
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O-mannosylation is essential for virulence of the fungus
physiological function
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pmt4 is important for pathogenesis (appressorium formation and penetration)
physiological function
role in cell wall integrity pathway and developmental patterning by providing spatial cues
physiological function
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the Pmt1p-Pmt2p complex participates in endoplasmic reticulum protein quality control. The Pmt1p-Pmt2p complex is required for the fast endoplasmic reticulum exit of wild-type substrate Gas1p
physiological function
Dol-P-beta-Man:protein alpha-mannosyltransferases are initiating the essential protein O-mannosylation of secretory and membrane proteins in the endoplasmic reticulum. Pmt1p-loop1 is crucial for cross-linking of the photoreactive peptide
physiological function
protein O-mannosylation in fungi is initiated at the endoplasmic reticulum by a family of protein-O-mannosyltransferases that transfer mannose from dolichyl phosphate-activated mannose to serine or threonine residues of proteins entering the endoplasmic reticulum
physiological function
the C-terminal Pmt1 MIR-containing region affects transcriptomes. Requirement of the C-terminal Pmt1 MIR containing region on Pmt1 O-mannosyltransferase enzyme activity in vivo. The C-terminal MIR-containing domain of Pmt1 is involved in cell wall integrity, cell surface characteristics, and cell adhesion. But the Pmt1 C-terminus domain containing the MIR motifs is dispensable for fungal virulence
physiological function
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protein O-mannosylation in fungi is initiated at the endoplasmic reticulum by a family of protein-O-mannosyltransferases that transfer mannose from dolichyl phosphate-activated mannose to serine or threonine residues of proteins entering the endoplasmic reticulum
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physiological function
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the C-terminal Pmt1 MIR-containing region affects transcriptomes. Requirement of the C-terminal Pmt1 MIR containing region on Pmt1 O-mannosyltransferase enzyme activity in vivo. The C-terminal MIR-containing domain of Pmt1 is involved in cell wall integrity, cell surface characteristics, and cell adhesion. But the Pmt1 C-terminus domain containing the MIR motifs is dispensable for fungal virulence
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additional information
cell wall composition of wild-type strain and the Pmt1DELTA311-902 mutant strain, overview
additional information
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cell wall composition of wild-type strain and the Pmt1DELTA311-902 mutant strain, overview
additional information
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cell wall composition of wild-type strain and the Pmt1DELTA311-902 mutant strain, overview
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yes
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mutants lacking or overexpressing one of the two or both O-mannosyltransferases Rotated Abdomen and Twisted show that both are required for in vivo production of high molecular mass dystroglycan, overexpression of only one isoform does not increase its amount over wild-type, lack of either one of the isoforms or both isoforms lacking double mutant do not produce the high molecular mass dystroglycan
D77A
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the PMT1 mutant shows 71.95% activity compared to the wild type enzyme
D77A/E78A/D92A/E93A
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the PMT1/PMT2 mutant shows 0.24% activity compared to the wild type enzyme
D80A
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the PMT4 mutant shows 3.21% activity compared to the wild type enzyme
D80E
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the PMT4 mutant shows 52.98% activity compared to the wild type enzyme
D80E/E81D
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the PMT4 mutant shows 116.54% activity compared to the wild type enzyme
D92A/E93A
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the PMT2 mutant shows 3.63% activity compared to the wild type enzyme
D96A
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the PMT1 mutant shows 63.21% activity compared to the wild type enzyme
E78A
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the PMT1 mutant shows 46.68% activity compared to the wild type enzyme
E81A
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the PMT4 mutant shows 1.43% activity compared to the wild type enzyme
E81D
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the PMT4 mutant shows 46.59% activity compared to the wild type enzyme
E86A
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the mutant shows about 70% activity compared to the wild type enzyme
F76A
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the PMT1 mutant shows 78.79% activity compared to the wild type enzyme
F81A
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the PMT1 mutant shows 71.71% activity compared to the wild type enzyme
H80A
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the PMT1 mutant shows 83.03% activity compared to the wild type enzyme
H98A
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the PMT1 mutant shows 62.77% activity compared to the wild type enzyme
L171A
stable enzyme with reduced activity causing phenotype limb girdle muscular dystrophy 2K, together with partial heterozygous deletion p.A589VfsX38 mutant, reduced amounts of O-mannosyl linked glyco-epitope (IIH6) on alpha-dystroglycans resulting in less than 100-125 kDa alpha-dystroglycans, about 40% residual enzyme activity
N330Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N98Q/N330Q/N445Q/N528Q/N583Q
P100A
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the PMT1 mutant shows 59.67% activity compared to the wild type enzyme
P99A
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the PMT1 mutant shows 61.77% activity compared to the wild type enzyme
R145A
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the mutant shows about 130% activity compared to the wild type enzyme
R30A
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the mutant shows less than 10% activity compared to the wild type enzyme
R72A
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the mutant shows about 65% activity compared to the wild type enzyme
V97A
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the PMT1 mutant shows 80.23% activity compared to the wild type enzyme
Y88A
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the PMT1 mutant shows 73.79% activity compared to the wild type enzyme
D96A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
E78A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
H346A/H348A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
H411A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
H472A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
K234A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
L399A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
L408A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
L408A/H411A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
N370A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
Q359A/Q360A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
Q493A/E495A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
R138A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
R398A
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site-directed mutagenesis, exchange of conserved residue in the central loop, reduced activity
R469A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
R64 A
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site-directed mutagenesis, exchange of conserved residue in the central loop, highly reduced activity
W253A
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site-directed mutagenesis, exchange of conserved residue in the central loop, slightly reduced activity
D77A/E78A
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the PMT1 mutant shows 0.19% activity compared to the wild type enzyme
D77A/E78A
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the PMT1 mutant shows 3.59% activity compared to the wild type enzyme
N16Q
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not smaller than wild-type, may be too close to membrane for a glycosylation site, single mutation with about 70% of wild-type activity
N16Q
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the mutant shows a lower enzymatic activity to about 70% of wild type
N16Q/N435Q/N471Q/N539Q
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together with POMT2 mutant N98Q/N330Q/N445Q/N528Q/N583Q, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
N16Q/N435Q/N471Q/N539Q
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together with wild-type POMT2, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
N435Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with about 70% of wild-type activity
N435Q
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the mutant shows about wild type activity
N435Q
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the mutant shows a lower enzymatic activity to about 70% of wild type
N445Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N445Q
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the mutant shows about wild type activity
N471Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with about 70% of wild-type activity
N471Q
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the mutant shows a lower enzymatic activity to about 70% of wild type
N528Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N528Q
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the mutant shows about wild type activity
N539Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N539Q
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the mutant shows about wild type activity
N583Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with no effect on activity
N583Q
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the mutant shows about wild type activity
N98Q
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2-3 kDa smaller than wild-type corresponding to single N-glycan chain, single mutation with about 50% of wild-type activity
N98Q
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the mutant shows a lower enzymatic activity to about 50% of wild type
N98Q/N330Q/N445Q/N528Q/N583Q
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together with POMT1 mutant N16Q/N435Q/N471Q/N539Q, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
N98Q/N330Q/N445Q/N528Q/N583Q
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together with wild-type POMT1, significantly lower activity than double wild-type, a lack of glycosylation prevents solubilization
additional information
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enzyme disruption mutant, 6% of wild-type activity, underglycosylation of an extracellular glucoamylase. Disruption mutant shows abnormal cell morphology and alteration in carbohydrate composition, reduction n the skeletal polysaccharides in the cell wall
additional information
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Anpmta + AnpmtB double disruptant is viable but very slow growing with morphological characteristics (swollen hyphae with ballon structures + hyperbranched hyphae) cumulative of single disruptants at 30 and 42°C, partial improvement of defects by addition of osmotic stabilizer
additional information
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AnpmtA disruptant, increased sensitivity to hygromycin B (increased cell wall permeability), glycoprotetin profile (plasma membrane proteins) almost indistinguishable from wild-type, underglycosylation of protein AN5660 upon AnpmtC diruption
additional information
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AnPmtB disruptant shows wild-type colony formation at 30°C, slightly repressed growth at 42°C, the osmotic stabilizer 0.6 M KCl reduces these effects, conidiation reduced to about 56%, swollen vesicles, hyperbranching of hyphae (defect in polarity maintenance), underglycosylation of glucoamylase I upon gene disruption, higher sensitivity to inhibitors of cell wall synthesis (beta-glucan and beta-1,3-glucan production) congo red and micafungin, not to calcofluor (inhibiting chitin synthesis), no increased sensitivity to hygromycin B, glycoproetin profile (plasma membrane proteins) almost indistinguishable from wild-type, underglycosylation of glucoamylase I upon AnpmtB diruption
additional information
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AnpmtC disruptant with highest growth repression, swollen, frequently branched hyphae, strongly reduced conidia formation (6% of wild-type), recovery of hyphal structures in the presence of osmotic stabilizers (0.6 M KCl, 0.8 M NaCl, or 1.2 M sorbitol) at 42°C, enables conidiophore and conidia production (abnormal and fewer), underglycosylation of glucoamylase I upon gene diruption, higher sensitivity to inhibitors of cell wall synthesis (beta-glucan and beta-1,3-glucan production) congo red and micafungin, not to calcofluor (inhibiting chitin synthesis), more sensitive to hygromycin B than wild-type, increase of 65 kDa proteins, of mannose-containing glycoproteins (plasma membrane proteins) of about 80 kDa, reduced number of proteins larger than 100 kDa and of 75 kDa, underglycosylation of glucoamylase I and of protein AN5660 upon AnpmtC diruption
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol, the pmtA deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except double deletion mutant deltapmtA + deltapmtB, swollen conidia, partial or no conidiogenous layers, at 42°C 2 to 3times swollen conidia, no germ tubes, fewer conidia
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol, the pmtA deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except double deletion mutant deltapmtA + deltapmtB, swollen conidia, partial or no conidiogenous layers, at 42°C 2 to 3times swollen conidia, no germ tubes, fewer conidia
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol, the pmtA deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except double deletion mutant deltapmtA + deltapmtB, swollen conidia, partial or no conidiogenous layers, at 42°C 2 to 3times swollen conidia, no germ tubes, fewer conidia
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the deltapmtC deletion mutant is resistant to Calcofluor at all temperatures but sensitive to Congo red at elevated temperatures, at 30°C more multiple germ tubes than in the wild-type and in the other deletion mutants, excessive aerial hyphae, fewer conidiophores on elongated stalks, condigiogenous layers misplaced, at 37°C vesicles and conidiogenous layers swollen, fewer spores at all temperatures at 42°C swollen germ tubes and hyperbranching
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the deltapmtC deletion mutant is resistant to Calcofluor at all temperatures but sensitive to Congo red at elevated temperatures, at 30°C more multiple germ tubes than in the wild-type and in the other deletion mutants, excessive aerial hyphae, fewer conidiophores on elongated stalks, condigiogenous layers misplaced, at 37°C vesicles and conidiogenous layers swollen, fewer spores at all temperatures at 42°C swollen germ tubes and hyperbranching
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, deltapmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the deltapmtC deletion mutant is resistant to Calcofluor at all temperatures but sensitive to Congo red at elevated temperatures, at 30°C more multiple germ tubes than in the wild-type and in the other deletion mutants, excessive aerial hyphae, fewer conidiophores on elongated stalks, condigiogenous layers misplaced, at 37°C vesicles and conidiogenous layers swollen, fewer spores at all temperatures at 42°C swollen germ tubes and hyperbranching
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), pmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl, at 25°C the pmtB deletion mutant grows as well as the wild-type in the presence of cell wall-perturbing agents, at 30 and 37°C it is hypersensitive to Calcofluor, at 42°C it is resistant to Calcofluor, to Congo red it is hypersensitive at 37 and 42°C, resistant at lower temperatures, at 42°C lysis of 30% of hyphen tips, at permissive temperature mostly normal conidiophores, occasional lysed vesicles, at restrictive temperature many swollen conidiophore stalks and lysed vesicles, fewer conidia, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), pmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl, at 25°C the pmtB deletion mutant grows as well as the wild-type in the presence of cell wall-perturbing agents, at 30 and 37°C it is hypersensitive to Calcofluor, at 42°C it is resistant to Calcofluor, to Congo red it is hypersensitive at 37 and 42°C, resistant at lower temperatures, at 42°C lysis of 30% of hyphen tips, at permissive temperature mostly normal conidiophores, occasional lysed vesicles, at restrictive temperature many swollen conidiophore stalks and lysed vesicles, fewer conidia, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
at 25 and 30°C normal growth of single deletion mutants, reduced growth at high temperatures (37 and 42°C), pmtA deletion mutant is more heat sensitive than deltapmtC and deltapmtB, double deletion mutant deltapmtA + deltapmtB is the most heat sensitive, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl, at 25°C the pmtB deletion mutant grows as well as the wild-type in the presence of cell wall-perturbing agents, at 30 and 37°C it is hypersensitive to Calcofluor, at 42°C it is resistant to Calcofluor, to Congo red it is hypersensitive at 37 and 42°C, resistant at lower temperatures, at 42°C lysis of 30% of hyphen tips, at permissive temperature mostly normal conidiophores, occasional lysed vesicles, at restrictive temperature many swollen conidiophore stalks and lysed vesicles, fewer conidia, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
double deletion mutant of pmtA + pmtB is the only viable double mutant, it shows slightly retarded growth even at 25°C and is the most heat sensitive deletion mutant, followed in sensitivity by deltapmtA, deltapmtC, and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the double deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type at all tested temperatures, at 25°C swollen conidiophore stalks, vesicles, and conidiogenous layers, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except deltapmtA, lysis of hyphen tips at permissive temperature, at 37°C vegetative and aerial hyphae badly swollen, conidiophores not detectable, reduced conidia productiondefective polar growth at restrictive temperature, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
double deletion mutant of pmtA + pmtB is the only viable double mutant, it shows slightly retarded growth even at 25°C and is the most heat sensitive deletion mutant, followed in sensitivity by deltapmtA, deltapmtC, and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the double deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type at all tested temperatures, at 25°C swollen conidiophore stalks, vesicles, and conidiogenous layers, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except deltapmtA, lysis of hyphen tips at permissive temperature, at 37°C vegetative and aerial hyphae badly swollen, conidiophores not detectable, reduced conidia productiondefective polar growth at restrictive temperature, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
double deletion mutant of pmtA + pmtB is the only viable double mutant, it shows slightly retarded growth even at 25°C and is the most heat sensitive deletion mutant, followed in sensitivity by deltapmtA, deltapmtC, and deltapmtB, partial restoration of heat tolerance by addition of the osmotic sorbitol or KCl (not conidial production), the double deletion mutant is more sensitive to cell wall-perturbing agents Calcofluor and Congo red than the wild-type at all tested temperatures, at 25°C swollen conidiophore stalks, vesicles, and conidiogenous layers, at 30°C more germ tubes emerge early compared to wild-type and the other deletion mutants except deltapmtA, lysis of hyphen tips at permissive temperature, at 37°C vegetative and aerial hyphae badly swollen, conidiophores not detectable, reduced conidia productiondefective polar growth at restrictive temperature, at 30°C hyphae are growing from adjacent compartments into lysed areas forming intrahyphal hyphae
additional information
double deletion mutant of pmtB + pmtC is not viable
additional information
double deletion mutant of pmtB + pmtC is not viable
additional information
double deletion mutant of pmtB + pmtC is not viable
additional information
double deletion mutants of pmtA + pmtC is not viable
additional information
double deletion mutants of pmtA + pmtC is not viable
additional information
double deletion mutants of pmtA + pmtC is not viable
additional information
the triple deletion mutant of pmtA + pmtB + pmtC is not viable
additional information
the triple deletion mutant of pmtA + pmtB + pmtC is not viable
additional information
the triple deletion mutant of pmtA + pmtB + pmtC is not viable
additional information
generation of a truncated mutant lacking the C-terminal Pmt1 MIR-containing region (Pmt1DELTA311-902) by targeted gene replacement and construction of the C-terminal Pmt1 MIR-containing region deletion strains and complementation strains. Construction and analysis of the C-terminal Pmt1 MIR-containing region-affected transcriptomes. Complementation by expression of wild-type enzyme. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion, phenotypes, overview
additional information
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generation of a truncated mutant lacking the C-terminal Pmt1 MIR-containing region (Pmt1DELTA311-902) by targeted gene replacement and construction of the C-terminal Pmt1 MIR-containing region deletion strains and complementation strains. Construction and analysis of the C-terminal Pmt1 MIR-containing region-affected transcriptomes. Complementation by expression of wild-type enzyme. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion, phenotypes, overview
additional information
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generation of a truncated mutant lacking the C-terminal Pmt1 MIR-containing region (Pmt1DELTA311-902) by targeted gene replacement and construction of the C-terminal Pmt1 MIR-containing region deletion strains and complementation strains. Construction and analysis of the C-terminal Pmt1 MIR-containing region-affected transcriptomes. Complementation by expression of wild-type enzyme. The mutant shows altered conidial yield, conidial germination, hydrophobicity and adhesion, phenotypes, overview
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additional information
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disruption after amino acid D439 results in pmt1A lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, pmt1A mutant is susceptible to sorbitol (2.5 M) and to 0.1% SDS, reduced survival upon macrophage attack
additional information
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disruption after amino acid E468 results in pmt2A lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability, may be due to interaction with the other isoforms
additional information
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disruption after amino acid K461 results in pmt4A lacking mutants, viable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4A mutant is susceptible to sorbitol (2 M), reduced survival upon macrophage attack
additional information
disruption after amino acid N508 results in pmt2D lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability may be due to interaction with the other isoforms
additional information
disruption after amino acid N508 results in pmt2D lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability may be due to interaction with the other isoforms
additional information
disruption after amino acid N508 results in pmt2D lacking mutants, not viable, one wild-type allele is necessary for growth, after sporulation no haploid pmt2 lacking mutants are found, Pmt2 is essential but an intact Pmt2 gene lacking the other two isoforms is not sufficient for viability may be due to interaction with the other isoforms
additional information
disruption after amino acid Q412 results in pmt4D lacking mutants, aviable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4D strain is not inhibited by sorbitol but is inhibited by SDS, bilateral crossing of two pmt4D mutant strains delays mating reaction with reduced filament formation, less aerial hyphae, irregular shape and thickness of filaments with swollen distal tips
additional information
disruption after amino acid Q412 results in pmt4D lacking mutants, aviable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4D strain is not inhibited by sorbitol but is inhibited by SDS, bilateral crossing of two pmt4D mutant strains delays mating reaction with reduced filament formation, less aerial hyphae, irregular shape and thickness of filaments with swollen distal tips
additional information
disruption after amino acid Q412 results in pmt4D lacking mutants, aviable but with distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, poor growth on high salt medium, abnormal septum formation, enlarged cells subject to spontaneous lysis, multi-cell aggregate formation based on defects in cell separation, delayed melanin production, slightly reduced capsule size, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, points to necessary interaction with the Pmt2 isoform or essential combined target, the pmt4D strain is not inhibited by sorbitol but is inhibited by SDS, bilateral crossing of two pmt4D mutant strains delays mating reaction with reduced filament formation, less aerial hyphae, irregular shape and thickness of filaments with swollen distal tips
additional information
disruption after amino acid W315 results in pmt1D lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, the pmt1D mutant grows poorly in sorbitol, is unaffected by SDS, no defects in mating and crossing are observed
additional information
disruption after amino acid W315 results in pmt1D lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, the pmt1D mutant grows poorly in sorbitol, is unaffected by SDS, no defects in mating and crossing are observed
additional information
disruption after amino acid W315 results in pmt1D lacking mutants are viable but show distinct defects in cell morphology and cell integrity (wild-type comparable growth at 30°C, reduced growth at 37°C, no growth at 39°C in contrast to wild-type, more susceptible to SDS medium, enlarged cells subject to spontaneous lysis, attenuated virulence), Pmt1/Pmt4 double mutants are not viable, the pmt1D mutant grows poorly in sorbitol, is unaffected by SDS, no defects in mating and crossing are observed
additional information
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mutants lacking or overexpressing one of the two or both O-mannosyltransferases Rotated Abdomen and Twisted show that both are required for in vivo production of high molecular mass dystroglycan, overexpression of only one isoform does not increase its amount over wild-type, lack of either one of the isoforms or both isoforms lacking double mutant do not produce the high molecular mass dystroglycan
additional information
heterozygous deletion leading to a frame shift mutation causing an amino acid exchange A589V and a premature stop codon after 38 amino acids (p.A589VfsX38), reduced enzyme stability, reduced amounts of O-mannosyl linked glyco-epitope (IIH6) on alpha-dystroglycans resulting in less than 100-125 kDa alpha-dystroglycans, about 40% residual enzyme activity, phenotype limb girdle muscular dystrophy 2K
additional information
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heterozygous deletion leading to a frame shift mutation causing an amino acid exchange A589V and a premature stop codon after 38 amino acids (p.A589VfsX38), reduced enzyme stability, reduced amounts of O-mannosyl linked glyco-epitope (IIH6) on alpha-dystroglycans resulting in less than 100-125 kDa alpha-dystroglycans, about 40% residual enzyme activity, phenotype limb girdle muscular dystrophy 2K
additional information
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single site mutations defective in potential glycosylation sites do not change enzyme activity, mutaions of all such sites cause a loss of enzyme activity, probably due to decreased hydrophilicity
additional information
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single site mutations defective in potential glycosylation sites do not change enzyme activity, mutations of all such sites cause a loss of enzyme activity, probably du to decreased hydrophilicity
additional information
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mutations of all N-glycosylation sites of either isoform POMT1 or POMT2 cause a loss of enzyme activity
additional information
construction of Pichia pastoris single and all PMT knockout mutant strains, the DELTApmt1 and DELTApmt2 strains secrete protein with significantly reduced O-glycan site occupancy
additional information
construction of Pichia pastoris single and all PMT knockout mutant strains, the DELTApmt1 and DELTApmt2 strains secrete protein with significantly reduced O-glycan site occupancy
additional information
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construction of Pichia pastoris single and all PMT knockout mutant strains, the DELTApmt1 and DELTApmt2 strains secrete protein with significantly reduced O-glycan site occupancy
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additional information
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construction of diverse deletion mutants of PMT1, effect on activity and complex formation with PMT2, overview
additional information
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homozygous diploid double disruption mutants of PMT1 and PMT2 lead to reduced enzyme activity and a severe defect in sporulation, lethal phenotype when combined with a disruption mutation in dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130, genes
additional information
homozygous diploid double disruption mutants of PMT1 and PMT2 lead to reduced enzyme activity and a severe defect in sporulation, lethal phenotype when combined with a disruption mutation in dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130, genes
additional information
homozygous diploid double disruption mutants of PMT1 and PMT2 lead to reduced enzyme activity and a severe defect in sporulation, lethal phenotype when combined with a disruption mutation in dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase, EC 2.4.1.130, genes
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
construction of all single, double and triple mutants of the genes PMT1-4 by gene disruption and crosses, characterization concerning growth, morphology, and their sensitivity to killer toxin K1, sorbitol dependence, caffeine and calcofluor white, overview
additional information
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PMT1 null mutant shows increased heat lability, alpa-D-mannose transfer only to serine residue of the substrate peptide Ac-YNPTSV-NH2, not to threonine and valine like with the wild-type
additional information
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PMT2 disruption mutant shows reduced in vitro and in vivo activity
additional information
PMT2 disruption mutant shows reduced in vitro and in vivo activity
additional information
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PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme
additional information
PMT1 and PMT2 double disruption mutant shows severe growth defect but retain residual activity due to an additional enzyme
additional information
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PMT3 and 4 gene disruption does not alter enzyme activity
additional information
PMT3 and 4 gene disruption does not alter enzyme activity
additional information
PMT3 and 4 gene disruption does not alter enzyme activity
additional information
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construction of defective mutants of PMT1-4,6, determination of substrate specificities
additional information
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PMT2 haploid mutants grow slightly slower than the wild-type, the enzyme is required but not essential for normal vegetative growth of the cells
additional information
PMT2 haploid mutants grow slightly slower than the wild-type, the enzyme is required but not essential for normal vegetative growth of the cells
additional information
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complementation studies with Schizosaccharomyces pombe deletion mutants show that pmt1 is a functional homolog
additional information
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complementation studies with Schizosaccharomyces pombe deletion mutants show that pmt4 is a functional homolog
additional information
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deletion mutants show reduced virulence
additional information
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pmt2 deletion mutants are not viable
additional information
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pmt4 and pmt1 and double deletion mutants are viable with normal growth rates and mating, normal disease symptoms are developed in infected Zea mays
additional information
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the single deletion mutant of pmt1 is viable with normal growth rates and mating, causes disease development in Zea may comparable to wild-type, no increased sensitivity to antifungal substances such as congo red, chlorpromazine, calcofluor white, and caffein or to thermal stress (34 and 36°C), oxidative stress (H2O2), osmotic stress (SDS and sorbitol), or salt-based stress (NaCl, CaCl2)
additional information
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the single deletion mutant of pmt4 is viable with normal growth rates and mating, causes no disease symptoms in Zea mays, not even in plants infected via the stigma, no increased sensitivity to antifungal substances such as congo red, chlorpromazine, calcofluor white, and caffein or to thermal stress (34 and 36°C), to oxidative stress (H2O2), to osmotic stress by sorbitol but to SDS, or to salt-based stress (NaCl, CaCl2), no changed activity of secreted hydrolytic enzymes (cellulase, pectinase, amylase activity), normal filament formation but lower appressorium formation and aberrant appressorium formation, hyphae are built close to the plant surface but do not intrude the epidermal cell layer, inhibition of the defensive plant reactive oxygen species formation does not restore virulence
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Lommel, M.; Willer, T.; Strahl, S.
POMT2, a key enzyme in Walker-Warburg syndrome: somatic sPOMT2, but not testis-specific tPOMT2, is crucial for mannosyltransferase activity in vivo
Glycobiology
18
615-625
2008
Bos taurus, Canis lupus familiaris, Equus caballus, Felis catus, Mus musculus
brenda
Haines, N.; Seabrooke, S.; Stewart, B.A.
Dystroglycan and protein O-mannosyltransferases 1 and 2 are required to maintain integrity of Drosophila larval muscles
Mol. Biol. Cell
18
4721-4730
2007
Drosophila sp. (in: flies)
brenda
Manya, H.; Bouchet, C.; Yanagisawa, A.; Vuillaumier-Barrot, S.; Quijano-Roy, S.; Suzuki, Y.; Maugenre, S.; Richard, P.; Inazu, T.; Merlini, L.; Romero, N.B.; Leturcq, F.; Bezier, I.; Topaloglu, H.; Estournet, B.; Seta, N.; Endo, T.; Guicheney, P.
Protein O-mannosyltransferase activities in lymphoblasts from patients with alpha-dystroglycanopathies
Neuromuscul. Disord.
18
45-51
2008
Homo sapiens (Q9UKY4), Homo sapiens (Q9Y6A1), Homo sapiens
brenda
Messina, S.; Mora, M.; Pegoraro, E.; Pini, A.; Mongini, T.; DAmico, A.; Pane, M.; Aiello, C.; Bruno, C.; Biancheri, R.; Berardinelli, A.; Boito, C.; Farina, L.; Morandi, L.; Moroni, I.; Pezzani, R.; Pichiecchio, A.; Ricci, E.; Ruggieri, A.; Saredi, S.; Scuderi, C.; Tessa, A.; Toscano, A.; Tortorella G; Trevisan C.P.; Uggetti C.; Santorelli F.M.; Bertini E.; Mercuri E.
POMT1 and POMT2 mutations in CMD patients: a multicentric Italian study
Neuromuscul. Disord.
18
565-571
2008
Homo sapiens (Q9UKY4), Homo sapiens (Q9Y6A1), Homo sapiens
brenda
Snoei, J.; Urbach, H.; Engels, G.; Fassunke, J.; von Lehe, M.; Becker, A.J.; Majores, M.
Genetic alterations of protein-o-mannosyltransferase-1 in glioneuronal and glial brain tumors with subarachnoid spread
Neuropathology
29
116-124
2009
Homo sapiens (Q9Y6A1), Homo sapiens
brenda
Goto, M.; Harada, Y.; Oka, T.; Matsumoto, S.; Takegawa, K.; Furukawa, K.
Protein O-mannosyltransferases B and C support hyphal development and differentiation in Aspergillus nidulans
Eukaryot. Cell
8
1465-1474
2009
Aspergillus nidulans
brenda
Kriangkripipat, T.; Momany, M.
Aspergillus nidulans protein O-mannosyltransferases play roles in cell wall integrity and developmental patterning
Eukaryot. Cell
8
1475-1485
2009
Aspergillus nidulans (Q5B3W9), Aspergillus nidulans (Q5BDC1), Aspergillus nidulans (Q96WN5)
brenda
Nakamura, N.; Stalnaker, S.H.; Lyalin, D.; Lavrova, O.; Wells, L.; Panin, V.M.
Drosophila Dystroglycan is a target of O-mannosyltransferase activity of two protein O-mannosyltransferases, Rotated Abdomen and Twisted
Glycobiology
20
381-394
2010
Drosophila melanogaster
brenda
Manya, H.; Akasaka-Manya, K.; Nakajima, A.; Kawakita, M.; Endo, T.
Role of N-glycans in maintaining the activity of protein O-mannosyltransferases POMT1 and POMT2
J. Biochem.
147
337-344
2009
Homo sapiens
brenda
Lommel, M.; Cirak, S.; Willer, T.; Hermann, R.; Uyanik, G.; van Bokhoven, H.; Koerner, C.; Voit, T.; Bari?, I.; Hehr, U.; Strahl, S.
Correlation of enzyme activity and clinical phenotype in POMT1-associated dystroglycanopathies
Neurology
74
157-164
2010
Homo sapiens (Q9Y6A1), Homo sapiens
brenda
Fernandez-Alvarez, A.; Elias-Villalobos, A.; Ibeas, J.I.
The O-mannosyltransferase PMT4 is essential for normal appressorium formation and penetration in Ustilago maydis
Plant Cell
21
3397-3412
2009
Ustilago maydis
brenda
Fernandez-Alvarez, A.; Elias-Villalobos, A.; Ibeas, J.I.
The requirement for protein O-mannosylation for Ustilago maydis virulence seems to be linked to intrinsic aspects of the infection process rather than an altered plant response
Plant Signal. Behav.
5
412-4
2010
Ustilago maydis
brenda
Willger, S.D.; Ernst, J.F.; Alspaugh, J.A.; Lengeler, K.B.
Characterization of the PMT gene family in Cryptococcus neoformans
PLoS ONE
4
e6321
2009
Cryptococcus neoformans var. grubii, Cryptococcus neoformans var. neoformans (Q5KAF1), Cryptococcus neoformans var. neoformans (Q5KHK5), Cryptococcus neoformans var. neoformans (Q5KIZ1)
brenda
Akasaka-Manya, K.; Manya, H.; Hayashi, M.; Endo, T.
Different roles of the two components of human protein O-mannosyltransferase, POMT1 and POMT2
Biochem. Biophys. Res. Commun.
411
721-725
2011
Homo sapiens
brenda
Lommel, M.; Schott, A.; Jank, T.; Hofmann, V.; Strahl, S.
A conserved acidic motif is crucial for enzymatic activity of protein O-mannosyltransferases
J. Biol. Chem.
286
39768-39775
2011
Homo sapiens
brenda
Goder, V.; Melero, A.
Protein O-mannosyltransferases participate in ER protein quality control
J. Cell Sci.
124
144-153
2011
Saccharomyces cerevisiae
brenda
Lommel, M.; Willer, T.; Cruces, J.; Strahl, S.
POMT1 is essential for protein O-mannosylation in mammals
Methods Enzymol.
479
323-342
2010
Mus musculus
brenda
Loibl, M.; Strahl, S.
Photoaffinity labeling of protein O-mannosyltransferases of the PMT1/PMT2 subfamily
Methods Mol. Biol.
1022
107-117
2013
Saccharomyces cerevisiae (P33775), Saccharomyces cerevisiae
brenda
Nett, J.H.; Cook, W.J.; Chen, M.T.; Davidson, R.C.; Bobrowicz, P.; Kett, W.; Brevnova, E.; Potgieter, T.I.; Mellon, M.T.; Prinz, B.; Choi, B.K.; Zha, D.; Burnina, I.; Bukowski, J.T.; Du, M.; Wildt, S.; Hamilton, S.R.
Characterization of the Pichia pastoris protein-O-mannosyltransferase gene family
PLoS ONE
8
e68325
2013
Komagataella pastoris (C4QZZ6), Komagataella pastoris (C4R044), Komagataella pastoris GS115 (C4QZZ6), Komagataella pastoris GS115 (C4R044)
brenda
He, Z.; Luo, L.; Keyhani, N.O.; Yu, X.; Ying, S.; Zhang, Y.
The C-terminal MIR-containing region in the Pmt1 O-mannosyltransferase restrains sporulation and is dispensable for virulence in Beauveria bassiana
Appl. Microbiol. Biotechnol.
101
1143-1161
2017
Beauveria bassiana (J5JB66), Beauveria bassiana, Beauveria bassiana ARSEF 2860 (J5JB66)
brenda