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4 S-adenosyl-L-methionine + adenine1518/1519 in 18S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 18S rRNA
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methylation of Escherichia coli 30S ribosomes. Under assay conditions the enzyme produces both N6-methyladenine and N6-dimethyladenine, with 0.8times as much N6-methyladenine as N6-dimethyladenine
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4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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4 methyl groups are incorporated per 16S RNA molecule, both adenine residues in the 16S RNA sequence AACCUG are dimethylated
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4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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dimethylates the adenine residues in 16S rRNA-derived oligonucleotide with the specific sequence AACCUG
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4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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dimethylation of AI518 and A1519 in the hairpin loop of 16S rRNA. Site-specific mutagenesis of 16S rRNA of Escherichia coli ribosomes is used to make five mutations around the highly conserved UI512-GI523 base pair in the 3'-terminal hairpin. G1523 and C1524 in the stem are important determinants for the dimethylation of A1518 and AI519 in the loop
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4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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neither of the adenine residues is required for methylation of the other, ruling out any obligate order of methylation of A1518 and A1519. Mutation of either A1518 or A1519 to C, G or U has little effect on the ability of the mutant RNA to reconstitute a 30S ribosome containing a full complement of ribosomal proteins
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4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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recombinant KsgA is able to efficiently methylate 30S subunits isolated from strains of Escherichia coli resistant to kasugamycin, but not wild-type 30S subunits, indicating that the methylation function is specific for A1518 and A1519. KsgA is unable to utilize 30S subunits in the translationally active state as a substrate
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4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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binding of 30S subunit and S-adenosyl-L-methionine, structure, overview. After the S-adenosyl-L-methionine addition, KsgA dissociates rapidly from the subunits. The binding of KsgA to substrate is complex and requires regions of rRNA well beyond helix 45, including regions of the 790 loop
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4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
KsgA introduces the most highly conserved ribosomal RNA modification, the dimethylation of A1518 and A1519 of 16S rRNA. Methylation of 30S ribosomal subunits by Thermus thermophilus KsgA is more efficient at low concentrations of magnesium ions suggesting that partially unfolded RNA is the preferred substrate
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4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
4 S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
KsgA introduces the most highly conserved ribosomal RNA modification, the dimethylation of A1518 and A1519 of 16S rRNA. Methylation of 30S ribosomal subunits by Thermus thermophilus KsgA is more efficient at low concentrations of magnesium ions suggesting that partially unfolded RNA is the preferred substrate
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S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA
S-adenosyl-L-homocysteine + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA
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evolution
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the KsgA family belongs tothe group of S-adenosyl-L-methionine-dependent methyltransferases, known as class I MTases, KsgA is related to DNA adenosine methyltransferases, which transfer only a single methyl group to their target adenosine residue. Part of the discrimination between mono- and dimethyltransferase activity lies in a single residue in the active site, L114; this residue is part of a conserved motif, known as motif IV, which is common to a large group of S-adenosyl-L-methionine-dependent methyltransferases
malfunction
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acquisition of high-level resistance to kasugamycin at an extraordinarily high frequency, ksgA mutants display a disadvantage in overall fitness compared to the parent strain
malfunction
cold sensitivity and altered ribosomal profiles are associated with a DELTAksgA genotype in Escherichia coli
malfunction
loss of this dimethylation confers resistance to the antibiotic kasugamycin
malfunction
mutants which contain a frameshift mutation in ksgA are severely impaired for growth
malfunction
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spontaneous KSGR mutants in Neisseria gonorrhoeae arise through mutations in ksgA, which are likely to reduce KsgA activity and lead to undermethylated rRNA and thus resistance to kasugamycin
malfunction
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strains lacking the methylase are resistant to kasugamycin
malfunction
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the inability to form dimethyladenine in the 16S rRNA-derived oligonucleotide is accompanied by muatation from kasugamycin sensitivity to resistance
malfunction
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yeast enzyme Dim1 complements heterologously for ksgA- mutation in Escherichia coli, demonstrating functional equivalence of the two proteins
malfunction
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the enzyme knockout strain is sensitive to oxidative stress and has a lower survival rate in murine macrophage RAW264.7 cells than the parent strain
malfunction
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mutants which contain a frameshift mutation in ksgA are severely impaired for growth
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malfunction
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loss of this dimethylation confers resistance to the antibiotic kasugamycin
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malfunction
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the enzyme knockout strain is sensitive to oxidative stress and has a lower survival rate in murine macrophage RAW264.7 cells than the parent strain
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physiological function
KsgA acts as a ribosome biogenesis factor. KsgA alters 16S rRNA processing and has a critical role is as a supervisor of biogenesis of 30S subunits in vivo
physiological function
KsgA confers kasugamycin sensitivity to Chlamydia trachomatis and impacts bacterial fitness
physiological function
KsgA has a DNA glycosylase/AP lyase activity for C mispaired with oxidized T that prevents the formation of mutations, which is in addition to its rRNA adenine methyltransferase activity essential for ribosome biogenesis
physiological function
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KsgA, in addition to its methyltransferase activity, has another unidentified function that plays a role in the suppression of the cold-sensitive phenotype of the Era(E200K) strain. The additional function may be involved in the acid shock response
physiological function
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the KsgA methyltransferase is universally conserved and plays a key role in regulating ribosome biogenesis. KsgA has a complex reaction mechanism, transferring a total of four methyl groups onto two separate adenosine residues, A1518 and A1519, in the small subunit rRNA. This means that the active site pocket must accept both adenosine and N6-methyladenosine as substrates to catalyze formation of the final product N6,N6-dimethyladenosine
physiological function
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the enzyme contributes to maintain ribosome function under oxidative conditions and thus to Staphylococcus aureus virulence
physiological function
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the enzyme plays a role in intrinsic clarithromycin resistance and ribosome biogenesis in Mycobacterium tuberculosis
physiological function
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knockout of KsgA attenuates the killing ability against silkworms. The KsgA knockout strain is sensitive to oxidative stress and has a lower survival rate in murine macrophages than the parent strain. The KsgA knockout strain exhibits decreased translational fidelity in oxidative stress conditions. Administration of N-acetyl-L-cysteine restores the killing ability of the knockout strain against silkworms
physiological function
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KsgA confers kasugamycin sensitivity to Chlamydia trachomatis and impacts bacterial fitness
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physiological function
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the enzyme plays a role in intrinsic clarithromycin resistance and ribosome biogenesis in Mycobacterium tuberculosis
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physiological function
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the enzyme contributes to maintain ribosome function under oxidative conditions and thus to Staphylococcus aureus virulence
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physiological function
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knockout of KsgA attenuates the killing ability against silkworms. The KsgA knockout strain is sensitive to oxidative stress and has a lower survival rate in murine macrophages than the parent strain. The KsgA knockout strain exhibits decreased translational fidelity in oxidative stress conditions. Administration of N-acetyl-L-cysteine restores the killing ability of the knockout strain against silkworms
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Formenoy, L.J.; Cunningham, P.R.; Nurse, K.; Pleij, C.W.A.; Ofengand, J.
Methylation of the conserved A1518-A1519 in Escherichia coli 16S ribosomal RNA by the ksgA methyltransferase is influenced by methylations around the similarly conserved U1512-G1523 base pair in the 3' terminal hairpin
Biochimie
76
1123-1128
1994
Escherichia coli
brenda
O'Farrell, H.C.; Scarsdale, J.N.; Rife, J.P.
Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli
J. Mol. Biol.
339
337-353
2004
Escherichia coli (P06992)
brenda
Ochi, K.; Kim, J.Y.; Tanaka, Y.; Wang, G.; Masuda, K.; Nanamiya, H.; Okamoto, S.; Tokuyama, S.; Adachi, Y.; Kawamura, F.
Inactivation of KsgA, a 16S rRNA methyltransferase, causes vigorous emergence of mutants with high-level kasugamycin resistance
Antimicrob. Agents Chemother.
53
193-201
2009
Bacillus subtilis
brenda
Desai, P.M.; Rife, J.P.
The adenosine dimethyltransferase KsgA recognizes a specific conformational state of the 30S ribosomal subunit
Arch. Biochem. Biophys.
449
57-63
2006
Escherichia coli
brenda
Cunningham, P.R.; Weitzmann, C.J.; Nurse, K.; Masurel, R.; van Knippenberg, P.H.; Ofengand, J.
Site-specific mutation of the conserved m6(2)A m6(2)A residues of E. coli 16S ribosomal RNA. Effects on ribosome function and activity of the ksgA methyltransferase
Biochim. Biophys. Acta
1050
18-26
1990
Escherichia coli
brenda
Binet, R.; Maurelli, A.T.
The chlamydial functional homolog of KsgA confers kasugamycin sensitivity to Chlamydia trachomatis and impacts bacterial fitness
BMC Microbiol.
9
279
2009
Chlamydia trachomatis (B0B7S3), Chlamydia psittaci (C7EP45), Chlamydia trachomatis L2 (B0B7S3), Chlamydia psittaci 6BC (C7EP45)
brenda
van Buul, C.P.; van Knippenberg, P.H.
Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA
Gene
38
65-72
1985
Escherichia coli (P06992)
brenda
Duffin, P.M.; Seifert, H.S.
ksgA mutations confer resistance to kasugamycin in Neisseria gonorrhoeae
Int. J. Antimicrob. Agents
33
321-327
2009
Neisseria gonorrhoeae
brenda
Inoue, K.; Basu, S.; Inouye, M.
Dissection of 16S rRNA methyltransferase (KsgA) function in Escherichia coli
J. Bacteriol.
189
8510-8518
2007
Escherichia coli
brenda
Poldermans, B.; Roza, L.; van Knippenberg, P.H.
Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3' end of 16 S ribosomal RNA of Escherichia coli. III. Purification and properties of the methylating enzyme and methylase-30 S interactions
J. Biol. Chem.
254
9094-9100
1979
Escherichia coli
brenda
Lafontaine, D.; Delcour, J.; Glasser, A.L.; Desgres, J.; Vandenhaute, J.
The DIM1 gene responsible for the conserved m6(2)Am6(2)A dimethylation in the 3'-terminal loop of 18 S rRNA is essential in yeast
J. Mol. Biol.
241
492-497
1994
Escherichia coli
brenda
Demirci, H.; Belardinelli, R.; Seri, E.; Gregory, S.T.; Gualerzi, C.; Dahlberg, A.E.; Jogl, G.
Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine
J. Mol. Biol.
388
271-282
2009
Thermus thermophilus (Q5SM60), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SM60)
brenda
Andresson, O.S.; Davies, J.E.
Some properties of the ribosomal RNA methyltransferase encoded by ksgA and the polarity of ksgA transcription
Mol. Gen. Genet.
179
217-222
1980
Escherichia coli
brenda
Connolly, K.; Rife, J.P.; Culver, G.
Mechanistic insight into the ribosome biogenesis functions of the ancient protein KsgA
Mol. Microbiol.
70
1062-1075
2008
Escherichia coli (P06992)
brenda
Helser, T.L.; Davies, J.E.; Dahlberg, J.E.
Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli
Nat. New Biol.
233
12-14
1971
Escherichia coli
brenda
Helser, T.L.; Davies, J.E.; Dahlberg, J.E.
Mechanism of kasugamycin resistance in Escherichia coli
Nat. New Biol.
235
6-9
1972
Escherichia coli
brenda
Zhang-Akiyama, Q.M.; Morinaga, H.; Kikuchi, M.; Yonekura, S.; Sugiyama, H.; Yamamoto, K.; Yonei, S.
KsgA, a 16S rRNA adenine methyltransferase, has a novel DNA glycosylase/AP lyase activity to prevent mutations in Escherichia coli
Nucleic Acids Res.
37
2116-2125
2009
Escherichia coli (P06992)
brenda
O'Farrell, H.C.; Pulicherla, N.; Desai, P.M.; Rife, J.P.
Recognition of a complex substrate by the KsgA/Dim1 family of enzymes has been conserved throughout evolution
RNA
12
725-733
2006
Escherichia coli
brenda
Tu, C.; Tropea, J.E.; Austin, B.P.; Court, D.L.; Waugh, D.S.; Ji, X.
Structural basis for binding of RNA and cofactor by a KsgA methyltransferase
Structure
17
374-385
2009
Aquifex aeolicus (O67680), Aquifex aeolicus
brenda
O'Farrell, H.C.; Musayev, F.N.; Scarsdale, J.N.; Rife, J.P.
Control of substrate specificity by a single active site residue of the KsgA methyltransferase
Biochemistry
51
466-474
2012
Escherichia coli
brenda
Kyuma, T.; Kizaki, H.; Ryuno, H.; Sekimizu, K.; Kaito, C.
16S rRNA methyltransferase KsgA contributes to oxidative stress resistance and virulence in Staphylococcus aureus
Biochimie
119
166-174
2015
Staphylococcus aureus, Staphylococcus aureus RN4220
brenda
Phunpruch, S.; Warit, S.; Suksamran, R.; Billamas, P.; Jaitrong, S.; Palittapongarnpim, P.; Prammananan, T.
A role for 16S rRNA dimethyltransferase (ksgA) in intrinsic clarithromycin resistance in Mycobacterium tuberculosis
Int. J. Antimicrob. Agents
41
548-551
2013
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Kyuma, T.; Kizaki, H.; Ryuno, H.; Sekimizu, K.; Kaito, C.
16S rRNA methyltransferase KsgA contributes to oxidative stress resistance and virulence in Staphylococcus aureus
Biochimie
119
166-174
2015
Staphylococcus aureus, Staphylococcus aureus RN4220
brenda