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Literature summary for 2.1.1.214 extracted from

  • Bourgeois, G.; Marcoux, J.; Saliou, J.M.; Cianferani, S.; Graille, M.
    Activation mode of the eukaryotic m2G10 tRNA methyltransferase Trm11 by its partner protein Trm112 (2017), Nucleic Acids Res., 45, 1971-1982 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.214

Activating Compound

Activating Compound Comment Organism Structure
TRM112 dependent on, Trm11 proves to be completely inactive alone. This lack of activity cannot be attributed to protein unfolding as the circular dichroism (CD) spectrum recorded on this protein is typical of well-folded proteins containing alpha-helices and beta-strands. Trm112 stimulates SAM binding to Trm11 and contributes to tRNA binding. Analysis of the activation mode of the eukaryotic m2G10 tRNA methyltransferase Trm11 by its partner protein Trm112. Yeast Trm112 has a calculated molecular weight of 15067.6 Da. A zinc atom is attached to its Zn-binding domain. The Trm112-Trm11 interaction mode is reminiscent of the other Trm112-MTase complexes. Three-dimensional Trm11-Trm112 complex structrue analysis, and thermodynamics of interaction at 10°C, overview Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
gene YOL124c, recombinant expression of soluble C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21-Gold (DE3), coexpression of yeast Trm11 with yeast Trm112 in Escherichia coli, the holonezyme complex is active Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten steady-state kinetics analysis Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae
Zn2+ zinc might be important for Trm11 binding to Trm112, most probably by maintaining the three-dimensional structure of Trm112 zinc-binding domain, which in the other Trm112-MTase complexes is directly interacting with the MTase domains Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66322
-
 a heterodimeric Trm11-Trm112 complex in the presence of zinc, sequence calculation Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + guanine10 in tRNA Saccharomyces cerevisiae
-
 S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
-
 ?
S-adenosyl-L-methionine + guanine10 in tRNA Saccharomyces cerevisiae ATCC 204508
-
 S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q12463
-
-
Saccharomyces cerevisiae ATCC 204508 Q12463
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant soluble C-terminally His6-tagged wild-type and mutant enzymes to homogeneity from Escherichia coli strain BL21-Gold (DE3) by nickel affinity chromatography and gel filtration Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + guanine10 in tRNA
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
-
 ?
S-adenosyl-L-methionine + guanine10 in tRNA
-
 Saccharomyces cerevisiae ATCC 204508 S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
-
 ?
S-adenosyl-L-methionine + guanine10 in tRNAIle(AAU)
-
 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNAIle(AAU)
-
 ?
S-adenosyl-L-methionine + guanine10 in tRNAIle(AAU)
-
 Saccharomyces cerevisiae ATCC 204508 S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNAIle(AAU)
-
 ?

Subunits

Subunits Comment Organism
? x * 51109, His-tagged enzyme, sequence calculation Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
eukaryotic m2G10 tRNA methyltransferase
-
 Saccharomyces cerevisiae
eukaryotic Trm11
-
 Saccharomyces cerevisiae
Trm11
-
 Saccharomyces cerevisiae
tRNA MTase
-
 Saccharomyces cerevisiae
YOL124c
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information generation of a Saccharomyces cerevisiae Trm11-Trm112 three-dimensional structure model, overview, the Trm11 region encompasses residues 1 to 406 Saccharomyces cerevisiae
physiological function the enzyme is active only in complex with its partner protein Trm112, Trm11 proves to be completely inactive alone. The Trm112-Trm11 interaction mode is reminiscent of the other Trm112-MTase complexes. zinc might be important for Trm11 binding to Trm112, most probably by maintaining the three-dimensional structure of Trm112 zinc-binding domain, which in the other Trm112-MTase complexes is directly interacting with the MTase domains. Trm112 stimulates SAM binding to Trm11 and contributes to tRNA binding. Also the tRNA 3'-CCA tail from the aminoacyl stem loop for tRNA is important for methyltransferase activity Saccharomyces cerevisiae