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 (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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten steady-state kinetics analysis | Saccharomyces cerevisiae |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
66322 | - |
a heterodimeric Trm11-Trm112 complex in the presence of zinc, sequence calculation | Saccharomyces cerevisiae |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | Q12463 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | Q12463 | - |
- |
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 | 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 | Comment | Organism |
---|---|---|
? | x * 51109, His-tagged enzyme, sequence calculation | Saccharomyces cerevisiae |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | - |
Saccharomyces cerevisiae |
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 |