EC Number   |
General Information |
Reference |
|---|
   2.1.1.214 | evolution |
although the eukaryotic counterpart (Trm11) requires another subunit Trm112 for enzymatic activity, the archaeal enzyme does not require a partner subunit. Furthermore, the eukaryotic Trm11-Trm112 complex catalyzes a single methyl transfer reaction and forms only m2G10 in tRNA. The archaeal enzyme is called Trm-G10 or Trm-m22G10 to distinguish it from the eukaryotic enzyme |
-, 757106 |
| 2.1.1.214 | malfunction |
the DELTAtrm11 knockout strain grows poorly at 95°C |
-, 757106 |
| 2.1.1.214 | malfunction |
TRM112 mutant strains show growth defects, as well as nuclear genomic instability and mitotic defects, overview. Chromosome instability increases 6-7-fold in trm112-0 compared with wild-type. trm112-0 strain is resistant to zymocin, thetRNase toxin produced by Kluyveromyces lactis that specifically targets the mcm5s2U modification at position 34 and cleaves tRNAUUGGln, tRNAUUCGlu, and tRNAUUU |
712436 |
| 2.1.1.214 | malfunction |
While deletion of TRM11 has no detectable phenotype under laboratory conditions, deletion of TRM112 leads to a severe growth defect, suggesting that it has additional functions in the cell |
675961 |
| 2.1.1.214 | more |
generation of a Saccharomyces cerevisiae Trm11-Trm112 three-dimensional structure model, overview, the Trm11 region encompasses residues 1 to 406 |
-, 757844 |
| 2.1.1.214 | 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 |
-, 757844 |
| 2.1.1.214 | physiological function |
Trm11p and Trm112p are two interacting proteins that are both required for catalyzing the formation of m2G at position 10 in several tRNAs. Trm11p is the catalytic subunit, but also Trm112p is essential for the formation of m2G10, Trm112p is essential for the activity of Trm11p, another tRNA methyltransferase, because Trm112p is capable of directing the proper folding of Trm11p, leading to the synthesis of an active complex. Trm112p is required in vivo for the formation of mcm5U34 and mcm5s2U34, overview. Trm112p is also required for the activity of Mtq2p, a protein methyltransferase that catalyzes the methylation of the glutamine of the universally conserved GGQ tripeptide of the translation termination factor eRF1/Sup45. Trm112p is associated with other partners involved in ribosome biogenesis and chromatin remodeling, suggesting that it has additional roles in the cell |
712436 |
| 2.1.1.214 | physiological function |
tRNA m2G10/m2 2G10 methyltransferase (archaeal Trm11) methylates the 2-amino group in guanosine at position 10 in tRNA and forms N2,N2-dimethylguanosine (m22G10) via intermediate N2-methylguanosine (m2G10). The archaeal Trm11 is required for Thermococcus kodakarensis survival at high temperatures. The m22G10 modification might have effects on stabilization of tRNA and/or correct folding of tRNA at the high temperatures |
-, 757106 |
