In contrast to the archaeal enzyme tRNA (guanine10-N2)-dimethyltransferase (EC 18.104.22.168), tRNA (guanine10-N2)-methyltransferase from yeast does not catalyse the methylation from N2-methylguanine10 to N2-dimethylguanine10 in tRNA.
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
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
composed of at least two subunits that are associated in vivo: Trm11p (Yol124c), which is the catalytic subunit, and Trm112p (Ynr046w), a putative zinc-binding protein. 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. Trm112p is associated with at least four proteins: two tRNA methyltransferases (Trm9p and Trm11p), one putative protein methyltransferase (Mtc6p/Ydr140w), and one protein with a Rossmann fold dehydrogenase domain (Lys9p/Ynr050c)
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gene TRM112, phylogenetic analysis, expression of His-tagged Trm112p, alone or with Trm9p, in Escherichia coli strain S15 (DE3-pLysS), Trm112p forms a complex with Trm9p, which renders the latter soluble