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Post-transcriptional and post-translational modifications of factors involved in translation are very important for the control and accuracy of protein biosynthesis. Among these factors, tRNAs harbor the largest variety of grafted chemical structures, which participate in tRNA stability or mRNA decoding. Here, we focused on Trm112 protein, which associates with four different eukaryotic methyltransferases modifying tRNAs (Trm9 and Trm11) but also 18S-rRNA (Bud23) and translation termination factor eRF1 (Mtq2). In particular, we have investigated the role of Trm112 in the Trm11-Trm112 complex, which forms 2-methylguanosine at position 10 on several tRNAs and thereby is assumed to stabilize tRNA structure. We show that Trm112 is important for Trm11 enzymatic activity by influencing S-adenosyl-L-methionine binding and by contributing to tRNA binding. Using hydrogen-deuterium eXchange coupled to mass spectrometry, we obtained experimental evidences that the Trm11-Trm112 interaction relies on the same molecular bases as those described for other Trm112-methyltransferases complexes. Hence, all Trm112-dependent methyltransferases compete to interact with this partner.

Activation mode of the eukaryotic m2G10tRNA methyltransferase Trm11 by its partner protein Trm112

Activation mode of the eukaryotic m²G₁₀tRNA methyltransferase Trm11 by its partner protein Trm112