1. The catalytic activity of the translation termination factor methyltransferase Mtq2-Trm112 complex is required for large ribosomal subunit biogenesis.
- Author
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Lacoux C, Wacheul L, Saraf K, Pythoud N, Huvelle E, Figaro S, Graille M, Carapito C, Lafontaine DLJ, and Heurgué-Hamard V
- Subjects
- Binding Sites, Biocatalysis, Cloning, Molecular, Crystallography, X-Ray, Escherichia coli genetics, Escherichia coli metabolism, Genetic Vectors chemistry, Genetic Vectors metabolism, Methyltransferases chemistry, Methyltransferases metabolism, Models, Molecular, Peptide Chain Termination, Translational, Peptide Termination Factors metabolism, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, RNA, Ribosomal biosynthesis, RNA, Ribosomal genetics, RNA, Ribosomal, 5.8S biosynthesis, RNA, Ribosomal, 5.8S genetics, Recombinant Proteins chemistry, Recombinant Proteins genetics, Recombinant Proteins metabolism, Ribosome Subunits, Large, Eukaryotic metabolism, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins chemistry, Saccharomyces cerevisiae Proteins metabolism, Substrate Specificity, tRNA Methyltransferases chemistry, tRNA Methyltransferases metabolism, Gene Expression Regulation, Fungal, Methyltransferases genetics, Organelle Biogenesis, Peptide Termination Factors genetics, Ribosome Subunits, Large, Eukaryotic genetics, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins genetics, tRNA Methyltransferases genetics
- Abstract
The Mtq2-Trm112 methyltransferase modifies the eukaryotic translation termination factor eRF1 on the glutamine side chain of a universally conserved GGQ motif that is essential for release of newly synthesized peptides. Although this modification is found in the three domains of life, its exact role in eukaryotes remains unknown. As the deletion of MTQ2 leads to severe growth impairment in yeast, we have investigated its role further and tested its putative involvement in ribosome biogenesis. We found that Mtq2 is associated with nuclear 60S subunit precursors, and we demonstrate that its catalytic activity is required for nucleolar release of pre-60S and for efficient production of mature 5.8S and 25S rRNAs. Thus, we identify Mtq2 as a novel ribosome assembly factor important for large ribosomal subunit formation. We propose that Mtq2-Trm112 might modify eRF1 in the nucleus as part of a quality control mechanism aimed at proof-reading the peptidyl transferase center, where it will subsequently bind during translation termination., (© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.)
- Published
- 2020
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