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Activation mode of the eukaryotic m(2)G(10) tRNA methyltransferase Trm11 by its partner protein Trm112

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 deco...

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Autores principales: Bourgeois, Gabrielle, Marcoux, Julien, Saliou, Jean-Michel, Cianférani, Sarah, Graille, Marc
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5389515/
https://www.ncbi.nlm.nih.gov/pubmed/27986851
http://dx.doi.org/10.1093/nar/gkw1271
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author Bourgeois, Gabrielle
Marcoux, Julien
Saliou, Jean-Michel
Cianférani, Sarah
Graille, Marc
author_facet Bourgeois, Gabrielle
Marcoux, Julien
Saliou, Jean-Michel
Cianférani, Sarah
Graille, Marc
author_sort Bourgeois, Gabrielle
collection PubMed
description 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.
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spelling pubmed-53895152017-04-24 Activation mode of the eukaryotic m(2)G(10) tRNA methyltransferase Trm11 by its partner protein Trm112 Bourgeois, Gabrielle Marcoux, Julien Saliou, Jean-Michel Cianférani, Sarah Graille, Marc Nucleic Acids Res Nucleic Acid Enzymes 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. Oxford University Press 2017-02-28 2016-12-16 /pmc/articles/PMC5389515/ /pubmed/27986851 http://dx.doi.org/10.1093/nar/gkw1271 Text en © The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Nucleic Acid Enzymes
Bourgeois, Gabrielle
Marcoux, Julien
Saliou, Jean-Michel
Cianférani, Sarah
Graille, Marc
Activation mode of the eukaryotic m(2)G(10) tRNA methyltransferase Trm11 by its partner protein Trm112
title Activation mode of the eukaryotic m(2)G(10) tRNA methyltransferase Trm11 by its partner protein Trm112
title_full Activation mode of the eukaryotic m(2)G(10) tRNA methyltransferase Trm11 by its partner protein Trm112
title_fullStr Activation mode of the eukaryotic m(2)G(10) tRNA methyltransferase Trm11 by its partner protein Trm112
title_full_unstemmed Activation mode of the eukaryotic m(2)G(10) tRNA methyltransferase Trm11 by its partner protein Trm112
title_short Activation mode of the eukaryotic m(2)G(10) tRNA methyltransferase Trm11 by its partner protein Trm112
title_sort activation mode of the eukaryotic m(2)g(10) trna methyltransferase trm11 by its partner protein trm112
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5389515/
https://www.ncbi.nlm.nih.gov/pubmed/27986851
http://dx.doi.org/10.1093/nar/gkw1271
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