The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates

Eukaryotic elongation factor 1 alpha (eEF1A) is subject to extensive post-translational methylation but not all responsible enzymes are known. Here, the authors identify METTL13 as an eEF1A methyltransferase with dual specificity, which is involved in the codon-specific modulation of mRNA translatio...

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Autores principales:	Magnus E. Jakobsson, Jędrzej M. Małecki, Levon Halabelian, Benedikt S. Nilges, Rita Pinto, Srikanth Kudithipudi, Stephanie Munk, Erna Davydova, Fawzi R. Zuhairi, Cheryl H. Arrowsmith, Albert Jeltsch, Sebastian A. Leidel, Jesper V. Olsen, Pål Ø. Falnes
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1682b8aad27f487895096c47624bca86
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spelling	oai:doaj.org-article:1682b8aad27f487895096c47624bca862021-12-02T15:34:15ZThe dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates10.1038/s41467-018-05646-y2041-1723https://doaj.org/article/1682b8aad27f487895096c47624bca862018-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05646-yhttps://doaj.org/toc/2041-1723Eukaryotic elongation factor 1 alpha (eEF1A) is subject to extensive post-translational methylation but not all responsible enzymes are known. Here, the authors identify METTL13 as an eEF1A methyltransferase with dual specificity, which is involved in the codon-specific modulation of mRNA translation.Magnus E. JakobssonJędrzej M. MałeckiLevon HalabelianBenedikt S. NilgesRita PintoSrikanth KudithipudiStephanie MunkErna DavydovaFawzi R. ZuhairiCheryl H. ArrowsmithAlbert JeltschSebastian A. LeidelJesper V. OlsenPål Ø. FalnesNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Magnus E. Jakobsson Jędrzej M. Małecki Levon Halabelian Benedikt S. Nilges Rita Pinto Srikanth Kudithipudi Stephanie Munk Erna Davydova Fawzi R. Zuhairi Cheryl H. Arrowsmith Albert Jeltsch Sebastian A. Leidel Jesper V. Olsen Pål Ø. Falnes The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates
description	Eukaryotic elongation factor 1 alpha (eEF1A) is subject to extensive post-translational methylation but not all responsible enzymes are known. Here, the authors identify METTL13 as an eEF1A methyltransferase with dual specificity, which is involved in the codon-specific modulation of mRNA translation.
format	article
author	Magnus E. Jakobsson Jędrzej M. Małecki Levon Halabelian Benedikt S. Nilges Rita Pinto Srikanth Kudithipudi Stephanie Munk Erna Davydova Fawzi R. Zuhairi Cheryl H. Arrowsmith Albert Jeltsch Sebastian A. Leidel Jesper V. Olsen Pål Ø. Falnes
author_facet	Magnus E. Jakobsson Jędrzej M. Małecki Levon Halabelian Benedikt S. Nilges Rita Pinto Srikanth Kudithipudi Stephanie Munk Erna Davydova Fawzi R. Zuhairi Cheryl H. Arrowsmith Albert Jeltsch Sebastian A. Leidel Jesper V. Olsen Pål Ø. Falnes
author_sort	Magnus E. Jakobsson
title	The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates
title_short	The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates
title_full	The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates
title_fullStr	The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates
title_full_unstemmed	The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates
title_sort	dual methyltransferase mettl13 targets n terminus and lys55 of eef1a and modulates codon-specific translation rates
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/1682b8aad27f487895096c47624bca86
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The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates

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