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Aminoacyl-tRNA Synthetase Complexes in Evolution
Aminoacyl-tRNA synthetases are essential enzymes for interpreting the genetic code. They are responsible for the proper pairing of codons on mRNA with amino acids. In addition to this canonical, translational function, they are also involved in the control of many cellular pathways essential for the...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4394549/ https://www.ncbi.nlm.nih.gov/pubmed/25807264 http://dx.doi.org/10.3390/ijms16036571 |
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author | Havrylenko, Svitlana Mirande, Marc |
author_facet | Havrylenko, Svitlana Mirande, Marc |
author_sort | Havrylenko, Svitlana |
collection | PubMed |
description | Aminoacyl-tRNA synthetases are essential enzymes for interpreting the genetic code. They are responsible for the proper pairing of codons on mRNA with amino acids. In addition to this canonical, translational function, they are also involved in the control of many cellular pathways essential for the maintenance of cellular homeostasis. Association of several of these enzymes within supramolecular assemblies is a key feature of organization of the translation apparatus in eukaryotes. It could be a means to control their oscillation between translational functions, when associated within a multi-aminoacyl-tRNA synthetase complex (MARS), and nontranslational functions, after dissociation from the MARS and association with other partners. In this review, we summarize the composition of the different MARS described from archaea to mammals, the mode of assembly of these complexes, and their roles in maintenance of cellular homeostasis. |
format | Online Article Text |
id | pubmed-4394549 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-43945492015-05-21 Aminoacyl-tRNA Synthetase Complexes in Evolution Havrylenko, Svitlana Mirande, Marc Int J Mol Sci Review Aminoacyl-tRNA synthetases are essential enzymes for interpreting the genetic code. They are responsible for the proper pairing of codons on mRNA with amino acids. In addition to this canonical, translational function, they are also involved in the control of many cellular pathways essential for the maintenance of cellular homeostasis. Association of several of these enzymes within supramolecular assemblies is a key feature of organization of the translation apparatus in eukaryotes. It could be a means to control their oscillation between translational functions, when associated within a multi-aminoacyl-tRNA synthetase complex (MARS), and nontranslational functions, after dissociation from the MARS and association with other partners. In this review, we summarize the composition of the different MARS described from archaea to mammals, the mode of assembly of these complexes, and their roles in maintenance of cellular homeostasis. MDPI 2015-03-23 /pmc/articles/PMC4394549/ /pubmed/25807264 http://dx.doi.org/10.3390/ijms16036571 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Havrylenko, Svitlana Mirande, Marc Aminoacyl-tRNA Synthetase Complexes in Evolution |
title | Aminoacyl-tRNA Synthetase Complexes in Evolution |
title_full | Aminoacyl-tRNA Synthetase Complexes in Evolution |
title_fullStr | Aminoacyl-tRNA Synthetase Complexes in Evolution |
title_full_unstemmed | Aminoacyl-tRNA Synthetase Complexes in Evolution |
title_short | Aminoacyl-tRNA Synthetase Complexes in Evolution |
title_sort | aminoacyl-trna synthetase complexes in evolution |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4394549/ https://www.ncbi.nlm.nih.gov/pubmed/25807264 http://dx.doi.org/10.3390/ijms16036571 |
work_keys_str_mv | AT havrylenkosvitlana aminoacyltrnasynthetasecomplexesinevolution AT mirandemarc aminoacyltrnasynthetasecomplexesinevolution |