Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis

Aminoacyl-tRNA synthetases (ARSs) are critical components of protein translation, providing ribosomes with aminoacyl-tRNAs. In return, ribosomes release uncharged tRNAs as ARS substrates. Here, we show that tRNA deacylation can be uncoupled from protein synthesis in an amino acid specific manner. Wh...

Descripción completa

Detalles Bibliográficos
Autores principales: David, Alexandre, Das, Suman R., Gibbs, James S., Bennink, Jack R., Yewdell, Jonathan W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3302863/
https://www.ncbi.nlm.nih.gov/pubmed/22427952
http://dx.doi.org/10.1371/journal.pone.0033072
_version_ 1782226693790892032
author David, Alexandre
Das, Suman R.
Gibbs, James S.
Bennink, Jack R.
Yewdell, Jonathan W.
author_facet David, Alexandre
Das, Suman R.
Gibbs, James S.
Bennink, Jack R.
Yewdell, Jonathan W.
author_sort David, Alexandre
collection PubMed
description Aminoacyl-tRNA synthetases (ARSs) are critical components of protein translation, providing ribosomes with aminoacyl-tRNAs. In return, ribosomes release uncharged tRNAs as ARS substrates. Here, we show that tRNA deacylation can be uncoupled from protein synthesis in an amino acid specific manner. While tRNAs coupled to radiolabeled Met, Leu Lys, or Ser are stable in cells following translation inhibition with arsenite, radiolabeled Cys is released from tRNA at a high rate. We discuss possible translation independent functions for tRNA(Cys).
format Online
Article
Text
id pubmed-3302863
institution National Center for Biotechnology Information
language English
publishDate 2012
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-33028632012-03-16 Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis David, Alexandre Das, Suman R. Gibbs, James S. Bennink, Jack R. Yewdell, Jonathan W. PLoS One Research Article Aminoacyl-tRNA synthetases (ARSs) are critical components of protein translation, providing ribosomes with aminoacyl-tRNAs. In return, ribosomes release uncharged tRNAs as ARS substrates. Here, we show that tRNA deacylation can be uncoupled from protein synthesis in an amino acid specific manner. While tRNAs coupled to radiolabeled Met, Leu Lys, or Ser are stable in cells following translation inhibition with arsenite, radiolabeled Cys is released from tRNA at a high rate. We discuss possible translation independent functions for tRNA(Cys). Public Library of Science 2012-03-09 /pmc/articles/PMC3302863/ /pubmed/22427952 http://dx.doi.org/10.1371/journal.pone.0033072 Text en This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.
spellingShingle Research Article
David, Alexandre
Das, Suman R.
Gibbs, James S.
Bennink, Jack R.
Yewdell, Jonathan W.
Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis
title Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis
title_full Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis
title_fullStr Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis
title_full_unstemmed Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis
title_short Cysteinyl-tRNA Deacylation Can Be Uncoupled from Protein Synthesis
title_sort cysteinyl-trna deacylation can be uncoupled from protein synthesis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3302863/
https://www.ncbi.nlm.nih.gov/pubmed/22427952
http://dx.doi.org/10.1371/journal.pone.0033072
work_keys_str_mv AT davidalexandre cysteinyltrnadeacylationcanbeuncoupledfromproteinsynthesis
AT dassumanr cysteinyltrnadeacylationcanbeuncoupledfromproteinsynthesis
AT gibbsjamess cysteinyltrnadeacylationcanbeuncoupledfromproteinsynthesis
AT benninkjackr cysteinyltrnadeacylationcanbeuncoupledfromproteinsynthesis
AT yewdelljonathanw cysteinyltrnadeacylationcanbeuncoupledfromproteinsynthesis

Ejemplares similares