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Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria

Mitochondrial translation synthesizes key subunits of the respiratory complexes. In Schizosaccharomyces pombe, strains lacking Mrf1, the mitochondrial stop codon recognition factor, are viable, suggesting that other factors can play a role in translation termination. S. pombe contains four predicted...

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Detalles Bibliográficos
Autores principales: Dujeancourt, Laurent, Richter, Ricarda, Chrzanowska-Lightowlers, Zofia M., Bonnefoy, Nathalie, Herbert, Christopher J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3919214/
https://www.ncbi.nlm.nih.gov/pubmed/23892058
http://dx.doi.org/10.1016/j.mito.2013.07.115
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author Dujeancourt, Laurent
Richter, Ricarda
Chrzanowska-Lightowlers, Zofia M.
Bonnefoy, Nathalie
Herbert, Christopher J.
author_facet Dujeancourt, Laurent
Richter, Ricarda
Chrzanowska-Lightowlers, Zofia M.
Bonnefoy, Nathalie
Herbert, Christopher J.
author_sort Dujeancourt, Laurent
collection PubMed
description Mitochondrial translation synthesizes key subunits of the respiratory complexes. In Schizosaccharomyces pombe, strains lacking Mrf1, the mitochondrial stop codon recognition factor, are viable, suggesting that other factors can play a role in translation termination. S. pombe contains four predicted peptidyl tRNA hydrolases, two of which (Pth3 and Pth4), have a GGQ motif that is conserved in class I release factors. We show that high dosage of Pth4 can compensate for the absence of Mrf1 and loss of Pth4 exacerbates the lack of Mrf1. Also Pth4 is a component of the mitochondrial ribosome, suggesting that it could help recycling stalled ribosomes.
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spelling pubmed-39192142014-02-10 Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria Dujeancourt, Laurent Richter, Ricarda Chrzanowska-Lightowlers, Zofia M. Bonnefoy, Nathalie Herbert, Christopher J. Mitochondrion Article Mitochondrial translation synthesizes key subunits of the respiratory complexes. In Schizosaccharomyces pombe, strains lacking Mrf1, the mitochondrial stop codon recognition factor, are viable, suggesting that other factors can play a role in translation termination. S. pombe contains four predicted peptidyl tRNA hydrolases, two of which (Pth3 and Pth4), have a GGQ motif that is conserved in class I release factors. We show that high dosage of Pth4 can compensate for the absence of Mrf1 and loss of Pth4 exacerbates the lack of Mrf1. Also Pth4 is a component of the mitochondrial ribosome, suggesting that it could help recycling stalled ribosomes. Elsevier Science 2013-11 /pmc/articles/PMC3919214/ /pubmed/23892058 http://dx.doi.org/10.1016/j.mito.2013.07.115 Text en © 2013 Elsevier B.V. https://creativecommons.org/licenses/by/3.0/This is an open access article under the CC BY license (https://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Dujeancourt, Laurent
Richter, Ricarda
Chrzanowska-Lightowlers, Zofia M.
Bonnefoy, Nathalie
Herbert, Christopher J.
Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria
title Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria
title_full Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria
title_fullStr Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria
title_full_unstemmed Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria
title_short Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria
title_sort interactions between peptidyl trna hydrolase homologs and the ribosomal release factor mrf1 in s. pombe mitochondria
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3919214/
https://www.ncbi.nlm.nih.gov/pubmed/23892058
http://dx.doi.org/10.1016/j.mito.2013.07.115
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