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Localization and RNA Binding of Mitochondrial Aminoacyl tRNA Synthetases

Mitochondria contain a complete translation machinery that is used to translate its internally transcribed mRNAs. This machinery uses a distinct set of tRNAs that are charged with cognate amino acids inside the organelle. Interestingly, charging is executed by aminoacyl tRNA synthetases (aaRS) that...

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Autores principales: Garin, Shahar, Levi, Ofri, Cohen, Bar, Golani-Armon, Adi, Arava, Yoav S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7600831/
https://www.ncbi.nlm.nih.gov/pubmed/33053729
http://dx.doi.org/10.3390/genes11101185
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author Garin, Shahar
Levi, Ofri
Cohen, Bar
Golani-Armon, Adi
Arava, Yoav S.
author_facet Garin, Shahar
Levi, Ofri
Cohen, Bar
Golani-Armon, Adi
Arava, Yoav S.
author_sort Garin, Shahar
collection PubMed
description Mitochondria contain a complete translation machinery that is used to translate its internally transcribed mRNAs. This machinery uses a distinct set of tRNAs that are charged with cognate amino acids inside the organelle. Interestingly, charging is executed by aminoacyl tRNA synthetases (aaRS) that are encoded by the nuclear genome, translated in the cytosol, and need to be imported into the mitochondria. Here, we review import mechanisms of these enzymes with emphasis on those that are localized to both mitochondria and cytosol. Furthermore, we describe RNA recognition features of these enzymes and their interaction with tRNA and non-tRNA molecules. The dual localization of mitochondria-destined aaRSs and their association with various RNA types impose diverse impacts on cellular physiology. Yet, the breadth and significance of these functions are not fully resolved. We highlight here possibilities for future explorations.
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spelling pubmed-76008312020-11-01 Localization and RNA Binding of Mitochondrial Aminoacyl tRNA Synthetases Garin, Shahar Levi, Ofri Cohen, Bar Golani-Armon, Adi Arava, Yoav S. Genes (Basel) Review Mitochondria contain a complete translation machinery that is used to translate its internally transcribed mRNAs. This machinery uses a distinct set of tRNAs that are charged with cognate amino acids inside the organelle. Interestingly, charging is executed by aminoacyl tRNA synthetases (aaRS) that are encoded by the nuclear genome, translated in the cytosol, and need to be imported into the mitochondria. Here, we review import mechanisms of these enzymes with emphasis on those that are localized to both mitochondria and cytosol. Furthermore, we describe RNA recognition features of these enzymes and their interaction with tRNA and non-tRNA molecules. The dual localization of mitochondria-destined aaRSs and their association with various RNA types impose diverse impacts on cellular physiology. Yet, the breadth and significance of these functions are not fully resolved. We highlight here possibilities for future explorations. MDPI 2020-10-12 /pmc/articles/PMC7600831/ /pubmed/33053729 http://dx.doi.org/10.3390/genes11101185 Text en © 2020 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 (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Garin, Shahar
Levi, Ofri
Cohen, Bar
Golani-Armon, Adi
Arava, Yoav S.
Localization and RNA Binding of Mitochondrial Aminoacyl tRNA Synthetases
title Localization and RNA Binding of Mitochondrial Aminoacyl tRNA Synthetases
title_full Localization and RNA Binding of Mitochondrial Aminoacyl tRNA Synthetases
title_fullStr Localization and RNA Binding of Mitochondrial Aminoacyl tRNA Synthetases
title_full_unstemmed Localization and RNA Binding of Mitochondrial Aminoacyl tRNA Synthetases
title_short Localization and RNA Binding of Mitochondrial Aminoacyl tRNA Synthetases
title_sort localization and rna binding of mitochondrial aminoacyl trna synthetases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7600831/
https://www.ncbi.nlm.nih.gov/pubmed/33053729
http://dx.doi.org/10.3390/genes11101185
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