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FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface
The spatial organization of protein synthesis in the eukaryotic cell is essential for maintaining the integrity of the proteome and the functioning of the cell. Translation on free polysomes or on ribosomes associated with the endoplasmic reticulum has been studied for a long time. More recent data...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9826127/ https://www.ncbi.nlm.nih.gov/pubmed/36050837 http://dx.doi.org/10.1111/tpj.15962 |
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author | Hemono, Mickaele Salinas‐Giegé, Thalia Roignant, Jeanne Vingadassalon, Audrey Hammann, Philippe Ubrig, Elodie Ngondo, Patryk Duchêne, Anne‐Marie |
author_facet | Hemono, Mickaele Salinas‐Giegé, Thalia Roignant, Jeanne Vingadassalon, Audrey Hammann, Philippe Ubrig, Elodie Ngondo, Patryk Duchêne, Anne‐Marie |
author_sort | Hemono, Mickaele |
collection | PubMed |
description | The spatial organization of protein synthesis in the eukaryotic cell is essential for maintaining the integrity of the proteome and the functioning of the cell. Translation on free polysomes or on ribosomes associated with the endoplasmic reticulum has been studied for a long time. More recent data have revealed selective translation of mRNAs in other compartments, in particular at the surface of mitochondria. Although these processes have been described in many organisms, particularky in plants, the mRNA targeting and localized translation mechanisms remain poorly understood. Here, the Arabidopsis thaliana Friendly (FMT) protein is shown to be a cytosolic RNA binding protein that associates with cytosolic ribosomes at the surface of mitochondria. FMT knockout delays seedling development and causes mitochondrial clustering. The mutation also disrupts the mitochondrial proteome, as well as the localization of nuclear transcripts encoding mitochondrial proteins at the surface of mitochondria. These data indicate that FMT participates in the localization of mRNAs and their translation at the surface of mitochondria. |
format | Online Article Text |
id | pubmed-9826127 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-98261272023-01-09 FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface Hemono, Mickaele Salinas‐Giegé, Thalia Roignant, Jeanne Vingadassalon, Audrey Hammann, Philippe Ubrig, Elodie Ngondo, Patryk Duchêne, Anne‐Marie Plant J Original Articles The spatial organization of protein synthesis in the eukaryotic cell is essential for maintaining the integrity of the proteome and the functioning of the cell. Translation on free polysomes or on ribosomes associated with the endoplasmic reticulum has been studied for a long time. More recent data have revealed selective translation of mRNAs in other compartments, in particular at the surface of mitochondria. Although these processes have been described in many organisms, particularky in plants, the mRNA targeting and localized translation mechanisms remain poorly understood. Here, the Arabidopsis thaliana Friendly (FMT) protein is shown to be a cytosolic RNA binding protein that associates with cytosolic ribosomes at the surface of mitochondria. FMT knockout delays seedling development and causes mitochondrial clustering. The mutation also disrupts the mitochondrial proteome, as well as the localization of nuclear transcripts encoding mitochondrial proteins at the surface of mitochondria. These data indicate that FMT participates in the localization of mRNAs and their translation at the surface of mitochondria. John Wiley and Sons Inc. 2022-09-12 2022-10 /pmc/articles/PMC9826127/ /pubmed/36050837 http://dx.doi.org/10.1111/tpj.15962 Text en © 2022 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Original Articles Hemono, Mickaele Salinas‐Giegé, Thalia Roignant, Jeanne Vingadassalon, Audrey Hammann, Philippe Ubrig, Elodie Ngondo, Patryk Duchêne, Anne‐Marie FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface |
title |
FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface |
title_full |
FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface |
title_fullStr |
FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface |
title_full_unstemmed |
FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface |
title_short |
FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface |
title_sort | friendly (fmt) is an rna binding protein associated with cytosolic ribosomes at the mitochondrial surface |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9826127/ https://www.ncbi.nlm.nih.gov/pubmed/36050837 http://dx.doi.org/10.1111/tpj.15962 |
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