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Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo‐tomography
We employed electron cryo‐tomography to visualize cytosolic ribosomes on the surface of mitochondria. Translation‐arrested ribosomes reveal the clustered organization of the TOM complex, corroborating earlier reports of localized translation. Ribosomes are shown to interact specifically with the TOM...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5623831/ https://www.ncbi.nlm.nih.gov/pubmed/28827470 http://dx.doi.org/10.15252/embr.201744261 |
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author | Gold, Vicki AM Chroscicki, Piotr Bragoszewski, Piotr Chacinska, Agnieszka |
author_facet | Gold, Vicki AM Chroscicki, Piotr Bragoszewski, Piotr Chacinska, Agnieszka |
author_sort | Gold, Vicki AM |
collection | PubMed |
description | We employed electron cryo‐tomography to visualize cytosolic ribosomes on the surface of mitochondria. Translation‐arrested ribosomes reveal the clustered organization of the TOM complex, corroborating earlier reports of localized translation. Ribosomes are shown to interact specifically with the TOM complex, and nascent chain binding is crucial for ribosome recruitment and stabilization. Ribosomes are bound to the membrane in discrete clusters, often in the vicinity of the crista junctions. This interaction highlights how protein synthesis may be coupled with transport. Our work provides unique insights into the spatial organization of cytosolic ribosomes on mitochondria. |
format | Online Article Text |
id | pubmed-5623831 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-56238312017-10-04 Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo‐tomography Gold, Vicki AM Chroscicki, Piotr Bragoszewski, Piotr Chacinska, Agnieszka EMBO Rep Articles We employed electron cryo‐tomography to visualize cytosolic ribosomes on the surface of mitochondria. Translation‐arrested ribosomes reveal the clustered organization of the TOM complex, corroborating earlier reports of localized translation. Ribosomes are shown to interact specifically with the TOM complex, and nascent chain binding is crucial for ribosome recruitment and stabilization. Ribosomes are bound to the membrane in discrete clusters, often in the vicinity of the crista junctions. This interaction highlights how protein synthesis may be coupled with transport. Our work provides unique insights into the spatial organization of cytosolic ribosomes on mitochondria. John Wiley and Sons Inc. 2017-08-21 2017-10 /pmc/articles/PMC5623831/ /pubmed/28827470 http://dx.doi.org/10.15252/embr.201744261 Text en © 2017 The Authors. Published under the terms of the CC BY 4.0 license This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Gold, Vicki AM Chroscicki, Piotr Bragoszewski, Piotr Chacinska, Agnieszka Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo‐tomography |
title | Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo‐tomography |
title_full | Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo‐tomography |
title_fullStr | Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo‐tomography |
title_full_unstemmed | Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo‐tomography |
title_short | Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo‐tomography |
title_sort | visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo‐tomography |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5623831/ https://www.ncbi.nlm.nih.gov/pubmed/28827470 http://dx.doi.org/10.15252/embr.201744261 |
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