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The structural and functional coupling of two molecular machines, the ribosome and the translocon
Ribosomes synthesizing secretory and membrane proteins are bound to translocons at the membrane of the endoplasmic reticulum (ER). Both the ribosome and translocon are complex macromolecular machines whose structural and functional interactions are poorly understood. A new study by Pool (Pool, M.R....
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2711596/ https://www.ncbi.nlm.nih.gov/pubmed/19468072 http://dx.doi.org/10.1083/jcb.200902014 |
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author | Johnson, Arthur E. |
author_facet | Johnson, Arthur E. |
author_sort | Johnson, Arthur E. |
collection | PubMed |
description | Ribosomes synthesizing secretory and membrane proteins are bound to translocons at the membrane of the endoplasmic reticulum (ER). Both the ribosome and translocon are complex macromolecular machines whose structural and functional interactions are poorly understood. A new study by Pool (Pool, M.R. 2009. J. Cell Biol. 185:889–902) has now shown that the structure of the translocon is dictated by the identity of the protein being synthesized by the ribosome, thereby demonstrating that the two macromolecular machines are structurally coupled for functional purposes. The study also identifies an unexpected component in the apparent molecular linkage that connects the two machines, a discovery that shows the current view of translocon structure is oversimplified. |
format | Text |
id | pubmed-2711596 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-27115962009-12-01 The structural and functional coupling of two molecular machines, the ribosome and the translocon Johnson, Arthur E. J Cell Biol Reviews Ribosomes synthesizing secretory and membrane proteins are bound to translocons at the membrane of the endoplasmic reticulum (ER). Both the ribosome and translocon are complex macromolecular machines whose structural and functional interactions are poorly understood. A new study by Pool (Pool, M.R. 2009. J. Cell Biol. 185:889–902) has now shown that the structure of the translocon is dictated by the identity of the protein being synthesized by the ribosome, thereby demonstrating that the two macromolecular machines are structurally coupled for functional purposes. The study also identifies an unexpected component in the apparent molecular linkage that connects the two machines, a discovery that shows the current view of translocon structure is oversimplified. The Rockefeller University Press 2009-06-01 /pmc/articles/PMC2711596/ /pubmed/19468072 http://dx.doi.org/10.1083/jcb.200902014 Text en © 2009 Johnson This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Reviews Johnson, Arthur E. The structural and functional coupling of two molecular machines, the ribosome and the translocon |
title | The structural and functional coupling of two molecular machines, the ribosome and the translocon |
title_full | The structural and functional coupling of two molecular machines, the ribosome and the translocon |
title_fullStr | The structural and functional coupling of two molecular machines, the ribosome and the translocon |
title_full_unstemmed | The structural and functional coupling of two molecular machines, the ribosome and the translocon |
title_short | The structural and functional coupling of two molecular machines, the ribosome and the translocon |
title_sort | structural and functional coupling of two molecular machines, the ribosome and the translocon |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2711596/ https://www.ncbi.nlm.nih.gov/pubmed/19468072 http://dx.doi.org/10.1083/jcb.200902014 |
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