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NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum
Nascent polypeptide-associated complex (NAC) was initially found to bind to any segment of the nascent chain except signal sequences. In this way, NAC is believed to prevent mistargeting due to binding of signal recognition particle (SRP) to signalless ribosome nascent chain complexes (RNCs). Here w...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3418300/ https://www.ncbi.nlm.nih.gov/pubmed/22740632 http://dx.doi.org/10.1091/mbc.E12-02-0112 |
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author | Zhang, Ying Berndt, Uta Gölz, Hanna Tais, Arlette Oellerer, Stefan Wölfle, Tina Fitzke, Edith Rospert, Sabine |
author_facet | Zhang, Ying Berndt, Uta Gölz, Hanna Tais, Arlette Oellerer, Stefan Wölfle, Tina Fitzke, Edith Rospert, Sabine |
author_sort | Zhang, Ying |
collection | PubMed |
description | Nascent polypeptide-associated complex (NAC) was initially found to bind to any segment of the nascent chain except signal sequences. In this way, NAC is believed to prevent mistargeting due to binding of signal recognition particle (SRP) to signalless ribosome nascent chain complexes (RNCs). Here we revisit the interplay between NAC and SRP. NAC does not affect SRP function with respect to signalless RNCs; however, NAC does affect SRP function with respect to RNCs targeted to the endoplasmic reticulum (ER). First, early recruitment of SRP to RNCs containing a signal sequence within the ribosomal tunnel is NAC dependent. Second, NAC is able to directly and tightly bind to nascent signal sequences. Third, SRP initially displaces NAC from RNCs; however, when the signal sequence emerges further, trimeric NAC·RNC·SRP complexes form. Fourth, upon docking to the ER membrane NAC remains bound to RNCs, allowing NAC to shield cytosolically exposed nascent chain domains not only before but also during cotranslational translocation. The combined data indicate a functional interplay between NAC and SRP on ER-targeted RNCs, which is based on the ability of the two complexes to bind simultaneously to distinct segments of a single nascent chain. |
format | Online Article Text |
id | pubmed-3418300 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-34183002012-10-30 NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum Zhang, Ying Berndt, Uta Gölz, Hanna Tais, Arlette Oellerer, Stefan Wölfle, Tina Fitzke, Edith Rospert, Sabine Mol Biol Cell Articles Nascent polypeptide-associated complex (NAC) was initially found to bind to any segment of the nascent chain except signal sequences. In this way, NAC is believed to prevent mistargeting due to binding of signal recognition particle (SRP) to signalless ribosome nascent chain complexes (RNCs). Here we revisit the interplay between NAC and SRP. NAC does not affect SRP function with respect to signalless RNCs; however, NAC does affect SRP function with respect to RNCs targeted to the endoplasmic reticulum (ER). First, early recruitment of SRP to RNCs containing a signal sequence within the ribosomal tunnel is NAC dependent. Second, NAC is able to directly and tightly bind to nascent signal sequences. Third, SRP initially displaces NAC from RNCs; however, when the signal sequence emerges further, trimeric NAC·RNC·SRP complexes form. Fourth, upon docking to the ER membrane NAC remains bound to RNCs, allowing NAC to shield cytosolically exposed nascent chain domains not only before but also during cotranslational translocation. The combined data indicate a functional interplay between NAC and SRP on ER-targeted RNCs, which is based on the ability of the two complexes to bind simultaneously to distinct segments of a single nascent chain. The American Society for Cell Biology 2012-08-15 /pmc/articles/PMC3418300/ /pubmed/22740632 http://dx.doi.org/10.1091/mbc.E12-02-0112 Text en © 2012 Zhang et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Zhang, Ying Berndt, Uta Gölz, Hanna Tais, Arlette Oellerer, Stefan Wölfle, Tina Fitzke, Edith Rospert, Sabine NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum |
title | NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum |
title_full | NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum |
title_fullStr | NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum |
title_full_unstemmed | NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum |
title_short | NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum |
title_sort | nac functions as a modulator of srp during the early steps of protein targeting to the endoplasmic reticulum |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3418300/ https://www.ncbi.nlm.nih.gov/pubmed/22740632 http://dx.doi.org/10.1091/mbc.E12-02-0112 |
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