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A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes
The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to ribosomes and contacts nascent polypeptides to assist cotranslational folding. In this study, we demonstrate that nascent polypeptide–associated complex (NAC), another ribosome-tethered system, is functionally conne...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2854369/ https://www.ncbi.nlm.nih.gov/pubmed/20368618 http://dx.doi.org/10.1083/jcb.200910074 |
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author | Koplin, Ansgar Preissler, Steffen Ilina, Yulia Koch, Miriam Scior, Annika Erhardt, Marc Deuerling, Elke |
author_facet | Koplin, Ansgar Preissler, Steffen Ilina, Yulia Koch, Miriam Scior, Annika Erhardt, Marc Deuerling, Elke |
author_sort | Koplin, Ansgar |
collection | PubMed |
description | The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to ribosomes and contacts nascent polypeptides to assist cotranslational folding. In this study, we demonstrate that nascent polypeptide–associated complex (NAC), another ribosome-tethered system, is functionally connected to SSB–RAC and the cytosolic Hsp70 network. Simultaneous deletions of genes encoding NAC and SSB caused conditional loss of cell viability under protein-folding stress conditions. Furthermore, NAC mutations revealed genetic interaction with a deletion of Sse1, a nucleotide exchange factor regulating the cytosolic Hsp70 network. Cells lacking SSB or Sse1 showed protein aggregation, which is enhanced by additional loss of NAC; however, these mutants differ in their potential client repertoire. Aggregation of ribosomal proteins and biogenesis factors accompanied by a pronounced deficiency in ribosomal particles and translating ribosomes only occurs in ssbΔ and nacΔssbΔ cells, suggesting that SSB and NAC control ribosome biogenesis. Thus, SSB–RAC and NAC assist protein folding and likewise have important functions for regulation of ribosome levels. These findings emphasize the concept that ribosome production is coordinated with the protein-folding capacity of ribosome-associated chaperones. |
format | Text |
id | pubmed-2854369 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-28543692010-10-05 A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes Koplin, Ansgar Preissler, Steffen Ilina, Yulia Koch, Miriam Scior, Annika Erhardt, Marc Deuerling, Elke J Cell Biol Research Articles The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to ribosomes and contacts nascent polypeptides to assist cotranslational folding. In this study, we demonstrate that nascent polypeptide–associated complex (NAC), another ribosome-tethered system, is functionally connected to SSB–RAC and the cytosolic Hsp70 network. Simultaneous deletions of genes encoding NAC and SSB caused conditional loss of cell viability under protein-folding stress conditions. Furthermore, NAC mutations revealed genetic interaction with a deletion of Sse1, a nucleotide exchange factor regulating the cytosolic Hsp70 network. Cells lacking SSB or Sse1 showed protein aggregation, which is enhanced by additional loss of NAC; however, these mutants differ in their potential client repertoire. Aggregation of ribosomal proteins and biogenesis factors accompanied by a pronounced deficiency in ribosomal particles and translating ribosomes only occurs in ssbΔ and nacΔssbΔ cells, suggesting that SSB and NAC control ribosome biogenesis. Thus, SSB–RAC and NAC assist protein folding and likewise have important functions for regulation of ribosome levels. These findings emphasize the concept that ribosome production is coordinated with the protein-folding capacity of ribosome-associated chaperones. The Rockefeller University Press 2010-04-05 /pmc/articles/PMC2854369/ /pubmed/20368618 http://dx.doi.org/10.1083/jcb.200910074 Text en © 2010 Koplin et al. 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.rupress.org/terms). 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 | Research Articles Koplin, Ansgar Preissler, Steffen Ilina, Yulia Koch, Miriam Scior, Annika Erhardt, Marc Deuerling, Elke A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes |
title | A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes |
title_full | A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes |
title_fullStr | A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes |
title_full_unstemmed | A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes |
title_short | A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes |
title_sort | dual function for chaperones ssb–rac and the nac nascent polypeptide–associated complex on ribosomes |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2854369/ https://www.ncbi.nlm.nih.gov/pubmed/20368618 http://dx.doi.org/10.1083/jcb.200910074 |
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