A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes

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2010
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Koplin, Ansgar
Preissler, Steffen
Ilina, Yulia
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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.

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ISO 690KOPLIN, Ansgar, Steffen PREISSLER, Yulia ILINA, Miriam KOCH, Annika SCIOR, Marc ERHARDT, Elke DEUERLING, 2010. A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes. In: The Journal of Cell Biology. 2010, 189(1), pp. 57-68. ISSN 0021-9525. eISSN 1540-8140. Available under: doi: 10.1083/jcb.200910074
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@article{Koplin2010-04-05funct-12493,
  year={2010},
  doi={10.1083/jcb.200910074},
  title={A dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes},
  number={1},
  volume={189},
  issn={0021-9525},
  journal={The Journal of Cell Biology},
  pages={57--68},
  author={Koplin, Ansgar and Preissler, Steffen and Ilina, Yulia and Koch, Miriam and Scior, Annika and Erhardt, Marc and Deuerling, Elke},
  note={Supplemental material findet man unter: http://jcb.rupress.org/content/suppl/2010/04/05/jcb.200910074.DC1/JCB_200910074_sm.pdf}
}
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    <dcterms:abstract xml:lang="eng">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.</dcterms:abstract>
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Supplemental material findet man unter: http://jcb.rupress.org/content/suppl/2010/04/05/jcb.200910074.DC1/JCB_200910074_sm.pdf
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