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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Preissler, Steffen Erhardt, Marc Koplin, Ansgar Koch, Miriam Scior, Annika Ilina, Yulia Deuerling, Elke |
| Description | Author Affiliation: Koplin A ( Laboratory of Molecular Microbiology, Department of Biology, and 2 Konstanz Research School of Chemical Biology, University of Konstanz, 78457 Konstanz, Germany.) |
| Abstract | 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. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 189 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2010-04-05 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | HSP70 Heat-Shock Proteins Metabolism Molecular Chaperones Ribosomal Proteins Ribosomes Saccharomyces Cerevisiae Proteins Binding Sites Cytosol Genetics Models, Biological Phenotype Protein Folding Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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