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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Tyedmers, Jens Winkler, Juliane Bukau, Bernd Mogk, Axel |
| Description | Author Affiliation: Winkler J ( Center for Molecular Biology of the University of Heidelberg and German Cancer Research Center, DKFZ-ZMBH Alliance, Universität Heidelberg, Heidelberg D-69120, Germany.) |
| Abstract | Hsp100 and Hsp70 chaperones in bacteria, yeast, and plants cooperate to reactivate aggregated proteins. Disaggregation relies on Hsp70 function and on ATP-dependent threading of aggregated polypeptides through the pore of the Hsp100 $AAA^{+}$ hexamer. In yeast, both chaperones also promote propagation of prions by fibril fragmentation, but their functional interplay is controversial. Here, we demonstrate that Hsp70 chaperones were essential for species-specific targeting of their Hsp100 partner chaperones ClpB and Hsp104, respectively, to heat-induced protein aggregates in vivo. Hsp70 inactivation in yeast also abrogated Hsp104 targeting to almost all prions tested and reduced fibril mobility, which indicates that fibril fragmentation by Hsp104 requires Hsp70. The Sup35 prion was unique in allowing Hsp70-independent association of Hsp104 via its N-terminal domain, which, however, was nonproductive. Hsp104 overproduction even outcompeted Hsp70 for Sup35 prion binding, which explains why this condition prevented Sup35 fragmentation and caused prion curing. Our findings indicate a conserved mechanism of Hsp70–Hsp100 cooperation at the surface of protein aggregates and prion fibrils. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 3 |
| Volume Number | 198 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2012-08-06 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | HSP70 Heat-Shock Proteins Metabolism Heat-Shock Proteins Prions Chemistry Escherichia Coli Escherichia Coli Proteins Fluorescent Dyes Pharmacology Green Fluorescent Proteins Microscopy, Fluorescence Molecular Chaperones Peptide Termination Factors Peptides Plasmids Protein Structure, Tertiary Proteins Saccharomyces Cerevisiae Genetics Saccharomyces Cerevisiae Proteins Time Factors Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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