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| Subject Categories: Proteins |
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| The EMBO Journal
(2008) 27, 328–335, doi:10.1038/sj.emboj.7601970 |
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| Chaperones in control of protein disaggregation |
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Krzysztof Liberek, Agnieszka Lewandowska and Szymon Zi tkiewicz
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Department of Molecular and Cellular Biology, Faculty of Biotechnology, University of Gdansk, Gdansk, Poland To whom correspondence should be addressed Krzysztof Liberek, Department of Molecular and Cellular Biology, Faculty of Biotechnology, University of Gdansk, Kladki 24, Gdansk 80-822, Poland. Tel.: +48 58 3019222; Fax: +48 58 3019292; E-mail: liberek@biotech.ug.gda.pl Received 7 September 2007; Accepted 3 December 2007. |
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| Abstract |
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| The chaperone protein network controls both initial protein folding and subsequent maintenance of proteins in the cell. Although the native structure of a protein is principally encoded in its amino-acid sequence, the process of folding in vivo very often requires the assistance of molecular chaperones. Chaperones also play a role in a post-translational quality control system and thus are required to maintain the proper conformation of proteins under changing environmental conditions. Many factors leading to unfolding and misfolding of proteins eventually result in protein aggregation. Stress imposed by high temperature was one of the first aggregation-inducing factors studied and remains one of the main models in this field. With massive protein aggregation occurring in response to heat exposure, the cell needs chaperones to control and counteract the aggregation process. Elimination of aggregates can be achieved by solubilization of aggregates and either refolding of the liberated polypeptides or their proteolysis. Here, we focus on the molecular mechanisms by which heat-shock protein 70 (Hsp70), Hsp100 and small Hsp chaperones liberate and refold polypeptides trapped in protein aggregates. |
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| Keywords: chaperones, Hsp70, Hsp100, protein disaggregation, protein folding |
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Top of page MORE ARTICLES LIKE THISThese links to content published by NPG are automatically generated NEWS AND VIEWSNavigating the ClpB channel to solution Nature Structural & Molecular Biology News and Views (01 Jan 2005) A new twist for an Hsp70 chaperone Nature Structural Biology News and Views (01 Jun 2002) |
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