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  Novel insights into the mechanism of chaperone-assisted protein disaggregation

Weibezahn, J., Schlieker, C., Tessarz, P., Mogk, A., & Bukau, B. (2005). Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol Chem, 386(8), 739-44. doi:10.1515/BC.2005.086.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-693F-A Version Permalink: https://hdl.handle.net/21.11116/0000-000B-6940-7
Genre: Journal Article

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https://www.ncbi.nlm.nih.gov/pubmed/16201868 (Any fulltext)
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 Creators:
Weibezahn, J., Author
Schlieker, C., Author
Tessarz, P.1, Author           
Mogk, A., Author
Bukau, B., Author
Affiliations:
1Tessarz – Chromatin and Ageing, Max Planck Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_1942296              

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Free keywords: Escherichia coli Proteins/chemistry/metabolism HSP70 Heat-Shock Proteins/chemistry/*metabolism Heat-Shock Proteins/chemistry/metabolism Heat-Shock Response Kinetics Molecular Chaperones/genetics/*metabolism Protein Conformation *Protein Folding *Protein Renaturation
 Abstract: Cell survival under severe thermal stress requires the activity of a bi-chaperone system, consisting of the ring-forming AAA+ chaperone ClpB (Hsp104) and the DnaK (Hsp70) chaperone system, which acts to solubilize and reactivate aggregated proteins. Recent studies have provided novel insight into the mechanism of protein disaggregation, demonstrating that ClpB/Hsp104 extracts unfolded polypeptides from an aggregate by threading them through its central pore. This translocation activity is necessary but not sufficient for aggregate solubilization. In addition, the middle (M) domain of ClpB and the DnaK system have essential roles, possibly by providing an unfolding force, which facilitates the extraction of misfolded proteins from aggregates.

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 Dates: 2005-082005
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: Other: 16201868
DOI: 10.1515/BC.2005.086
ISSN: 1431-6730 (Print)1431-6730 (Linking)
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Title: Biol Chem
Source Genre: Journal
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Pages: - Volume / Issue: 386 (8) Sequence Number: - Start / End Page: 739 - 44 Identifier: -