Projects per year
The AAA(+)-ATPases are a family of molecular motors which have been seconded into a plethora of cellular tasks. One subset, the Hsp100 molecular chaperones, are general protein remodellers that help to maintain the integrity of the cellular proteome by means of protein destruction or resurrection. In this review we focus on one family of Hsp100s, the homologous ClpB and Hsp104 molecular chaperones that convey thermotolerance by resolubilising and rescuing proteins from aggregates. We explore how the nucleotide binding and hydrolysis properties at the twelve nucleotide-binding domains of these hexameric rings are coupled to protein disaggregation, highlighting similarities and differences between ClpB and Hsp104.
|Number of pages||11|
|Journal||Journal of Structural Biology|
|Publication status||Published - Aug 2012|
Bibliographical noteCopyright © 2012 Elsevier Inc. All rights reserved.
- Escherichia coli Proteins
- Heat-Shock Proteins
- Molecular Chaperones
FingerprintDive into the research topics of 'Mapping the road to recovery: the ClpB/Hsp104 molecular chaperone'. Together they form a unique fingerprint.
- 1 Finished
THE MECHANISM OF A MULTI-CHAPERONE SYSTEM FOR PROMOTING PROTEIN DISAGGREGATION
15/08/09 → 15/08/12