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  Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB

Werbeck, N. D., Schlee, S., & Reinstein, J. (2008). Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB. Journal of Molecular Biology (London), 378(1), 178-190. doi:10.1016/j.jmb.2008.02.026.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-0A7A-E Version Permalink: http://hdl.handle.net/21.11116/0000-0000-DE60-A
Genre: Journal Article

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JMolBiol_378_2008_178.pdf (Any fulltext), 2MB
 
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 Creators:
Werbeck, Nicolas D.1, Author              
Schlee, Sandra1, Author              
Reinstein, Jochen1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: ClpB; chaperones; AAA+ proteins; oligomer
 Abstract: The bacterial AAA+ protein ClpB and its eukaryotic homologue Hsp104 ensure thermotolerance of their respective organisms by reactivating aggregated proteins in cooperation with the Hsp70/Hsp40 chaperone system. Like many members of the AAA+ superfamily, the ClpB protomers form ringlike homohexameric complexes. The mechanical energy necessary to disentangle protein aggregates is provided by ATP hydrolysis at the two nucleotide-binding domains of each monomer. Previous studies on ClpB and Hsp104 show a complex interplay of domains and subunits resulting in homotypic and heterotypic cooperativity. Using mutations in the Walker A and Walker B nucleotide-binding motifs in combination with mixing experiments we investigated the degree of inter-subunit coupling with respect to different aspects of the ClpB working cycle. We find that subunits are tightly coupled with regard to ATPase and chaperone activity, but no coupling can be observed for ADP binding. Comparison of the data with statistical calculations suggests that for double Walker mutants, approximately two in six subunits are sufficient to abolish chaperone and ATPase activity completely. In further experiments, we determined the dynamics of subunit reshuffling. Our results show that ClpB forms a very dynamic complex, reshuffling subunits on a timescale comparable to steady-state ATP hydrolysis. We propose that this could be a protection mechanism to prevent very stable aggregates from becoming suicide inhibitors for ClpB.

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Language(s): eng - English
 Dates: 2007-11-272008-02-142008-02-212008-04-18
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 378 (1) Sequence Number: - Start / End Page: 178 - 190 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042