ArticleThe Journal of biological chemistry2015
Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- A stochastic mechanism drives fast substrate translocation in the AAA+ machine ClpB.Nature communications · 2026Article
- Exogenous application of γ-aminobutyric acid alleviates temperature stress in mungbean (Vigna radiata) and its wild non-progenitor (Vigna glabrescens) by regulating heat shock protein genes.BMC plant biology · 2025Article
- Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation.The Journal of biological chemistry · 2018Article
- Dynamic structural states of ClpB involved in its disaggregation function.Nature communications · 2018Article
- Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation.The Journal of biological chemistry · 2017Article
- Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.Frontiers in molecular biosciences · 2017Review
- Mutant Analysis Reveals Allosteric Regulation of ClpB Disaggregase.Frontiers in molecular biosciences · 2017Article
- Article
- Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation.Frontiers in molecular biosciences · 2015Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ClpB/Hsp104 chaperone solubilizes and reactivates protein aggregates in cooperation with DnaK/Hsp70 and its cofactors. The ClpB/Hsp104 protomer has two AAA+ modules, AAA-1 and AAA-2, and forms a homohexamer. In the hexamer, these modules form a two-tiered ring in which each tier consists of homotypic AAA+ modules. By ATP binding and its hydrolysis at these AAA+ modules, ClpB/Hsp104 exerts the mechanical power required for protein disaggregation. Although ATPase cycle of this chaperone has been studied by several groups, an integrated understanding of this cycle has not been obtained because of the complexity of the mechanism and differences between species. To improve our understanding of the ATPase cycle, we prepared many ordered heterohexamers of ClpB from Thermus thermophilus, in which two subunits having different mutations were cross-linked to each other and arranged alternately and measured their nucleotide binding, ATP hydrolysis, and disaggregation abilities. The results indicated that the ATPase cycle of ClpB proceeded as follows: (i) the 12 AAA+ modules randomly bound ATP, (ii) the binding of four or more ATP to one AAA+ ring was sensed by a conserved Arg residue and converted another AAA+ ring into the ATPase-active form, and (iii) ATP hydrolysis occurred cooperatively in each ring. We also found that cooperative ATP hydrolysis in at least one ring was needed for the disaggregation activity of ClpB.
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