ReviewFrontiers in molecular biosciences2017
Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.
Review in Frontiers in molecular biosciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- A stochastic mechanism drives fast substrate translocation in the AAA+ machine ClpB.Nature communications · 2026Article
- Quantitative insights into processivity of an Hsp100 protein disaggregase on folded proteins.Biophysical journal · 2025Article
- Single turnover transient state kinetics reveals processive protein unfolding catalyzed byeLife · 2024Article
- Directed evolution of material-producing microorganisms.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024Review
- Bioinformatic identification of ClpI, a distinct class of Clp unfoldases in Actinomycetota.Frontiers in microbiology · 2023Article
- Cytoplasmic molecular chaperones in Pseudomonas species.Journal of microbiology (Seoul, Korea) · 2022Review
- Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022Review
- General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021Article
- Biochemical characterization of ClpB3, a chloroplastic disaggregase from Arabidopsis thaliana.Plant molecular biology · 2020Article
- 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
- Kinetic Analysis of AAA+ Translocases by Combined Fluorescence and Anisotropy Methods.Biophysical journal · 2020Article
- Proteomic analyses unraveling water stress response in two Eucalyptus species originating from contrasting environments for aridity.Molecular biology reports · 2020Article
- Crossing the Vacuolar Rubicon: Structural Insights into Effector Protein Trafficking in Apicomplexan Parasites.Microorganisms · 2020Review
- Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.Nature structural & molecular biology · 2020Article
- Structural and kinetic basis for the regulation and potentiation of Hsp104 function.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP-dependent substrate translocation.Protein science : a publication of the Protein Society · 2020Review
- Protein aggregation in bacteria.FEMS microbiology reviews · 2020Review
- Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.Cold Spring Harbor perspectives in biology · 2019Review
- Tunable microsecond dynamics of an allosteric switch regulate the activity of a AAA+ disaggregation machine.Nature communications · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellular proteostasis involves not only the expression of proteins in response to environmental needs, but also the timely repair or removal of damaged or unneeded proteins. AAA+ motor proteins are critically involved in these pathways. Here, we review the structure and function of AAA+ proteins ClpA, ClpB, and Hsp104. ClpB and Hsp104 rescue damaged proteins from toxic aggregates and do not partner with any protease. ClpA functions as the regulatory component of the ATP dependent protease complex ClpAP, and also remodels inactive RepA dimers into active monomers in the absence of the protease. Because ClpA functions both with and without a proteolytic component, it is an ideal system for developing strategies that address one of the major challenges in the study of protein remodeling machines: how do we observe a reaction in which the substrate protein does not undergo covalent modification? Here, we review experimental designs developed for the examination of polypeptide translocation catalyzed by the AAA+ motors in the absence of proteolytic degradation. We propose that transient state kinetic methods are essential for the examination of elementary kinetic mechanisms of these motor proteins. Furthermore, rigorous kinetic analysis must also account for the thermodynamic properties of these complicated systems that reside in a dynamic equilibrium of oligomeric states, including the biologically active hexamer.
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