Sequential allosteric mechanism of ATP hydrolysis by the CCT/TRiC chaperone is revealed through Arrhenius analysis
Open accessAbstract
Knowing the mechanism of allosteric switching is important for understanding how molecular machines work. The CCT/TRiC chaperonin nanomachine undergoes ATP-driven conformational changes that are crucial for its folding function. Here, we demonstrate that insight into its allosteric mechanism of ATP hydrolysis can be achieved by Arrhenius analysis. Our results show that ATP hydrolysis triggers sequential ‟conformational waves." They also suggest that these waves start from subunits CCT6 and CCT8 (or CCT3 and CCT6) and proceed clockwise and counterclockwise, respectively.
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The intraring conformational changes in CCT/TRiC associated with ATP hydrolysis are sequential.
“A different approach based on an Arrhenius analysis of ATP hydrolysis by the group II chaperonin CCT/ TRiC, the eukaryotic homolog of GroEL, revealed that the intraring conformational changes in this protein associated with ATP hydrolysis are sequential (Gruber et al., 2017).”
From Allostery in Its Many Disguises: From Theory to Applications (2019) · cites this paper as Gruber et al., 2017
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Allostery in Its Many Disguises: From Theory to Applications
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- Authors
- Gruber, R., Levitt, M., & Horovitz, A.
- Affiliations
- Weizmann Institute of Science (IL)
- Stanford Medicine (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-05
- Volume
- 114
- Issue
- 20
- Pages
- 5189-5194
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5441784
- OpenAlex
- W2610194091
- Cited by
- 25
- References
- 26
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 6 · 2017: 2
- FWCI
- 1.67
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Israel Science Foundation (158/12)
- NIH (GM1157490)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- ATP hydrolysis, allosteric mechanism, Arrhenius analysis, CCT8, CCT3, CCT6A, protein folding
- MeSH terms
- Adenosine Triphosphate, Allosteric Regulation, Hydrolysis, Models, Molecular, Protein Conformation, Saccharomyces cerevisiae, Protein Folding, Chaperonins, Protein Subunits, Saccharomyces cerevisiae Proteins, Chaperonin Containing TCP-1
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