ArticleProtein science : a publication of the Protein Society2004
A mobile loop order-disorder transition modulates the speed of chaperonin cycling.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Structural interplay of the redox co-chaperone CnoX to GroEL/ES chaperonin.Life science alliance · 2026Article
- Suppressors ofInternational journal of molecular sciences · 2023Article
- Multicopy Suppressor Analysis of Strains Lacking Cytoplasmic Peptidyl-ProlylInternational journal of molecular sciences · 2020Article
- Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes.The Journal of biological chemistry · 2012Article
- An ORFan no more: the bacteriophage T4 39.2 gene product, NwgI, modulates GroEL chaperone function.Genetics · 2012Article
- Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin.PloS one · 2012Article
- Allosteric transitions of supramolecular systems explored by network models: application to chaperonin GroEL.PLoS computational biology · 2009Article
- Markov propagation of allosteric effects in biomolecular systems: application to GroEL-GroES.Molecular systems biology · 2006Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular machines order and disorder polypeptides as they form and dissolve large intermolecular interfaces, but the biological significance of coupled ordering and binding has been established in few, if any, macromolecular systems. The ordering and binding of GroES co-chaperonin mobile loops accompany an ATP-dependent conformational change in the GroEL chaperonin that promotes client protein folding. Following ATP hydrolysis, disordering of the mobile loops accompanies co-chaperonin dissociation, reversal of the GroEL conformational change, and release of the client protein. "High-affinity" GroEL mutants were identified by their compatibility with "low-affinity" co-chaperonin mutants and incompatibility with high-affinity co-chaperonin mutants. Analysis of binding kinetics using the intrinsic fluorescence of tryptophan-containing co-chaperonin variants revealed that excessive affinity causes the chaperonin to stall in a conformation that forms in the presence of ATP. Destabilizing the beta-hairpins formed by the mobile loops restores the normal rate of dissociation. Thus, the free energy of mobile-loop ordering and disordering acts like the inertia of an engine's flywheel by modulating the speed of chaperonin conformational changes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.