The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

Martin, J.; Mayhew, M.; Langer, T.; Hartl, F. U.

doi:10.1038/366228a0

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The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding

Martin, J., Mayhew, M., Langer, T., & Hartl, F. U. (1993). The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature, 366(6452), 228-33. doi:10.1038/366228a0.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-6FC5-B Version Permalink: https://hdl.handle.net/21.11116/0000-000B-6FC6-A

Genre: Journal Article

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https://www.ncbi.nlm.nih.gov/pubmed/7901770 (Any fulltext) Open Access status unknown

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Martin, J., Author
Mayhew, M., Author
Langer, T.¹, Author
Hartl, F. U., Author

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1Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_3393994

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Free keywords: Adenosine Diphosphate/metabolism Adenosine Triphosphate/metabolism Bacterial Proteins/*metabolism Chaperonin 10 Chaperonin 60 Cross-Linking Reagents Escherichia coli/metabolism Heat-Shock Proteins/*metabolism Models, Biological Nucleotides/metabolism Protein Binding *Protein Folding Succinimides

Abstract: The reaction mechanism of protein folding by the chaperonin GroEL and its regulator GroES has been defined. GroES and substrate protein counteract each other's effects on GroEL: whereas GroES stabilizes GroEL in the ADP-bound state, binding of unfolded polypeptide within the cavity of the GroEL cylinder triggers ADP and GroES release. Upon ADP-ATP exchange, GroES reassociates with GroEL and ATP hydrolysis discharges the bound protein for folding. Partially folded protein rebinds to the chaperonin, thus perpetuating the cycle until folding is complete.

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Dates: Published Online: 1993-11-18Date issued: 1993-11-18

Publication Status: Issued

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Identifiers: Other: 7901770
DOI: 10.1038/366228a0
ISSN: 0028-0836 (Print)0028-0836 (Linking)

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Title: Nature

Source Genre: Journal

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Pages: - Volume / Issue: 366 (6452) Sequence Number: - Start / End Page: 228 - 33 Identifier: -