Successive action of DnaK, DnaJ and GroEL along the pathway of 
chaperone-mediated protein folding

Langer, T.; Lu, C.; Echols, H.; Flanagan, J.; Hayer, M. K.; Hartl, F. U.

doi:10.1038/356683a0

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Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M. K., & Hartl, F. U. (1992). Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature, 356(6371), 683-9. doi:10.1038/356683a0.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-6FAA-A Version Permalink: https://hdl.handle.net/21.11116/0000-000B-6FAB-9

Genre: Journal Article

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https://www.ncbi.nlm.nih.gov/pubmed/1349157 (Any fulltext) Open Access status unknown

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Creators:
Langer, T.¹, Author
Lu, C., Author
Echols, H., Author
Flanagan, J., Author
Hayer, M. K., 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: *Bacterial Proteins/*pharmacology Chaperonin 60 Chromatography, Gel Dose-Response Relationship, Drug Escherichia coli *Escherichia coli Proteins HSP40 Heat-Shock Proteins *HSP70 Heat-Shock Proteins *Heat-Shock Proteins/*pharmacology In Vitro Techniques Models, Biological Protein Conformation/*drug effects *Thiosulfate Sulfurtransferase/drug effects

Abstract: The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding polypeptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. Dependent on GrpE and ATP hydrolysis, the protein is then transferred to GroEL (heat-shock protein 60) which acts catalytically in the production of the native state. This sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides.

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Dates: Published Online: 1992-04-23Date issued: 1992-04-23

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Identifiers: Other: 1349157
DOI: 10.1038/356683a0
ISSN: 0028-0836 (Print)0028-0836 (Linking)

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Title: Nature

Source Genre: Journal

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Pages: - Volume / Issue: 356 (6371) Sequence Number: - Start / End Page: 683 - 9 Identifier: -