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PMID: 1361169 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.

The EMBO journal ·Vol. 11 ·No. 13 ·1992-12-00 ·Pages 4757-65

Langer T, Pfeifer G, Martin J, Baumeister W, Hartl FU

Abstract

The mechanism of GroEL (chaperonin)-mediated protein folding is only partially understood. We have analysed structural and functional properties of the interaction between GroEL and the co-chaperonin GroES. The stoichiometry of the GroEL 14mer and the GroES 7mer in the functional holo-chaperonin is 1:1. GroES protects half of the GroEL subunits from proteolytic truncation of the approximately 50 C-terminal residues. Removal of this region results in an inhibition of the GroEL ATPase, mimicking the effect of GroES on full-length GroEL. Image analysis of electron micrographs revealed that GroES binding triggers conspicuous conformational changes both in the GroES adjacent end and at the opposite end of the GroEL cylinder. This apparently prohibits the association of a second GroES oligomer. Addition of denatured polypeptide leads to the appearance of irregularly shaped, stain-excluding masses within the GroEL double-ring, which are larger with bound alcohol oxidase (75 kDa) than with rhodanese (35 kDa). We conclude that the functional complex of GroEL and GroES is characterized by asymmetrical binding of GroES to one end of the GroEL cylinder and suggest that binding of the substrate protein occurs within the central cavity of GroEL.

MeSH Terms
Bacterial Proteins/chemistry,metabolism,ultrastructure Chaperonin 10 Chaperonin 60 Chromatography, Gel Electrophoresis, Polyacrylamide Gel Escherichia coli/metabolism Heat-Shock Proteins/chemistry,metabolism,ultrastructure Image Processing, Computer-Assisted Microscopy, Electron Protein Folding
Chemicals
Bacterial Proteins Chaperonin 10 Chaperonin 60 Heat-Shock Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Langer T
Cellular Biochemistry and Biophysics Program, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, N.Y. 10021.
Pfeifer G
Martin J
Baumeister W
Hartl F U
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1992-12-00
Pages
4757-65
Language
English
Region
England
NLM ID
8208664
PMCID
PMC556951
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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