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A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL.

Authors
Type
Published Article
Journal
The Journal of biological chemistry
Publication Date
Volume
267
Issue
36
Pages
25672–25675
Identifiers
PMID: 1361186
Source
Medline
License
Unknown

Abstract

To facilitate folding and assembly of different proteins, chaperonin GroEL requires the presence of its helper protein GroES. Using a photochemical cross-linking approach, we show that GroES and newly synthesized pre-beta-lactamase (pre-beta lac) contact with each other only within the ternary complex with GroEL. Possibly owing to this contact GroES is able to directly influence the pre-beta lac/GroEL interaction. Furthermore, the cross-linking of pre-beta lac to GroES suggests that the binding of the protein ligands to GroEL occurs near the GroES binding site, known to be in the central hole space of GroEL.

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