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

Authors
  • Bochkareva, E S
  • Girshovich, A S
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Publication Date
Dec 25, 1992
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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