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
- 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.