Protein unfolding as a switch from self-recognition to high-affinity client binding

Protein unfolding as a switch from self-recognition to high-affinity client binding

Under stress conditions the molecular chaperone Hsp33 is activated to process unfolded proteins. Here, the authors use in vivo and in vitro crosslinking and 19F-NMR to elucidate the binding site for misfolded proteins and are able to propose a model for its mechanism of action.

Bibliographic Details
Main Authors: Bastian Groitl, Scott Horowitz, Karl A. T. Makepeace, Evgeniy V. Petrotchenko, Christoph H. Borchers, Dana Reichmann, James C. A. Bardwell, Ursula Jakob
Format: Article
Language:English
Published: Nature Publishing Group 2016-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms10357
Description
Summary:Under stress conditions the molecular chaperone Hsp33 is activated to process unfolded proteins. Here, the authors use in vivo and in vitro crosslinking and 19F-NMR to elucidate the binding site for misfolded proteins and are able to propose a model for its mechanism of action.
ISSN:2041-1723

Similar Items