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

Bastian Groitl; Scott Horowitz; Karl A. T. Makepeace; Evgeniy V. Petrotchenko; Christoph H. Borchers; Dana Reichmann; James C. A. Bardwell; Ursula Jakob

doi:10.1038/ncomms10357

Nature Communications (Jan 2016)

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

Bastian Groitl,
Scott Horowitz,
Karl A. T. Makepeace,
Evgeniy V. Petrotchenko,
Christoph H. Borchers,
Dana Reichmann,
James C. A. Bardwell,
Ursula Jakob

Affiliations

Bastian Groitl: Department of Molecular, Cellular and Developmental Biology, University of Michigan
Scott Horowitz: Department of Molecular, Cellular and Developmental Biology, University of Michigan
Karl A. T. Makepeace: Department of Biochemistry and Microbiology, Genome BC Proteomics Centre, University of Victoria
Evgeniy V. Petrotchenko: Department of Biochemistry and Microbiology, Genome BC Proteomics Centre, University of Victoria
Christoph H. Borchers: Department of Biochemistry and Microbiology, Genome BC Proteomics Centre, University of Victoria
Dana Reichmann: Department of Molecular, Cellular and Developmental Biology, University of Michigan
James C. A. Bardwell: Department of Molecular, Cellular and Developmental Biology, University of Michigan
Ursula Jakob: Department of Molecular, Cellular and Developmental Biology, University of Michigan

DOI: https://doi.org/10.1038/ncomms10357
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 12

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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