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

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract Stress-specific activation of the chaperone Hsp33 requires the unfolding of a central linker region. This activation mechanism suggests an intriguing functional relationship between the chaperone’s own partial unfolding and its ability to bind other partially folded client proteins. However, identifying where Hsp33 binds its clients has remained a major gap in our understanding of Hsp33’s working mechanism. By using site-specific Fluorine-19 nuclear magnetic resonance experiments guided by in vivo crosslinking studies, we now reveal that the partial unfolding of Hsp33’s linker region facilitates client binding to an amphipathic docking surface on Hsp33. Furthermore, our results provide experimental evidence for the direct involvement of conditionally disordered regions in unfolded protein binding. The observed structural similarities between Hsp33’s own metastable linker region and client proteins present a possible model for how Hsp33 uses protein unfolding as a switch from self-recognition to high-affinity client binding.

Date: 2016
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DOI: 10.1038/ncomms10357

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