The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli

Cell Reports
Liang ZhaoF Ulrich Hartl

Abstract

Stress-inducible molecular chaperones have essential roles in maintaining protein homeostasis, but the extent to which they affect overall proteome stability remains unclear. Here, we analyze the effects of the DnaK (Hsp70) system on protein stability in Escherichia coli using pulse proteolysis combined with quantitative proteomics. We quantify ∼1,500 soluble proteins and find ∼500 of these to be protease sensitive under normal growth conditions, indicating a high prevalence of conformationally dynamic proteins, forming a metastable subproteome. Acute heat stress results in the unfolding of an additional ∼200 proteins, reflected in the exposure of otherwise buried hydrophobic regions. Overexpression of the DnaK chaperone system markedly stabilizes numerous thermo-sensitive proteins, including multiple ribosomal proteins and large, hetero-oligomeric proteins containing the evolutionarily ancient c.37 fold (P loop nucleoside triphosphate hydrolases). Thus, the Hsp70 system, in addition to its known chaperone functions, has a remarkable capacity to stabilize proteins in their folded states under denaturing stress conditions.

Citations

Dec 18, 2019·ELife·Salvatore AssenzaAlessandro Barducci
Aug 4, 2020·Biological Chemistry·Verena Kohler, Claes Andréasson
Nov 5, 2019·Current Opinion in Structural Biology·Rodrigo GallardoSheena E Radford
Apr 13, 2021·FEMS Microbiology Reviews·Sara Restrepo-PinedaMauricio A Trujillo-Roldán
Jun 10, 2021·Molecular Cell·Liang ZhaoF Ulrich Hartl
Jun 12, 2021·Frontiers in Molecular Biosciences·Jiří KoubekGünter Kramer
Nov 18, 2021·Journal of the American Chemical Society·Nirnay SamantaSimon Ebbinghaus
Oct 15, 2020·Structure·Sebastian Pechmann

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