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

Zhao, L., Vecchi, G., Vendruscolo, M., Körner, R., Hayer-Hartl, M., & Hartl, F. U. (2019). The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome in E. coli. CELL REPORTS, 28(5), 1335-1345.e1-e6. doi:10.1016/j.celrep.2019.06.081.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-8867-E Version Permalink: http://hdl.handle.net/21.11116/0000-0005-8868-D
Genre: Journal Article

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 Creators:
Zhao, Liang1, Author              
Vecchi, Giulia2, Author
Vendruscolo, Michele2, Author
Körner, Roman1, Author              
Hayer-Hartl, Manajit3, Author              
Hartl, F. Ulrich1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2external, ou_persistent22              
3Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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Free keywords: ESCHERICHIA-COLI; PROTEOME-WIDE; PULSE PROTEOLYSIS; TRIGGER FACTOR; IN-VIVO; DNAK; PROTEINS; IDENTIFICATION; AGGREGATION; FRACTIONATIONCell Biology;
 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 similar to 1,500 soluble proteins and find similar to 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 similar to 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.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: CELL REPORTS
Source Genre: Journal
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Publ. Info: 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 28 (5) Sequence Number: - Start / End Page: 1335 - 1345.e1-e6 Identifier: ISSN: 2211-1247