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DsbA is a redox-switchable mechanical chaperone

Published:2021 Issue:33 Volume:12 Page:11109-11120
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Eckels Edward C.¹²,Chaudhuri Deep³,Chakraborty Soham³,Echelman Daniel J.¹,Haldar Shubhasis³^ORCID

Affiliation:

1. Department of Biological Sciences, Columbia University, New York, NY 10027, USA

2. Department of Internal Medicine, Columbia University Medical Center, New York, NY 10032, USA

3. Department of Biological Sciences, Ashoka University, Sonepat, Haryana 131029, India

Abstract

Protein translocation is facilitated by DsbA chaperone in a redox-dependent manner.

Funder

Science and Engineering Research Board

Department of Biotechnology, Ministry of Science and Technology

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/SC/D1SC03048E

Reference67 articles.

1. Detecting Folding Intermediates of a Protein as It Passes through the Bacterial Translocation Channel

2. Translocation of botulinum neurotoxin light chain protease through the heavy chain channel

3. Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane—Distinct translocases and mechanisms

4. Virulence factor secretion and translocation by Bordetella species

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1. Force‐regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ;Protein Science;2024-06-12

2. Elucidating the novel mechanisms of molecular chaperones by single-molecule technologies;Trends in Biochemical Sciences;2024-01

3. Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ: explained by strain energy;2023-05-02

4. Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ: explained by strain energy;2023-03-16

5. Single-molecule mechanical studies of chaperones and their clients;Biophysics Reviews;2022-12

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