A Stutter in the Coiled-Coil Domain of Escherichia coli Co-chaperone GrpE Connects Structure with Function-Reference-Cited by-同舟云学术

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A Stutter in the Coiled-Coil Domain of Escherichia coli Co-chaperone GrpE Connects Structure with Function

Published:2021-04-21 Issue:17 Volume:60 Page:1356-1367
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Upadhyay Tulsi¹,Potteth Upasana S.¹,Karekar Vaibhav V.²,Saraogi Ishu¹²^ORCID

Affiliation:

1. Department of Biological Sciences, Indian Institute of Science Education and Research Bhopal, Bhopal Bypass Road, Bhauri, Bhopal 462066, MP, India

2. Department of Chemistry, Indian Institute of Science Education and Research Bhopal, Bhopal Bypass Road, Bhauri, Bhopal 462066, MP, India

Funder

Science and Engineering Research Board

Indian Institute of Science Education and Research Bhopal

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00110

Reference69 articles.

1. The Hsp70 chaperone network

2. Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones

3. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.

4. Tuning of DnaK Chaperone Action by Nonnative Protein Sensor DnaJ and Thermosensor GrpE

5. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.

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