Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL-Reference-Cited by-同舟云学术

Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL

Published:2021-02-23 Issue:1 Volume:12 Page:
ISSN:2150-7511
Container-title:mBio
language:en
Short-container-title:mBio

Author:

Sivinski Jared¹,Ambrose Andrew J.¹,Panfilenko Iliya¹,Zerio Christopher J.¹,Machulis Jason M.¹,Mollasalehi Niloufar²³⁴,Kaneko Lynn K.¹,Stevens Mckayla⁵,Ray Anne-Marie⁵,Park Yangshin⁵⁶⁷,Wu Chunxiang⁵⁶⁷,Hoang Quyen Q.⁵⁶⁷,Johnson Steven M.⁵,Chapman Eli¹^ORCID

Affiliation:

1. Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, Tucson, Arizona, USA

2. Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona, USA

3. Center for Innovation in Brain Science, Tucson, Arizona, USA

4. Department of Pharmacology, College of Medicine, University of Arizona, Tucson, Arizona, USA

5. Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA

6. Stark Neurosciences Research Institute, Indiana University School of Medicine, Indianapolis, Indiana, USA

7. Department of Neurology, Indiana University School of Medicine, Indianapolis, Indiana, USA

Abstract

The GroES/GroEL chaperonin from E. coli has long served as the model system for other chaperonins. This assumption seemed valid because of the high conservation between the chaperonins.

Funder

HHS | NIH | OSC | Common Fund

Publisher

American Society for Microbiology

Subject

Virology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/mBio.02167-20

Reference51 articles.

1. Unfolded DapA forms aggregates when diluted into free solution, confounding comparison with folding by the GroEL/GroES chaperonin system

2. Molecular Chaperones: Opening and closing the Anfinsen cage

3. Purification and properties of groE, a host protein involved in bacteriophage assembly