Allosteric differences dictate GroEL complementation of E. coli.

Autor: Sivinski J; Department of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA., Ngo D; Department of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA., Zerio CJ; Department of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA., Ambrose AJ; Department of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA., Watson ER; Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, California, USA., Kaneko LK; Department of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA., Kostelic MM; Department of Chemistry and Biochemistry, The University of Arizona, Tucson, Arizona, USA., Stevens M; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA., Ray AM; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA., Park Y; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.; Stark Neurosciences Research Institute, Indiana University School of Medicine, Indianapolis, Indiana, USA.; Department of Neurology, Indiana University School of Medicine, Indianapolis, Indiana, USA., Wu C; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA., Marty MT; Department of Chemistry and Biochemistry, The University of Arizona, Tucson, Arizona, USA., Hoang QQ; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.; Stark Neurosciences Research Institute, Indiana University School of Medicine, Indianapolis, Indiana, USA.; Department of Neurology, Indiana University School of Medicine, Indianapolis, Indiana, USA., Zhang DD; Department of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA., Lander GC; Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, California, USA., Johnson SM; Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA., Chapman E; Department of Pharmacology and Toxicology, College of Pharmacy, The University of Arizona, Tucson, Arizona, USA.
Jazyk: angličtina
Zdroj: FASEB journal : official publication of the Federation of American Societies for Experimental Biology [FASEB J] 2022 Mar; Vol. 36 (3), pp. e22198.
DOI: 10.1096/fj.202101708RR
Abstrakt: GroES/GroEL is the only bacterial chaperone essential under all conditions, making it a potential antibiotic target. Rationally targeting ESKAPE GroES/GroEL as an antibiotic strategy necessitates studying their structure and function. Herein, we outline the structural similarities between Escherichia coli and ESKAPE GroES/GroEL and identify significant differences in intra- and inter-ring cooperativity, required in the refolding cycle of client polypeptides. Previously, we observed that one-half of ESKAPE GroES/GroEL family members could not support cell viability when each was individually expressed in GroES/GroEL-deficient E. coli cells. Cell viability was found to be dependent on the allosteric compatibility between ESKAPE and E. coli subunits within mixed (E. coli and ESKAPE) tetradecameric GroEL complexes. Interestingly, differences in allostery did not necessarily result in differences in refolding rate for a given homotetradecameric chaperonin. Characterization of ESKAPE GroEL allostery, ATPase, and refolding rates in this study will serve to inform future studies focused on inhibitor design and mechanism of action studies.
(© 2022 Federation of American Societies for Experimental Biology.)
Databáze: MEDLINE
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