Allosteric differences dictate GroEL complementation of E. coli. Issue 3 (24th February 2022)

• Record Type: Journal Article
• Authors: Sivinski, Jared; Ngo, Duc; Zerio, Christopher J.; Ambrose, Andrew J.; Watson, Edmond R.; Kaneko, Lynn K.; Kostelic, Marius M.; Stevens, Mckayla; Ray, Anne‐Marie; Park, Yangshin; Wu, Chunxiang; Marty, Michael T.; Hoang, Quyen Q.; Zhang, Donna D.; Lander, Gabriel C.; Johnson, Steven M.; Chapman, Eli
• Is Part Of: FASEB journal. Volume 36:Issue 3(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-02-24
• Subjects: allostery -- chaperone -- chaperonin -- ESKAPE -- GroEL -- GroES; Biology -- Periodicals; Biology, Experimental -- Periodicals; 570
• DOI: 10.1096/fj.202101708RR
• Languages: English
• ISSNs: 0892-6638

Abstract

Abstract: 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.