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The Multifaceted Benefits of Protein Co-expression in Escherichia coli
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Allosteric differences dictate GroEL complementation of E. coli.

Jared Sivinski1, Duc Ngo1, Christopher J Zerio1

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

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|February 24, 2022
PubMed
Summary
This summary is machine-generated.

The essential bacterial GroES/GroEL chaperone is a potential antibiotic target. Differences in ESKAPE bacterial GroES/GroEL allostery impact cell viability and refolding, informing future drug design.

Keywords:
ESKAPEGroELGroESallosterychaperonechaperonin

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • GroES/GroEL is the sole essential bacterial chaperone, crucial for protein folding under all conditions.
  • Its essentiality makes it a prime target for novel antibiotic development.
  • Understanding ESKAPE pathogen GroES/GroEL variants is key for rational drug design.

Purpose of the Study:

  • To investigate structural and functional differences between Escherichia coli and ESKAPE GroES/GroEL.
  • To identify how variations in allosteric cooperativity affect client polypeptide refolding.
  • To inform the development of targeted inhibitors against ESKAPE GroES/GroEL.

Main Methods:

  • Comparative structural analysis of E. coli and ESKAPE GroES/GroEL.
  • Assessment of cell viability in GroES/GroEL-deficient E. coli expressing mixed chaperonin complexes.
  • Characterization of allosteric compatibility, ATPase activity, and refolding rates.

Main Results:

  • Significant differences in intra- and inter-ring cooperativity were found between E. coli and ESKAPE GroES/GroEL.
  • Cell viability depended on allosteric compatibility within mixed E. coli-ESKAPE GroEL complexes.
  • Allosteric variations did not always correlate with altered refolding rates in homotetradecameric chaperonins.

Conclusions:

  • Allosteric compatibility is critical for ESKAPE GroES/GroEL function in vivo.
  • Characterizing ESKAPE GroEL allostery and function provides a basis for inhibitor design.
  • This research aids in developing strategies to target essential bacterial chaperones.