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Single-Ring Intermediates Are Essential for Some Chaperonins.

Jay M Bhatt1, Adrian S Enriquez1, Jinliang Wang1

  • 1Department of Chemistry, The University of Texas at El Paso, El Paso, TX, United States.

Frontiers in Molecular Biosciences
|May 15, 2018
PubMed
Summary
This summary is machine-generated.

Chaperonins assist protein folding. This review highlights how double-ring chaperonins form single-ring intermediates, crucial for protein folding, especially in bacteriophage systems.

Keywords:
GroELHSP60chaperoninsphiELprotein foldingsingle-ring chaperonins

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Chaperonins are essential molecular machines aiding protein folding across all life forms.
  • Traditionally classified into two groups, their mechanisms are continually being elucidated.
  • Conformational intermediates play a key role in the chaperonin-mediated protein-folding pathway.

Purpose of the Study:

  • To review chaperonins capable of forming double- and single-ring conformational intermediates.
  • To discuss the structural, functional, and biological significance of these single-ring intermediates.
  • To highlight unique chaperonins like ϕ-EL and OBP with mixed group characteristics.

Main Methods:

  • Literature review of existing studies on chaperonin structure and function.
  • Analysis of reported conformational intermediates in protein-folding pathways.
  • Comparative discussion of different chaperonin systems, including bacterial and viral.

Main Results:

  • Several chaperonins, including bacteriophage ϕ-EL and OBP, human mitochondrial chaperonin, and bacterial GroEL/ES, form single-ring intermediates.
  • These double-ring chaperonins can dissociate into functional single-ring structures.
  • Single-ring intermediates possess independent protein-folding capabilities.

Conclusions:

  • Single-ring intermediates are functionally relevant intermediates in the chaperonin catalytic cycle.
  • The ϕ-EL and OBP chaperonins exhibit characteristics of both Group I and Group II chaperonins.
  • Understanding these intermediates provides deeper insights into cellular protein homeostasis and folding mechanisms.