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Title: The Mechanism and Function of Group II Chaperonins

We report protein folding in the cell requires the assistance of enzymes collectively called chaperones. Among these, the chaperonins are 1-MDa ring-shaped oligomeric complexes that bind unfolded polypeptides and promote their folding within an isolated chamber in an ATP-dependent manner. Group II chaperonins, found in archaea and eukaryotes, contain a built-in lid that opens and closes over the central chamber. In eukaryotes, the chaperonin TRiC/CCT is hetero-oligomeric, consisting of two stacked rings of eight paralogous subunits each. TRiC facilitates folding of approximately 10% of the eukaryotic proteome, including many cytoskeletal components and cell cycle regulators. Folding of many cellular substrates of TRiC cannot be assisted by any other chaperone. A complete structural and mechanistic understanding of this highly conserved and essential chaperonin remains elusive. However, recent work is beginning to shed light on key aspects of chaperonin function and how their unique properties underlie their contribution to maintaining cellular proteostasis.
Authors:
 [1] ;  [2] ;  [3]
  1. Stanford Univ., CA (United States). Department of Biology
  2. Stanford Univ., CA (United States). Biophysics Program
  3. Stanford Univ., CA (United States). Department of Biology and Department of Genetics
Publication Date:
Grant/Contract Number:
SC0008504
Type:
Accepted Manuscript
Journal Name:
Journal of Molecular Biology
Additional Journal Information:
Journal Volume: 427; Journal Issue: 18; Journal ID: ISSN 0022-2836
Publisher:
Elsevier
Research Org:
Stanford Univ., CA (United States)
Sponsoring Org:
USDOE
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES
OSTI Identifier:
1440550
Alternate Identifier(s):
OSTI ID: 1246436