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Title: The Mechanism and Function of Group II Chaperonins

Abstract

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:
Research Org.:
Stanford Univ., CA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1440550
Alternate Identifier(s):
OSTI ID: 1246436
Grant/Contract Number:  
SC0008504
Resource 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
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Lopez, Tom, Dalton, Kevin, and Frydman, Judith. The Mechanism and Function of Group II Chaperonins. United States: N. p., 2015. Web. doi:10.1016/j.jmb.2015.04.013.
Lopez, Tom, Dalton, Kevin, & Frydman, Judith. The Mechanism and Function of Group II Chaperonins. United States. doi:10.1016/j.jmb.2015.04.013.
Lopez, Tom, Dalton, Kevin, and Frydman, Judith. Thu . "The Mechanism and Function of Group II Chaperonins". United States. doi:10.1016/j.jmb.2015.04.013. https://www.osti.gov/servlets/purl/1440550.
@article{osti_1440550,
title = {The Mechanism and Function of Group II Chaperonins},
author = {Lopez, Tom and Dalton, Kevin and Frydman, Judith},
abstractNote = {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.},
doi = {10.1016/j.jmb.2015.04.013},
journal = {Journal of Molecular Biology},
number = 18,
volume = 427,
place = {United States},
year = {2015},
month = {4}
}

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Works referencing / citing this record:

On the nature of the optimal form of the holdase‐type chaperone stress response
journal, August 2019


Heat shock response in archaea
journal, November 2018

  • Lemmens, Liesbeth; Baes, Rani; Peeters, Eveline
  • Emerging Topics in Life Sciences, Vol. 2, Issue 4
  • DOI: 10.1042/etls20180024

On the nature of the optimal form of the holdase‐type chaperone stress response
journal, August 2019


Heat shock response in archaea
journal, November 2018

  • Lemmens, Liesbeth; Baes, Rani; Peeters, Eveline
  • Emerging Topics in Life Sciences, Vol. 2, Issue 4
  • DOI: 10.1042/etls20180024