It is now well understood that, although proteins fold spontaneously (in a thermodynamic sense), many nevertheless require the assistance of helpers called molecular chaperones to reach their correct and active folded state in living cells. This is because the pathways of protein folding are full of traps for the unwary: the forces that drive proteins into their folded states can also drive them into insoluble aggregates, and, particularly when cells are stressed, this can lead, without prevention or correction, to cell death. The chaperonins are a family of molecular chaperones, practically ubiquitous in all living organisms, which possess a remarkable structure and mechanism of action. They act as nanoboxes in which proteins can fold, isolated from their environment and from other partners with which they might, with potentially deleterious consequences, interact. The opening and closing of these boxes is timed by the binding and hydrolysis of ATP. The chaperonins which are found in bacteria are extremely well characterized, and, although those found in archaea (also known as thermosomes) and eukaryotes have received less attention, our understanding of these proteins is constantly improving. This short review will summarize what we know about chaperonin function in the cell from studies on the archaeal chaperonins, and show how recent work is improving our understanding of this essential class of molecular chaperones.
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February 2011
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Conference Article|
January 19 2011
Insights into chaperonin function from studies on archaeal thermosomes
Peter Lund
Peter Lund
1
1School of Biosciences, University of Birmingham, Birmingham B15 2TT, U.K.
1email lundpa@gmail.com
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Publisher: Portland Press Ltd
Received:
September 14 2010
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (1): 94–98.
Article history
Received:
September 14 2010
Citation
Peter Lund; Insights into chaperonin function from studies on archaeal thermosomes. Biochem Soc Trans 1 February 2011; 39 (1): 94–98. doi: https://doi.org/10.1042/BST0390094
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