Projects per year
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.
|Number of pages||5|
|Journal||Biochemical Society Transactions|
|Early online date||19 Jan 2011|
|Publication status||Published - Feb 2011|
|Event||Molecular Biology of Archaea II - Robinson College, Cambridge, United Kingdom|
Duration: 16 Aug 2010 → 18 Aug 2010
- heat shock
- molecular chaperone
- protein folding
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- 1 Finished
1/08/07 → 30/09/10
Project: Research Councils