Insights into chaperonin function from studies on archaeal thermosomes.

Peter Lund*

*Corresponding author for this work

Research output: Contribution to journalConference articlepeer-review

8 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)94-98
Number of pages5
JournalBiochemical Society Transactions
Issue number1
Early online date19 Jan 2011
Publication statusPublished - Feb 2011
EventMolecular Biology of Archaea II - Robinson College, Cambridge, United Kingdom
Duration: 16 Aug 201018 Aug 2010


  • archaeon
  • chaperonin
  • heat shock
  • molecular chaperone
  • protein folding
  • thermosome


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