Allosteric Mechanisms in Chaperonin Machines

Ranit Gruber, Amnon Horovitz

Research output: Contribution to journalArticlepeer-review


Chaperonins are nanomachines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space owing to complex allosteric regulation. They consist of two back-to-back stacked oligomeric rings with a cavity at each end where protein substrate folding can take place. Here, we focus on the GroEL/GroES chaperonin system from Escherichia coli and, to a lesser extent, on the more poorly characterized eukaryotic chaperonin CCT/TRiC. We describe their various functional (allosteric) states and how they are affected by substrates and allosteric effectors that include ATP, ADP, nonfolded protein substrates, potassium ions, and GroES (in the case of GroEL). We also discuss the pathways of intra- and inter-ring allosteric communication by which they interconvert and the coupling between allosteric transitions and protein folding reactions.
Original languageEnglish
Article number26726755
Pages (from-to)6588-6606
Number of pages19
JournalChemical Reviews
Issue number11
StatePublished - Jan 2016


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