Abstract:
: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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Lopez T,Dalton K,Frydman Jdoi
10.1016/j.jmb.2015.04.013subject
Has Abstractpub_date
2015-09-11 00:00:00pages
2919-30issue
18eissn
0022-2836issn
1089-8638pii
S0022-2836(15)00267-3journal_volume
427pub_type
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