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. 1992 Dec;11(13):4767–4778. doi: 10.1002/j.1460-2075.1992.tb05582.x

Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits.

J Frydman 1, E Nimmesgern 1, H Erdjument-Bromage 1, J S Wall 1, P Tempst 1, F U Hartl 1
PMCID: PMC556952  PMID: 1361170

Abstract

T-complex polypeptide 1 (TCP-1) was analyzed as a potential chaperonin (GroEL/Hsp60) equivalent of the eukaryotic cytosol. We found TCP-1 to be part of a hetero-oligomeric 970 kDa complex containing several structurally related subunits of 52-65 kDa. These members of a new protein family are assembled into a TCP-1 ring complex (TRiC) which resembles the GroEL double ring. The main function of TRiC appears to be in chaperoning monomeric protein folding: TRiC binds unfolded polypeptides, thereby preventing their aggregation, and mediates the ATP-dependent renaturation of unfolded firefly luciferase and tubulin. At least in vitro, TRiC appears to function independently of a small co-chaperonin protein such as GroES. Folding of luciferase is mediated by TRiC but not by GroEL/ES. This suggests that the range of substrate proteins interacting productively with TRiC may differ from that of GroEL. We propose that TRiC mediates the folding of cytosolic proteins by a mechanism distinct from that of the chaperonins in specific aspects.

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