Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits Journal Article
| Authors: | Frydman, J.; Nimmesgern, E.; Erdjument-Bromage, H.; Wall, J. S.; Tempst, P.; Hartl, F. U. |
| Article Title: | Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits |
| 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 specirlc aspects. |
| Keywords: | nonhuman; proteins; animal; animal tissue; protein protein interaction; luciferase; protein binding; enzyme activation; in vitro study; nuclear proteins; bacterial proteins; amino acid sequence; molecular sequence data; sequence homology, amino acid; eukaryota; cattle; adenosine triphosphate; protein subunit; protein folding; protein family; tubulin; cytosol; electrophoresis, polyacrylamide gel; firefly luciferase; beetles; heat-shock proteins; protein denaturation; chaperonins; male; priority journal; article; support, u.s. gov't, p.h.s.; adenosinetriphosphatase; chaperonin; microscopy, electron, scanning transmission; groel protein; t-complex polypeptide |
| Journal Title: | EMBO Journal |
| Volume: | 11 |
| Issue: | 13 |
| ISSN: | 0261-4189 |
| Publisher: | Wiley Blackwell |
| Date Published: | 1992-12-01 |
| Start Page: | 4767 |
| End Page: | 4778 |
| Language: | English |
| PUBMED: | 1361170 |
| PROVIDER: | scopus |
| PMCID: | PMC556952 |
| DOI: | 10.1002/j.1460-2075.1992.tb05582.x |
| DOI/URL: | |
| Notes: | Article -- Export Date: 30 July 2019 -- Source: Scopus |
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