Abstract

Research Article1 December 1992free access Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. J. Frydman J. Frydman Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author E. Nimmesgern E. Nimmesgern Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author H. Erdjument-Bromage H. Erdjument-Bromage Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author J.S. Wall J.S. Wall Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author P. Tempst P. Tempst Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author F.U. Hartl F.U. Hartl Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author J. Frydman J. Frydman Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author E. Nimmesgern E. Nimmesgern Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author H. Erdjument-Bromage H. Erdjument-Bromage Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author J.S. Wall J.S. Wall Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author P. Tempst P. Tempst Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author F.U. Hartl F.U. Hartl Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. Search for more papers by this author Author Information J. Frydman1, E. Nimmesgern1, H. Erdjument-Bromage1, J.S. Wall1, P. Tempst1 and F.U. Hartl1 1Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021. The EMBO Journal (1992)11:4767-4778https://doi.org/10.1002/j.1460-2075.1992.tb05582.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info 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. Previous ArticleNext Article Volume 11Issue 131 December 1992In this issue RelatedDetailsLoading ...