Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.
Efficient de novo folding of actins and tubulins requires two molecular chaperones, the chaperonin TRiC (or CCT) and its novel cofactor GimC (or prefoldin). Recent studies indicate that TRiC is exquisitely adapted for this task, yet has the ability to interact with and assist the folding of numerous other cellular proteins.
Leroux
M R
MR
Department of Cellular Biochemistry, Max-Planck-Institut für Biochemie, Martinsried, D-82152, Germany.
Hartl
F U
FU
D056404:Chaperonin Containing TCP-1; D018833:Chaperonins / Q000145:classification / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism*; D008962:Models, Theoretical; D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding
D018832:Molecular Chaperones; C112806:prefoldin; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins