How TriC folds tricky proteins.


Author: Zhuravleva A1, Radford SE2.

Affiliation: 1Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK. Electronic address: a.zhuravleva@leeds.ac.uk. 2Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, UK. Electronic address: s.e.radford@leeds.ac.uk.
Conference/Journal: Cell
Date published: 2014 Dec 4
Other:
 Volume ID: 159   ,  Issue ID: 6   ,  Pages: 1251-2   ,  Special Notes: doi: 10.1016/j.cell.2014.11.029   ,  Word Count: 94  
    Abstract

How chaperonins orchestrate the successful folding of even the most elaborate of proteins is a question of central importance. In two recent studies in Cell by Joachimiak et al. and Freund et al., a new class of TRiC substrate is identified, and how the chaperonin exploits its different subunits to extend its substrate repertoire and direct productive folding is revealed.

Copyright © 2014 Elsevier Inc. All rights reserved.

Comment on

The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT. [Cell. 2014]

Proteostatic control of telomerase function through TRiC-mediated folding of TCAB1. [Cell. 2014]

PMID: 25480290