Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network

Protein folding and oligomeric complex assembly are essential for protein homeostasis. These processes are orchestrated by a network of host chaperones that interact with nascent and formed polypeptides. We investigated the mechanism by which a ubiquitous, essential, molecular chaperone, TRiC, folds an aggregation-prone protein subunit of a viral capsid. Structural studies, mass spectrometry, and in vitro folding and assembly experiments provided insights into the mechanism by which TRiC, in cooperation with a cochaperone, prefoldin, folds and assembles protein multimers. As the principles of protein folding and assembly are evolutionarily conserved, these findings likely point to common functions for TRiC and prefoldin in assembling a diversity of intracellular protein complexes.