Insights into the intra-ring subunit order of TRiC/CCT: a structural and evolutionary analysis.

ABSTRACT: TRiC is an important group II chaperonin that facilitates the folding of many eukaryotic proteins. The TRiC complex consists of two stacked rings, each comprised of eight paralogous subunits with a mutual sequence identity of 30-35%. Each subunit has unique functional roles that are manifested by corresponding sequence conservation. It is generally assumed that the subunit order within each ring is fixed, but this order is still uncertain. Here we address the problem of the intra-ring subunit order by combining two sources of information: evolutionary conservation and a structural hypothesis. Specifically, we identify residues in the TRiC subunits that are likely to be part of the intra-unit interface, based on homology modeling to the solved thermosome structure. Within this set of residu

SUBMITTER: Kalisman N 

PROVIDER: S-EPMC4033405 | biostudies-literature | 2010

REPOSITORIES: biostudies-literature