Ontology highlight
ABSTRACT:
SUBMITTER: Jaru-Ampornpan P
PROVIDER: S-EPMC2917185 | biostudies-literature | 2010 Jun
REPOSITORIES: biostudies-literature
Jaru-Ampornpan Peera P Shen Kuang K Lam Vinh Q VQ Ali Mona M Doniach Sebastian S Jia Tony Z TZ Shan Shu-Ou SO
Nature structural & molecular biology 20100427 6
Membrane proteins impose enormous challenges to cellular protein homeostasis during their post-translational targeting, and they require chaperones to keep them soluble and translocation competent. Here we show that a novel targeting factor in the chloroplast signal recognition particle (cpSRP), cpSRP43, is a highly specific molecular chaperone that efficiently reverses the aggregation of its substrate proteins. In contrast to 'ATPases associated with various cellular activities' (AAA(+)) chaper ...[more]