Article
Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions.
The Journal of biological chemistry - 4 Aug 2000
Woodbury R L, Topping T B, Diamond D L, Suciu D, Kumamoto C A, Hardy S J, Randall L L
Abstract excerpt
During localization to the periplasmic space or to the outer membrane of Escherichia coli some proteins are dependent on binding to the cytosolic chaperone SecB, which in turn is targeted to the membrane by specific interaction with SecA, a peripheral component of the translocase. Five variant forms of SecB, previously demonstrated to be defective in mediating export in vivo (Gannon, P. M., and Kumamoto, C. A....
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.