F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesisvan der Laan, M., Bechtluft, P., Kol, S., Nouwen, N. & Driessen, A. J. M., 26-Apr-2004, In : Journal of Cell Biology. 165, 2, p. 213-222 10 p.
Research output: Contribution to journal › Article › Academic › peer-review
The Escherichia coli YidC protein belongs to the Oxa1 family of membrane proteins that have been suggested to facilitate the insertion and assembly of membrane proteins either in cooperation with the Sec translocase or as a separate entity. Recently, we have shown that depletion of YidC causes a specific defect in the functional assembly of F1F0 ATP synthase and cytochrome o oxidase. We now demonstrate that the insertion of in vitro-synthesized F1F0 ATP synthase Subunit c (F(0)c) into inner membrane vesicles requires YidC. Insertion is independent of the proton motive force, and proteoliposomes containing only YidC catalyze the membrane insertion of F(0)c in its native transmembrane topology whereupon it assembles into large oligomers. Co-reconstituted SecYEG has no significant effect on the insertion efficiency. Remarkably, signal recognition particle and its membrane-bound receptor FtsY are not required for the membrane insertion of F(0)c. In conclusion, a novel membrane protein insertion pathway in E. coli is described in which YidC plays an exclusive role.
|Number of pages||10|
|Journal||Journal of Cell Biology|
|Publication status||Published - 26-Apr-2004|
- YidC, F(1)F(0)ATP synthase, membrane insertion, membrane targeting, complex assembly, ESCHERICHIA-COLI, INNER MEMBRANE, TARGETING PATHWAY, SEC TRANSLOCASE, OXA1 COMPLEX, COAT PROTEIN, INSERTION, MITOCHONDRIA, OXIDASE, SIGNAL