title: F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis.
abstract: 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 (F0c) into inner membrane vesicles requires YidC. Insertion is independent of the proton motive force, and proteoliposomes containing only YidC catalyze the membrane insertion of F0c 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 F0c. In conclusion, a novel membrane protein insertion pathway in E. coli is described in which YidC plays an exclusive role.
authors.affiliation: Dept. of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, Netherlands.
authors.forename: Martin
authors.initials: M
authors.lastname: van der Laan
authors.forename: Philipp
authors.initials: P
authors.lastname: Bechtluft
authors.forename: Stef
authors.initials: S
authors.lastname: Kol
authors.forename: Nico
authors.initials: N
authors.lastname: Nouwen
authors.forename: Arnold J M
authors.initials: AJ
authors.lastname: Driessen
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism*; D008081:Liposomes / Q000737:chemistry / Q000378:metabolism; D046911:Macromolecular Substances; D008564:Membrane Potentials; D008565:Membrane Proteins / Q000096:biosynthesis*; D026901:Membrane Transport Proteins / Q000378:metabolism*; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000378:metabolism*; D011522:Protons; D000069816:SEC Translocation Channels; D000081416:SecA Proteins; D018271:Signal Recognition Particle / Q000378:metabolism; D022161:Transport Vesicles / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008081:Liposomes; D046911:Macromolecular Substances; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D021122:Protein Subunits; D011522:Protons; D000069816:SEC Translocation Channels; D018271:Signal Recognition Particle; C412443:YIDC protein, E coli; D000251:Adenosine Triphosphatases; C474451:F1F0-ATP synthase; D025261:Mitochondrial Proton-Translocating ATPases; D000081416:SecA Proteins