title: Native architecture of the photosynthetic membrane from Rhodobacter veldkampii.
abstract: The photosynthetic membrane in purple bacteria contains several pigment-protein complexes that assure light capture and establishment of the chemiosmotic gradient. The bioenergetic tasks of the photosynthetic membrane require the strong interaction between these various complexes. In the present work, we acquired the first images of the native outer membrane architecture and the supramolecular organization of the photosynthetic apparatus in vesicular chromatophores of Rhodobacter (Rb.) veldkampii. Mixed with LH2 (light-harvesting complex 2) rings, the PufX-containing LH1-RC (light-harvesting complex 1--reaction center) core complexes appear as C-shaped monomers, with random orientations in the photosynthetic membrane. Within the LH1 fence surrounding the RC, a remarkable gap that is probably occupied (or partially occupied) by PufX is visualized. Sequence alignment revealed that one specific region in PufX may be essential for PufX-induced core dimerization. In this region of ten amino acids in length all Rhodobacter species had five conserved amino acids, with the exception of Rb. veldkampii. Our findings provide direct evidence that the presence of PufX in Rb. veldkampii does not directly govern the dimerization of LH1-RC core complexes in the native membrane. It is indicated, furthermore, that the high membrane curvature of Rb. veldkampii chromatophores (Rb. veldkampii features equally small vesicular chromatophores alike Rb. sphaeroides) is not due to membrane bending induced by dimeric RC-LH1-PufX cores, as it has been proposed in Rb. sphaeroides.
authors.affiliation: Institut Curie, U1006 INSERM, UMR168 CNRS, 26 Rue d'Ulm, 75248 Paris, France.
authors.forename: Lu-Ning
authors.initials: LN
authors.lastname: Liu
authors.forename: James N
authors.initials: JN
authors.lastname: Sturgis
authors.forename: Simon
authors.initials: S
authors.lastname: Scheuring
mesh_terms: D000595:Amino Acid Sequence; D020130:Bacterial Chromatophores / Q000648:ultrastructure*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D019281:Dimerization; D007425:Intracellular Membranes / Q000648:ultrastructure*; D045342:Light-Harvesting Protein Complexes / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D008969:Molecular Sequence Data; D045322:Photosynthetic Reaction Center Complex Proteins / Q000648:ultrastructure*; D016992:Rhodobacter / Q000166:cytology*; D016415:Sequence Alignment; D013045:Species Specificity; D013057:Spectrum Analysis
chemical_list: D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; C088749:PufX protein, Rhodobacter