201. Evidence for a Role of VIPP1 in the Structural Organization of the Photosynthetic Apparatus in Chlamydomonas
- Author
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Ann-Katrin Unger, Frederik Sommer, Stefan Geimer, Stefan Schmollinger, Mark Rütgers, André Nordhues, Anja Krieger-Liszkay, Barbara Soppa, Heiko Lokstein, Stephanie Schönfelder, Michael Schroda, Mark Aurel Schöttler, Giovanni Finazzi, Thomas Roach, Timo Mühlhaus, José L. Crespo, Max Planck Institute of Molecular Plant Physiology (MPI-MP), Max-Planck-Gesellschaft, Zellbiologie/Elektronenmikroskopie, Universität Bayreuth, Institut für Biochemie und Biologie/Pflanzenphysiologie, Universität Potsdam, Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Système membranaires, photobiologie, stress et détoxication (SMPSD), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Instituto de Bioquimica Vegetal y Fotosintesis (IBVF), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC), Fachbereich Biologie, Molekulare Biotechnologie und Systembiologie, Technische Universität Kaiserslautern (TU Kaiserslautern), Grants from the Deutsche Forschungsgemeinschaft (Schr 617/2-4 and 617/5-1) - Bundesministerium für Bildung und Forschung (Systems Biology Initiative FORSYS, Project GoFORSYS), Instituto de Bioquimica Vegetal y Fotosıntesis, University of Potsdam = Universität Potsdam, Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
- Subjects
Proteomics ,0106 biological sciences ,membrane biogenesis ,Light ,Photosystem II ,Algae ,thylakoid ,photosystem ,Plant Science ,macromolecular substances ,Thylakoids ,01 natural sciences ,Twin-arginine translocation pathway ,03 medical and health sciences ,chloroplast ,Gene Expression Regulation, Plant ,Light-dependent reactions ,subcellular localization ,polycyclic compounds ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,vesicle inducing protein ,Photosynthesis ,plastid ,Research Articles ,Institut für Biochemie und Biologie ,Plant Proteins ,030304 developmental biology ,Photosystem ,0303 health sciences ,lipid transport ,ATP synthase ,biology ,Chlamydomonas ,Membrane Proteins ,Photosystem II Protein Complex ,food and beverages ,Cell Biology ,Cell biology ,Thylakoid ,Mutation ,Membrane biogenesis ,Quantasome ,biology.protein ,RNA Interference ,010606 plant biology & botany - Abstract
International audience; The vesicle-inducing protein in plastids (VIPP1) was suggested to play a role in thylakoid membrane formation via membrane vesicles. As this functional assignment is under debate, we investigated the function of VIPP1 in Chlamydomonas reinhardtii. Using immunofluorescence, we localized VIPP1 to distinct spots within the chloroplast. In VIPP1-RNA interference/artificial microRNA cells, we consistently observed aberrant, prolamellar body-like structures at the origin of multiple thylakoid membrane layers, which appear to coincide with the immunofluorescent VIPP1 spots and suggest a defect in thylakoid membrane biogenesis. Accordingly, using quantitative shotgun proteomics, we found that unstressed vipp1 mutant cells accumulate 14 to 20% less photosystems, cytochrome b(6)f complex, and ATP synthase but 30% more light-harvesting complex II than control cells, while complex assembly, thylakoid membrane ultrastructure, and bulk lipid composition appeared unaltered. Photosystems in vipp1 mutants are sensitive to high light, which coincides with a lowered midpoint potential of the Q(A)/Q(A)(-) redox couple and increased thermosensitivity of photosystem II (PSII), suggesting structural defects in PSII. Moreover, swollen thylakoids, despite reduced membrane energization, in vipp1 mutants grown on ammonium suggest defects in the supermolecular organization of thylakoid membrane complexes. Overall, our data suggest a role of VIPP1 in the biogenesis/assembly of thylakoid membrane core complexes, most likely by supplying structural lipids.
- Published
- 2012