title: PsbI affects the stability, function, and phosphorylation patterns of photosystem II assemblies in tobacco.
abstract: Photosystem II (PSII) core complexes consist of CP47, CP43, D1, D2 proteins and of several low molecular weight integral membrane polypeptides, such as the chloroplast-encoded PsbE, PsbF, and PsbI proteins. To elucidate the function of PsbI in the photosynthetic process as well as in the biogenesis of PSII in higher plants, we generated homoplastomic knock-out plants by replacing most of the tobacco psbI gene with a spectinomycin resistance cartridge. Mutant plants are photoautotrophically viable under green house conditions but sensitive to high light irradiation. Antenna proteins of PSII accumulate to normal amounts, but levels of the PSII core complex are reduced by 50%. Bioenergetic and fluorescence studies uncovered that PsbI is required for the stability but not for the assembly of dimeric PSII and supercomplexes consisting of PSII and the outer antenna (PSII-LHCII). Thermoluminescence emission bands indicate that the presence of PsbI is required for assembly of a fully functional Q(A) binding site. We show that phosphorylation of the reaction center proteins D1 and D2 is light and redox-regulated in the wild type, but phosphorylation is abolished in the mutant, presumably due to structural alterations of PSII when PsbI is deficient. Unlike wild type, phosphorylation of LHCII is strongly increased in the dark due to accumulation of reduced plastoquinone, whereas even upon state II light phosphorylation is decreased in delta psbI. These data attest that phosphorylation of D1/D2, CP43, and LHCII is regulated differently.
authors.affiliation: Department Biology I, Botany, Ludwig-Maximilians-University Munich, Menzingerstrasse 67, 80638 Munich, Germany.
authors.forename: Serena
authors.initials: S
authors.lastname: Schwenkert
authors.forename: Pavan
authors.initials: P
authors.lastname: Umate
authors.forename: Cristina
authors.initials: C
authors.lastname: Dal Bosco
authors.forename: Stefanie
authors.initials: S
authors.lastname: Volz
authors.forename: Lada
authors.initials: L
authors.lastname: Mlçochová
authors.forename: Mikael
authors.initials: M
authors.lastname: Zoryan
authors.forename: Lutz A
authors.initials: LA
authors.lastname: Eichacker
authors.forename: Itzhak
authors.initials: I
authors.lastname: Ohad
authors.forename: Reinhold G
authors.initials: RG
authors.lastname: Herrmann
authors.forename: Jörg
authors.initials: J
authors.lastname: Meurer
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001665:Binding Sites; D002734:Chlorophyll / Q000378:metabolism; D024881:Drug Resistance, Bacterial; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D008027:Light; D045342:Light-Harvesting Protein Complexes; D010766:Phosphorylation; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism; D045332:Photosystem II Protein Complex / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D030821:Plants, Genetically Modified; D018087:Plastids / Q000378:metabolism; D010971:Plastoquinone; D016133:Polymerase Chain Reaction; D011494:Protein Kinases / Q000378:metabolism; D000198:Spectinomycin / Q000494:pharmacology; D014026:Nicotiana / Q000235:genetics / Q000378:metabolism*
chemical_list: D000900:Anti-Bacterial Agents; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; C083100:photosystem II, chlorophyll binding protein, CP-43; D002734:Chlorophyll; D000198:Spectinomycin; D011494:Protein Kinases; C120337:light-harvesting complex II kinase; D010971:Plastoquinone