title: The chloroplast gene ycf9 encodes a photosystem II (PSII) core subunit, PsbZ, that participates in PSII supramolecular architecture.
abstract: We have characterized the biochemical nature and the function of PsbZ, the protein product of a ubiquitous open reading frame, which is known as ycf9 in Chlamydomonas and ORF 62 in tobacco, that is present in chloroplast and cyanobacterial genomes. After raising specific antibodies to PsbZ from Chlamydomonas and tobacco, we demonstrated that it is a bona fide photosystem II (PSII) subunit. PsbZ copurifies with PSII cores in Chlamydomonas as well as in tobacco. Accordingly, PSII mutants from Chlamydomonas and tobacco are deficient in PsbZ. Using psbZ-targeted gene inactivation in tobacco and Chlamydomonas, we show that this protein controls the interaction of PSII cores with the light-harvesting antenna; in particular, PSII-LHCII supercomplexes no longer could be isolated from PsbZ-deficient tobacco plants. The content of the minor chlorophyll binding protein CP26, and to a lesser extent that of CP29, also was altered substantially under most growth conditions in the tobacco mutant and in Chlamydomonas mutant cells grown under photoautotrophic conditions. These PsbZ-dependent changes in the supramolecular organization of the PSII cores with their peripheral antennas cause two distinct phenotypes in tobacco and are accompanied by considerable modifications in (1) the pattern of protein phosphorylation within PSII units, (2) the deepoxidation of xanthophylls, and (3) the kinetics and amplitude of nonphotochemical quenching. The role of PsbZ in excitation energy dissipation within PSII is discussed in light of its proximity to CP43, in agreement with the most recent structural data on PSII.
authors.affiliation: Botanisches Institut der Ludwig-Maximilians-Universität, Menzingerstrasse 67, D-80638 Munich, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Swiatek
authors.forename: R
authors.initials: R
authors.lastname: Kuras
authors.forename: A
authors.initials: A
authors.lastname: Sokolenko
authors.forename: D
authors.initials: D
authors.lastname: Higgs
authors.forename: J
authors.initials: J
authors.lastname: Olive
authors.forename: G
authors.initials: G
authors.lastname: Cinque
authors.forename: B
authors.initials: B
authors.lastname: Müller
authors.forename: L A
authors.initials: LA
authors.lastname: Eichacker
authors.forename: D B
authors.initials: DB
authors.lastname: Stern
authors.forename: R
authors.initials: R
authors.lastname: Bassi
authors.forename: R G
authors.initials: RG
authors.lastname: Herrmann
authors.forename: F A
authors.initials: FA
authors.lastname: Wollman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002696:Chlamydomonas; D002736:Chloroplasts / Q000235:genetics*; D045342:Light-Harvesting Protein Complexes; D014975:Lutein / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics* / Q000502:physiology; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism; D010641:Phenotype; D010766:Phosphorylation; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry / Q000235:genetics*; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D010947:Plants, Toxic; D021122:Protein Subunits; D017386:Sequence Homology, Amino Acid; D014026:Nicotiana
chemical_list: D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins; D010455:Peptides; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D021122:Protein Subunits; C407702:ycf9 protein, plant; D014975:Lutein