4.4 Article

Characterization of a Synechocystis sp PCC 6803 double mutant lacking the CyanoP and Ycf48 proteins of Photosystem II

Journal

PHOTOSYNTHESIS RESEARCH
Volume 124, Issue 2, Pages 217-229

Publisher

SPRINGER
DOI: 10.1007/s11120-015-0122-0

Keywords

Assembly; Biogenesis; CyanoP; Photosystem II; PsbP; Synechocystis sp PCC 6803; Ycf48

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Funding

  1. University of Otago Division of Health Sciences Career Development Postdoctoral Fellowship
  2. Otago University Research grant

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Homologs of the Photosystem II (PS II) subunit PsbP are found in plants, algae, and cyanobacteria. In higher plants, PsbP is associated with mature PS II centers, but in cyanobacteria, the homologous CyanoP protein appears sub-stoichiometric to PS II. We have investigated the role of CyanoP by characterizing knockout mutants of the cyanobacterium Synechocystis sp. PCC 6803. Removal of CyanoP resulted in changes to phycobilisome coupling and energy transfer to PS II, but the function of PS II itself remained similar to wild type. We therefore investigated the hypothesis that CyanoP is involved in the biogenesis or repair of PS II by creating a double mutant lacking both CyanoP and the PS II assembly factor Ycf48. This strain exhibited an additive reduction in the amplitude of variable chlorophyll a fluorescence induction relative to either of the single mutants but displayed increased oxygen evolution, slight increases in PS II monomer and dimer levels, and a reduction in accumulation of an early PS II assembly complex containing CP47, compared to the Delta Ycf48 strain.

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