title: The role of the PsbU subunit in the light sensitivity of PSII in the cyanobacterium Synechococcus 7942.
abstract: In the present study we investigated the role of the PsbU subunit in the electron transport characteristics and light sensitivity of the Photosystem II complex. The experiments were performed by using an earlier characterized PsbU-less mutant of the cyanobacterium Synechococcus PCC 7942, which has enhanced antioxidant capacity (Balint et al. FEBS Lett. 580 (2006) 2117-2122). Flash induced Chl fluorescence measurements in the presence and absence of the electron transport inhibitor DCMU showed that both the S(2)Q(A)(-) and the S(2)Q(B)(-) recombination is slowed down in the PsbU mutant relative to the WT strain. Thermoluminescence measurements confirmed the increased stability of the S(2)Q(A)(-) and S(2)Q(B)(-) charge pairs by showing an increased peak temperature of Q and B bands, which were measured in the presence and absence of DCMU, respectively. In addition, the intensity of the TL bands is also increased in the PsbU mutant (≈1.7 times for the B band), as compared to the WT. The PsbU mutant shows enhanced loss of Photosystem II activity under exposure to high light intensity both in the absence and presence of the protein synthesis inhibitor lincomycin. It is concluded from the data that the lack of the PsbU subunit in Synechococcus PCC 7942 affects the energetic stability of the S(2)Q(A)(-) and S(2)Q(B)(-) charge pairs by modifying both the PSII donor and acceptor side components. This effect is most likely caused by structural changes in the vicinity of the Mn cluster and in the inner part of the PSII complex, which are induced by the lack of the PsbU subunit from the lumenal part of the complex. The light sensitivity of Photosystem II in Synechococcus 7942 in the absence of the PsbU subunit is likely due to reactive oxygen species, which are produced as a consequence of disturbed donor side structure and/or due to the modified energetic properties of the primary radical pair.
authors.affiliation: Institute of Plant Biology, Biological Research Center, H-6726 Szeged, Hungary.
authors.forename: Leyla
authors.initials: L
authors.lastname: Abasova
authors.forename: Zsuzsanna
authors.initials: Z
authors.lastname: Deák
authors.forename: Rakefet
authors.initials: R
authors.lastname: Schwarz
authors.forename: Imre
authors.initials: I
authors.lastname: Vass
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D004237:Diuron / Q000494:pharmacology; D004579:Electron Transport / Q000187:drug effects / Q000528:radiation effects; D007700:Kinetics; D008027:Light; D045332:Photosystem II Protein Complex / Q000378:metabolism*; D021122:Protein Subunits / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D046940:Synechococcus / Q000187:drug effects / Q000378:metabolism* / Q000528:radiation effects*; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D045332:Photosystem II Protein Complex; D021122:Protein Subunits; C107126:PsbU protein, Synechocystis; D004237:Diuron