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Insights into the function of PsbR protein in Arabidopsis thaliana
Authors:Yagut Allahverdiyeva  Marjaana Suorsa  Imre Vass
Affiliation:a Department of Biology, Plant Physiology and Molecular Biology, University of Turku, FIN-20014 Turku, Finland
b Department of the Photochemistry and Molecular Science, Ångström Laboratory, Box 532, Uppsala University, Uppsala 751 20, Sweden
c Plant Biology Institute, Biological Research Center, H-6701 Szeged, PO-Box 521, Hungary
Abstract:
The functional state of the Photosystem (PS) II complex in Arabidopsis psbR T-DNA insertion mutant was studied. The ΔPsbR thylakoids showed about 34% less oxygen evolution than WT, which correlates with the amounts of PSII estimated from YDox radical EPR signal. The increased time constant of the slow phase of flash fluorescence (FF)-relaxation and upshift in the peak position of the main TL-bands, both in the presence and in the absence of DCMU, confirmed that the S2QA and S2QB charge recombinations were stabilized in ΔPsbR thylakoids. Furthermore, the higher amount of dark oxidized Cyt-b559 and the increased proportion of fluorescence, which did not decay during the 100s time span of the measurement thus indicating higher amount of YD+QA recombination, pointed to the donor side modifications in ΔPsbR. EPR measurements revealed that S1-to-S2-transition and S2-state multiline signal were not affected by mutation. The fast phase of the FF-relaxation in the absence of DCMU was significantly slowed down with concomitant decrease in the relative amplitude of this phase, indicating a modification in QA to QB electron transfer in ΔPsbR thylakoids. It is concluded that the lack of the PsbR protein modifies both the donor and the acceptor side of the PSII complex.
Keywords:Chl, chlorophyll   DCMU, 3-(3&prime  ,4&prime  -dichlorphenyl)-1,1-dimethylurea   DCIP, 2,6-dichlorophenolindophenol   DMBQ, 2,6-dimethyl-p-benzoquinone   DPC, 2,2&prime  -diphenylcarbonic dihydrazide   EPR, electron paramagnetic resonance   Fv, variable fluorescence yield   PSII, Photosystem II   QA and QB, primary and secondary quinone acceptors in PSII   YZ and YZ  0"   alt="  radical dot"   src="  http://cdn.els-cdn.com/sd/entities/rad"   class="  glyphImg"  >, tyrosine 161 of the PSII D1 polypeptide and its radical   YD and YD  0"   alt="  radical dot"   src="  http://cdn.els-cdn.com/sd/entities/rad"   class="  glyphImg"  >, tyrosine 161 of the PSII D2 polypeptide and its radical   TL, thermoluminescence
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