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Research Paper |
Biologie VIII: Zellphysiologie1 and Biologie 12: Morphologie der Pflanzen und Feinbau der Zelle, Universität Bielefeld, D-33501 Bielefeld, Germany
Lehrstuhl für Biochemie der Pflanzen, Ruhr-Universität, D-44780 Bochum, Germany2
Author for correspondence: Elfriede K. Pistorius. Tel: +49 521 1065601. Fax: +49 521 1066410. e-mail: e.pistorius{at}biologie.uni-bielefeld.de
Slr1295 (and Slr0513) in the cyanobacterium Synechocystis sp. PCC 6803 has amino acid similarity to the bacterial FbpA protein family and also to IdiA of Synechococcus PCC 6301/PCC 7942. To determine whether Slr1295 is the periplasm-located component of an iron transporter, or has a function in protecting photosystem (PS) II, subcellular localization and
slr1295 mutant characterization studies were performed. Localization of Slr1295 provided evidence that it has an intracellular function, since virtually no Slr1295 was detected in the soluble protein fraction of the periplasm or in the cytoplasmic membrane. Characterization of a
slr1295 Synechocystis PCC 6803 mutant indicated that PS II is more susceptible to inactivation in the mutant than in the wild-type (WT). Under mild iron limitation, modification of PS I to the PS IIsiA complex is more advanced in the
slr1295 mutant, indicating that iron deficiency leads more rapidly to changes in the photosynthetic apparatus in the mutant than in the WT. Biochemical fractionation procedures provide evidence that Slr1295 co-purifies with PS II. These results suggest a function of Slr1295 that is comparable to the function of IdiA in Synechococcus PCC 6301/PCC 7942 being a protein that protects PS II under iron limitation in an as yet unknown way.
Keywords: Synechocystis PCC 6803, iron deficiency, Slr1295, photosystem I and II
Abbreviations: ABC, ATP-binding cassette; Chl, chlorophyll; DCPIP, 2,6-dichlorophenol-indophenol; Dig, digoxigenin; MV, methylviologen; PBQ, phenyl-p-benzoquinone; PCV, packed cell volume; PS I and PS II, photosystem I and II
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