Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1777, Issue 9, Pages 1184-1194Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2008.06.003
Keywords
Synechocystis sp PCC6803; phosphatidylglycerol; photosystem II; thermoluminescence; OJIP transient; cell division
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Funding
- Hungarian Science Foundation [T 60109, T 68692]
- Ministry of Education, Youth and Sports of the Czech Republic [MSM6007665808]
- Czech Academy of Sciences [AV0Z50200510, 1AA400200801]
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To analyze the role of phosphatidylglycerol (PG) in photosynthetic membranes of cyanobacteria we used two mutants of Synechocystis sp. PCC6803: the PAL mutant which has no phycobilisomes and shows a high PSII/PSI ratio, and a mutant derived from it by inactivating its cdsA gene encoding cytidine 5'-diphosphate diacylglycerol synthase, a key enzyme in PG synthesis. In a medium supplemented with PG the PAL/Delta cdsA mutant cells grew photoautotrophically. Depletion of PG in the medium resulted (a) in an arrest of cell growth and division, (b) in a slowdown of electron transfer from the acceptor Q(A) to Q(B) in PSII and (c) in a modification of chlorophyll fluorescence curve. The depletion of PG affected neither the redox levels of QA nor the S-2 state of the oxygen-evolving manganese complex, as indicated by thermoluminescence studies. Two-dimensional PAGE showed that in the absence of PG (a) the PSII dimer was decomposed into monomers, and (b) the CP43 protein was detached from a major Part of the PSII core complex. [S-35]-methionine labeling confirmed that PG depletion did not block de novo synthesis of the PSII proteins. We conclude that PG is required for the binding of CP43 within the PSII core complex. (C) 2008 Elsevier B.V. All rights reserved.
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