Role of phosphatidylglycerol in the function and assembly of Photosystem II reaction center, studied in a cdsA-inactivated PAL mutant strain of Synechocystis sp. PCC6803 that lacks phycobilisomes

Hajnalka Laczkó-Dobos, Bettina Ughy, Szilvia Z. Tóth, Josef Komenda, Ottó Zsiros, Ildikó Domonkos, A. Párducz, Balázs Bogos, Masayuki Komura, Shigeru Itoh, Z. Gombos

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

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/ΔcdsA 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 QA to QB in PSII and (c) in a modification of chlorophyll fluorescence curve. The depletion of PG affected neither the redox levels of QA nor the S2 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. [35S]-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.

Original languageEnglish
Pages (from-to)1184-1194
Number of pages11
JournalBBA - Bioenergetics
Volume1777
Issue number9
DOIs
Publication statusPublished - Sep 2008

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Phycobilisomes
Synechocystis
Phosphatidylglycerols
Photosystem II Protein Complex
Photosynthetic membranes
Cytidine Diphosphate
Cytidine
Gene encoding
Thermoluminescence
Diphosphates
Diglycerides
Cell growth
Cyanobacteria
Chlorophyll
Manganese
Methionine
Cell Division
Dimers
Labeling
Oxidation-Reduction

Keywords

  • Cell division
  • OJIP transient
  • Phosphatidylglycerol
  • Photosystem II
  • Synechocystis sp. PCC6803
  • Thermoluminescence

ASJC Scopus subject areas

  • Biophysics

Cite this

Role of phosphatidylglycerol in the function and assembly of Photosystem II reaction center, studied in a cdsA-inactivated PAL mutant strain of Synechocystis sp. PCC6803 that lacks phycobilisomes. / Laczkó-Dobos, Hajnalka; Ughy, Bettina; Tóth, Szilvia Z.; Komenda, Josef; Zsiros, Ottó; Domonkos, Ildikó; Párducz, A.; Bogos, Balázs; Komura, Masayuki; Itoh, Shigeru; Gombos, Z.

In: BBA - Bioenergetics, Vol. 1777, No. 9, 09.2008, p. 1184-1194.

Research output: Contribution to journalArticle

Laczkó-Dobos, Hajnalka ; Ughy, Bettina ; Tóth, Szilvia Z. ; Komenda, Josef ; Zsiros, Ottó ; Domonkos, Ildikó ; Párducz, A. ; Bogos, Balázs ; Komura, Masayuki ; Itoh, Shigeru ; Gombos, Z. / Role of phosphatidylglycerol in the function and assembly of Photosystem II reaction center, studied in a cdsA-inactivated PAL mutant strain of Synechocystis sp. PCC6803 that lacks phycobilisomes. In: BBA - Bioenergetics. 2008 ; Vol. 1777, No. 9. pp. 1184-1194.
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abstract = "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/ΔcdsA 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 QA to QB in PSII and (c) in a modification of chlorophyll fluorescence curve. The depletion of PG affected neither the redox levels of QA nor the S2 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. [35S]-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.",
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AU - Laczkó-Dobos, Hajnalka

AU - Ughy, Bettina

AU - Tóth, Szilvia Z.

AU - Komenda, Josef

AU - Zsiros, Ottó

AU - Domonkos, Ildikó

AU - Párducz, A.

AU - Bogos, Balázs

AU - Komura, Masayuki

AU - Itoh, Shigeru

AU - Gombos, Z.

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N2 - 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/ΔcdsA 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 QA to QB in PSII and (c) in a modification of chlorophyll fluorescence curve. The depletion of PG affected neither the redox levels of QA nor the S2 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. [35S]-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.

AB - 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/ΔcdsA 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 QA to QB in PSII and (c) in a modification of chlorophyll fluorescence curve. The depletion of PG affected neither the redox levels of QA nor the S2 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. [35S]-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.

KW - Cell division

KW - OJIP transient

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KW - Photosystem II

KW - Synechocystis sp. PCC6803

KW - Thermoluminescence

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