The role of phospholipids in the molecular organisation of pea chloroplast membranes. Effect of phospholipid depletion on photosynthetic activities

Jordan, Bill; Chow, W. S.; Baker, Andrew R.

doi:10.1016/0005-2728(83)90226-8

Cited by 72 publications

(38 citation statements)

References 31 publications

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“…This suggests that the decrease in lipids in the PSII reaction center complex is due to the preferential removal of galactolipids, as opposed to sulfolipids and phospholipids. This is in agreement with the finding that the enzymatic hydrolysis of phospholipids inhibits specifically PSII (23). All this indicates that lipids are an essential part of the PSII reaction center complex and that their composition is different from the overall lipid composition of grana membranes.…”

Section: Discussionsupporting

confidence: 92%

Isolation of the photosystem II reaction center complex from barley. Characterization by circular dichroism spectroscopy and amino acid sequencing

Hinz

1985

Carlsberg Res. Commun.

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A photosystem II (PSII) reaction center complex containing Chla-protein 2, Chlo-protein 3, cytochromc b~,, the herbicide-binding polypeptide and the 33 kD polypeptide from the oxygen-evolving site of PSII was isolated by sucrose gradient centrifugation of the dodecyl-13,D-maltoside extract of grana membranes highly enriched in PSII. The reaction center complex contained ca 19 lipid molecules per reaction center and sedimented slightly faster than catalase. It mediated light-induced, DCMU-sensitive electron transport from 1,5-diphenylcarbazide to dichlorophenolindophenol.The N-terminal amino acid sequence of a proteolytic fragment of ChL-protein 2 was determined. Eighteen out of 20 amino acid residues were identical with the deduced amino acid sequence of the 51 kD ChL-apoprotein from spinach.In contrast to grana membranes, which had a 77 K fluorescence emission maximum at 685 nm with a pronounced shoulder at 695 nm, the PSII reaction center complex had a single peak at 685 nm. Circular dichroism measurements in the visible range showed that the pigments associated with the isolated PSII reaction center complex and the light-harvesting complex (LHC) were highly oriented. The secondary structure of the PSII reaction center complex and LHC was investigated by circular dichroism measurements in the ultraviolet range. Both had a high ct-helix content, suggesting that the chlorophyll molecules may be oriented between transmembrane helices in a similar way as in bacterial reaction centers and light harvesting systems. INTRODUCrlONOver the last seven years many different PSII preparations with varying degrees of complexity have been described. Preparations of grana membranes highly enriched in PSII by phase partitioning (l, 20) or 30) made it possible to study the function of PSII in a system which was close to the in vivo situation and to investigate the lateral distribution of proteins and lipids in the thylakoid membrane. Additionally, grana membranes were fractionated by extraction with various detergents folAbbreviations: Chl = chlorophyll; DCMU = 3-(3,4-dichlorophenyl)-l,l-dimethylurea; DCPIP = 2,6-dichlorophenolindopbenol; DPC = 1,5-diphenylcarbazide; HEPES = N-(2-hydroxyethyl)-piperazine-N'-2-ethane sulfonic acid; LHC = light harvesting complex; LHCII = LHC of photosystem II; PAGE = polyacrylamide gel electrophoresis; PS = photosystem; PTH = phenylthiohydantoin; SDS = sodium dodecyl sulfate; tricine = N-(tris(hydroxymethyl)methyl)glycine; Tris = tris-(hydroxymethyl)aminomethane.Springer-Verlag 0105 -1938/85/0050/0285/$02.80

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Section: Discussionsupporting

confidence: 92%

Isolation of the photosystem II reaction center complex from barley. Characterization by circular dichroism spectroscopy and amino acid sequencing

Hinz

1985

Carlsberg Res. Commun.

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“…Decomposition of approximately 70% of PG from thylakoid membranes by treatment with phospholipase A 2 was found to strongly inhibit photosynthetic electron transport in PSII without any significant effect on photosynthetic electron transport in PSI (Jordan et al, 1983). Similarly, Droppa et al (1995) reported that phospholipase C treatment of pea (Pisum sativum) thylakoid membranes, degrading approximately one-half of the PG, eliminated photosynthetic electron transport in PSII.…”

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confidence: 97%

Effects of the Lack of Phosphatidylglycerol on the Donor Side of Photosystem II

et al. 2007

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Our previous studies with the pgsA mutant of the cyanobacterium Synechocystis sp. PCC6803 (hereafter termed pgsA mutant), which is defective for the biosynthesis of phosphatidylglycerol (PG), revealed an important role for PG in the electron acceptor side of photosystem II (PSII), especially in the electron transport between plastoquinones Q A and Q B . This study now shows that PG also plays an important role in the electron donor side of PSII, namely, the oxygen-evolving system. Analyses of purified PSII complexes indicated that PSII from PG-depleted pgsA mutant cells sustained only approximately 50% of the oxygen-evolving activity compared to wild-type cells. Dissociation of the extrinsic proteins PsbO, PsbV, and PsbU, which are required for stabilization of the manganese (Mn) cluster, followed by the release of a Mn atom, was observed in PSII of the PG-depleted mutant cells. The released PsbO rebound to PSII when PG was added back to the PG-depleted mutant cells, even when de novo protein synthesis was inhibited. Changes in photosynthetic activity of the PG-depleted pgsA mutant cells induced by heat treatment or dark incubation resembled those of DpsbO, DpsbV, and DpsbU mutant cells. These results suggest that PG plays an important role in binding extrinsic proteins required for sustaining a functional Mn cluster on the donor side of PSII.

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“…It is also an integral component of the PSI reaction center (Jordan et al, 2001) and is required for the in vitro reconstitution of the light-harvesting pigment-protein complexes of PSI (Schmid et al, 1997). Thylakoid membranes treated with phospholipase A 2 are PG depleted and are inhibited in their photosynthetic electron transport activities (Jordan et al, 1983;Siegenthaler et al, 1987). Furthermore, the anionic lipid PG interacts with the transit peptide of chloroplast precursor proteins during protein import into chloroplasts (van't Hof et al, 1993).…”

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confidence: 99%

The pgp1 Mutant Locus of Arabidopsis Encodes a Phosphatidylglycerolphosphate Synthase with Impaired Activity

et al. 2002

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Phosphatidylglycerol is a ubiquitous phospholipid that is also present in the photosynthetic membranes of plants. Multiple independent lines of evidence suggest that this lipid plays a critical role for the proper function of photosynthetic membranes and cold acclimation. In eukaryotes, different subcellular compartments are competent for the biosynthesis of phosphatidylglycerol. Details on the plant-specific pathways in different organelles are scarce. Here, we describe a phosphatidylglycerol biosynthesis-deficient mutant of Arabidopsis, pgp1. The overall content of phosphatidylglycerol is reduced by 30%. This mutant carries a point mutation in the CDP-alcohol phosphotransferase motif of the phosphatidylglycerolphosphate synthase (EC 2.7.8.5) isoform encoded by a gene on chromosome 2. The mutant shows an 80% reduction in plastidic phosphatidylglycerolphosphate synthase activity consistent with the plastidic location of this particular isoform. Mutant plants are pale green, and their photosynthesis is impaired. This mutant provides a promising new tool to elucidate the biosynthesis and function of plastidic phosphatidylglycerol in seed plants.Phosphatidylglycerol (PG) is one of the most common phosphoglycerolipids found in nature. It is the only major phospholipid present in the thylakoid membranes of plant chloroplasts (Marechal et al., 1997) and the only phospholipid in cyanobacteria, which strikingly resemble plant chloroplasts in their lipid composition (Murata and Nishida, 1987). A large body of correlative and direct evidence suggests that PG is critical for the structural and functional integrity of the thylakoid membrane. Thus, the presence of specific molecular species of PG in photosynthetic membranes correlates well with lowtemperature-induced photoinhibition and chilling sensitivity of plants and cyanobacteria (Murata et al., 1992;Somerville, 1995). Light-harvesting pigmentprotein complexes of PSII are specifically enriched in PG (Murata et al., 1990;Tremolieres et al., 1994). Moreover, PG is crucial for the in vitro trimerization of the major peripheral light-harvesting pigmentprotein complexes (Nussberger et al., 1993; Hobe et al., 1994;Kü hlbrandt, 1994) and the dimerization of the reaction/center core pigment-protein complexes of PSII (Kruse et al., 2000). It is also an integral component of the PSI reaction center (Jordan et al., 2001) and is required for the in vitro reconstitution of the light-harvesting pigment-protein complexes of PSI (Schmid et al., 1997). Thylakoid membranes treated with phospholipase A 2 are PG depleted and are inhibited in their photosynthetic electron transport activities (Jordan et al., 1983;Siegenthaler et al., 1987). Furthermore, the anionic lipid PG interacts with the transit peptide of chloroplast precursor proteins during protein import into chloroplasts (van't Hof et al., 1993).PG-deficient auxotrophic mutants of the cyanobacterium Synechocystis sp. PCC6803 that are severely impaired in photosynthesis have recently been isolated (Hagio et al., 2000;Sato et al., ...

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The role of phospholipids in the molecular organisation of pea chloroplast membranes. Effect of phospholipid depletion on photosynthetic activities

Cited by 72 publications

References 31 publications

Isolation of the photosystem II reaction center complex from barley. Characterization by circular dichroism spectroscopy and amino acid sequencing

Isolation of the photosystem II reaction center complex from barley. Characterization by circular dichroism spectroscopy and amino acid sequencing

Effects of the Lack of Phosphatidylglycerol on the Donor Side of Photosystem II

The pgp1 Mutant Locus of Arabidopsis Encodes a Phosphatidylglycerolphosphate Synthase with Impaired Activity

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