A Null Mutant of Synechococcus sp. PCC7942 Deficient in the Sulfolipid Sulfoquinovosyl Diacylglycerol

Güler, Sinan; Seeliger, A. G.; Härtel, Heiko; Ренгер, Г.; Benning, Christoph

doi:10.1074/jbc.271.13.7501

Cited by 170 publications

(139 citation statements)

References 34 publications

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“…Cyanobacteria mutants with impaired SQDG synthesis are severely affected in growth only under Pilimiting conditions, suggesting that sulfolipids can replace phospholipids to maintain membrane functionality and integrity (18). In plants it has been shown that not only sulfolipids but also galactolipids increase after Pi deprivation (8,19).…”

Section: Discussionmentioning

confidence: 99%

Phospholipase DZ2 plays an important role in extraplastidic galactolipid biosynthesis and phosphate recycling in Arabidopsis roots

Cruz‐Ramírez¹,

Oropeza-Aburto²,

Razo-Hernández³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

245

232

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Low phosphate (Pi) availability is one of the major constraints for plant productivity in natural and agricultural ecosystems. Plants have evolved a myriad of developmental and biochemical mechanisms to increase internal Pi uptake and utilization efficiency. One important biochemical pathway leading to an increase in internal Pi availability is the hydrolysis of phospholipids. Hydrolyzed phospholipids are replaced by nonphosphorus lipids such as galactolipids and sulfolipids, which help to maintain the functionality and structure of membrane systems. Here we report that a member of the Arabidopsis phospholipase D gene family (PLDZ2) is gradually induced upon Pi starvation in both shoots and roots. From lipid content analysis we show that an Arabidopsis pldz2 mutant is defective in the hydrolysis of phospholipids and has a reduced capacity to accumulate galactolipids under limiting Pi conditions. Morphological analysis of the pldz2 root system shows a premature change in root architecture in response to Pi starvation. These results show that PLDZ2 is involved in the eukaryotic galactolipid biosynthesis pathway, specifically in hydrolyzing phosphatidylcholine and phosphatidylethanolamine to produce diacylglycerol for digalactosyldiacylglycerol synthesis and free Pi to sustain other Pi-requiring processes.phosphate starvation ͉ phospholipids ͉ root architecture ͉ sulfolipids P hosphate (Pi) influences virtually all developmental and biochemical processes in plants. Pi is not only a constituent of key cell molecules such as ATP, nucleic acids, and phospholipids, but it is also a pivotal metabolic regulator of many processes including energy transfer, protein activation, and carbon and nitrogen metabolism. However, Pi availability can be one of the major constraints for plant growth in both natural and agricultural ecosystems because of its low mobility and high absorption capacity in the soil. As a response to this limitation, plants have evolved a range of developmental, biochemical, and symbiotic adaptive strategies to cope with low Pi availability (1, 2). In Arabidopsis, a general, 3-fold strategy to cope with low Pi availability has been described. (i) The release and uptake of Pi from external sources that are not readily available for plant uptake. This mechanism includes the transcriptional activation of high-affinity Pi transporters and the excretion of RNases, acid phosphatases, and organic acids (3-5). (ii) Changes in the architecture of the root system that reflect alterations in cell length, root meristem activity, root hair elongation, and an increased number of lateral roots (6, 7). These changes presumably increase the exploratory capacity of the root and the absorptive surface area. (iii) Optimization of Pi utilization due to a wide range of metabolic alterations, and the mobilization of Pi from internal reserves by the hydrolysis of nucleic acids, proteins, and the recycling of Pi from membrane phospholipids.During Pi deprivation, the total content of diverse phospholipids such as phosphatidylcholin...

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Section: Discussionmentioning

confidence: 99%

Phospholipase DZ2 plays an important role in extraplastidic galactolipid biosynthesis and phosphate recycling in Arabidopsis roots

Cruz‐Ramírez¹,

Oropeza-Aburto²,

Razo-Hernández³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

245

232

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“…These included phosphate and phosphonate uptake proteins and the sulfolipid (UDP-sulfoquinovose) biosynthesis protein (Guler et al, 1996;Van Mooy et al, 2006). In addition, a PhoH-like phosphate starvation-inducible protein encoded by Prochlorococcus, but not Synechococcus, was also detected.…”

Section: Abundant Cyanobacterial Proteinsmentioning

confidence: 99%

Transport functions dominate the SAR11 metaproteome at low-nutrient extremes in the Sargasso Sea

et al. 2008

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The northwestern Sargasso Sea undergoes annual cycles of productivity with increased production in spring corresponding to periods of upwelling, and oligotrophy in summer and autumn, when the water column becomes highly stratified. The biological productivity of this region is reduced during stratified periods as a result of low concentrations of phosphorus and nitrogen in the euphotic zone. To better understand the mechanisms of microbial survival in this oligotrophic environment, we used capillary liquid chromatography (LC)-tandem mass spectrometry to detect microbial proteins in surface samples collected in September 2005. A total of 2215 peptides that mapped to 236 SAR11 proteins, 1911 peptides that mapped to 402 Prochlorococcus proteins and 2407 peptides that mapped to 404 Synechococcus proteins were detected. Mass spectra from SAR11 periplasmic substrate-binding proteins accounted for a disproportionately large fraction of the peptides detected, consistent with observations that these extremely small cells devote a large proportion of their volume to periplasm. Abundances were highest for periplasmic substrate-binding proteins for phosphate, amino acids, phosphonate, sugars and spermidine. Proteins implicated in the prevention of oxidative damage and protein refolding were also abundant. Our findings support the view that competition for multiple nutrients in oligotrophic systems is extreme, but nutrient flux is sufficient to sustain microbial community activity.

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“…PCC 7120 (Anabaena) were chosen because their genomes had been fully sequenced (Kaneko et al, 1996(Kaneko et al, , 2001). So far, four genes encoding enzymes for membrane-lipid assembly have been reported in cyanobacteria: UDPsulfoquinovose synthase (Gü ler et al, 1996), sulfoquinovosyldiacylglycerol (SQDG) synthase (Gü ler et al, 2000), cytidine diphosphate-diacylglycerol synthase , and phosphatidylglycerol phosphate synthase . In all cases, proteins are highly conserved between Synechocystis and Anabaena, being 84%, 72%, 62%, and 61% identical, respectively, suggesting that the enzymes for MGDG synthesis are also conserved between these two bacteria.…”

Section: Mglcdg Synthase Activity Is Conserved In Both Unicellular Anmentioning

confidence: 99%

Comparative Genomic Analysis Revealed a Gene for Monoglucosyldiacylglycerol Synthase, an Enzyme for Photosynthetic Membrane Lipid Synthesis in Cyanobacteria

Awai

Kakimoto²,

Awai³

et al. 2006

Plant Physiology

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Cyanobacteria have a thylakoid lipid composition very similar to that of plant chloroplasts, yet cyanobacteria are proposed to synthesize monogalactosyldiacylglycerol (MGDG), a major membrane polar lipid in photosynthetic membranes, by a different pathway. In addition, plant MGDG synthase has been cloned, but no ortholog has been reported in cyanobacterial genomes. We report here identification of the gene for monoglucosyldiacylglycerol (MGlcDG) synthase, which catalyzes the first step of galactolipid synthesis in cyanobacteria. Using comparative genomic analysis, candidates for the gene were selected based on the criteria that the enzyme activity is conserved between two species of cyanobacteria (unicellular [Synechocystis sp. PCC 6803] and filamentous [Anabaena sp. PCC 7120]), and we assumed three characteristics of the enzyme; namely, it harbors a glycosyltransferase motif, falls into a category of genes with unknown function, and shares significant similarity in amino acid sequence between these two cyanobacteria. By a motif search of all genes of Synechocystis, BLAST searches, and similarity searches between these two cyanobacteria, we identified four candidates for the enzyme that have all the characteristics we predicted. When expressed in Escherichia coli, one of the Synechocystis candidate proteins showed MGlcDG synthase activity in a UDP-glucose-dependent manner. The ortholog in Anabaena also showed the same activity. The enzyme was predicted to require a divalent cation for its activity, and this was confirmed by biochemical analysis. The MGlcDG synthase and the plant MGDG synthase shared low similarity, supporting the presumption that cyanobacteria and plants utilize different pathways to synthesize MGDG.

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A Null Mutant of Synechococcus sp. PCC7942 Deficient in the Sulfolipid Sulfoquinovosyl Diacylglycerol

Cited by 170 publications

References 34 publications

Phospholipase DZ2 plays an important role in extraplastidic galactolipid biosynthesis and phosphate recycling in Arabidopsis roots

Phospholipase DZ2 plays an important role in extraplastidic galactolipid biosynthesis and phosphate recycling in Arabidopsis roots

Transport functions dominate the SAR11 metaproteome at low-nutrient extremes in the Sargasso Sea

Comparative Genomic Analysis Revealed a Gene for Monoglucosyldiacylglycerol Synthase, an Enzyme for Photosynthetic Membrane Lipid Synthesis in Cyanobacteria

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