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The authors localized a PGP1 fusion protein in mesophyll protoplasts and determined the activities of PG-phosphate activities in subcellular fractions of a loss-of-function pgp1 mutant of Arabidopsis. This work provided evidence that the PGP1 gene encodes a preprotein that is targeted in vivo to both plastids and mitochondria. Deficiency in the plastidial PG-phosphate synthase led to photosynthetically inactive plastids, as reported in [17]. On the other hand, deficiency in the mitochondrial PG-phosphate synthase of Arabidopsis had no significant effects on the biogenesis, the protein and glycerolipid composition or the ultrastructure of mitochondria. Hence, PGP1 is essential for plastidial PG biosynthesis and for photoautotrophic growth, whereas it is redundant for the biosynthesis of PG in mitochondria.
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Babiychuk E., Müller F., Eubel H., Braun H.P., Frentzen M., Kushnir S. Arabidopsis phosphatidylglycerophosphate synthase 1 is essential for chloroplast differentiation, but is dispensable for mitochondrial function. Plant J. 33:2003;899-909 The authors localized a PGP1 fusion protein in mesophyll protoplasts and determined the activities of PG-phosphate activities in subcellular fractions of a loss-of-function pgp1 mutant of Arabidopsis. This work provided evidence that the PGP1 gene encodes a preprotein that is targeted in vivo to both plastids and mitochondria. Deficiency in the plastidial PG-phosphate synthase led to photosynthetically inactive plastids, as reported in [17]. On the other hand, deficiency in the mitochondrial PG-phosphate synthase of Arabidopsis had no significant effects on the biogenesis, the protein and glycerolipid composition or the ultrastructure of mitochondria. Hence, PGP1 is essential for plastidial PG biosynthesis and for photoautotrophic growth, whereas it is redundant for the biosynthesis of PG in mitochondria.
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Kawasaki K., Kuge O., Chang S.C., Heacock P.N., Rho M., Suzuki K., Nishijima M., Dowhan W. Isolation of a Chinese hamster ovary (CHO) cDNA encoding phosphatidylglycerophosphate (PGP) synthase, expression of which corrects the mitochondrial abnormalities of a PGP synthase-defective mutant of CHO-K1 cells. J Biol Chem. 274:1999;1828-1834
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Hagio M., Gombos Z., Várkonyi Z., Masamoto K., Sato N., Tsuzuki M., Wada H. Direct evidence for requirement of phosphatidylglycerol in photosystem II of photosynthesis. Plant Physiol. 124:2000;795-804
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Hagio, M.1
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Phosphatidylglycerol is essential for the development of thylakoid membranes in Arabidopsis thaliana
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The authors of this paper describe the isolation and characterization of Arabidopsis mutants in which the PGP1 gene is completely inactivated by T-DNA insertions. This gene disruption causes a reduction in the PG proportion of the total leaf lipid content to 12% of the wildtype level, a reduction in the mesophyll cell number, a severe defect in chloroplast development and a requirement for sucrose for growth. Hence, the data presented demonstrate that PGP1 plays a major role in the biosynthesis of plastidial PG, and that PG is essential for the development of thylakoid membranes in Arabidopsis.
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Hagio M., Sakurai I., Sato S., Kato T., Tabata S., Wada H. Phosphatidylglycerol is essential for the development of thylakoid membranes in Arabidopsis thaliana. Plant Cell Physiol. 43:2002;1456-1464 The authors of this paper describe the isolation and characterization of Arabidopsis mutants in which the PGP1 gene is completely inactivated by T-DNA insertions. This gene disruption causes a reduction in the PG proportion of the total leaf lipid content to 12% of the wildtype level, a reduction in the mesophyll cell number, a severe defect in chloroplast development and a requirement for sucrose for growth. Hence, the data presented demonstrate that PGP1 plays a major role in the biosynthesis of plastidial PG, and that PG is essential for the development of thylakoid membranes in Arabidopsis.
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Hagio, M.1
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Wada, H.6
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19
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This paper describes the isolation and characterization of an Arabidopsis mutant that carries a point mutation in the PGP1 gene. This mutation leads to a 80% reduction in the plastidial PG-phosphate synthase activity, a reduction in the PG proportion of the total leaf lipid content by 30%, a retarded biogenesis of thylakoid membranes and an impairment in PS II activity. Thus, the data presented in this paper show that a slight reduction in the level of plastidial PG causes severe defects in photosynthesis.
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Xu C., Härtel H., Wada H., Hagio M., Yu B., Eakin C., Benning C. The pgp1 mutant locus of Arabidopsis encodes a phosphatidylglycerolphosphate synthase with impaired activity. Plant Physiol. 129:2002;594-604 This paper describes the isolation and characterization of an Arabidopsis mutant that carries a point mutation in the PGP1 gene. This mutation leads to a 80% reduction in the plastidial PG-phosphate synthase activity, a reduction in the PG proportion of the total leaf lipid content by 30%, a retarded biogenesis of thylakoid membranes and an impairment in PS II activity. Thus, the data presented in this paper show that a slight reduction in the level of plastidial PG causes severe defects in photosynthesis.
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Xu, C.1
Härtel, H.2
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Yu, B.5
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20
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Lack of mitochondrial anionic phospholipids causes an inhibition of translation of protein components of the electron transport chain
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Ostrander D.B., Zhang M., Mileykovskaya E., Rho M., Dowhan W. Lack of mitochondrial anionic phospholipids causes an inhibition of translation of protein components of the electron transport chain. J Biol Chem. 276:2001;25262-25272
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Ostrander, D.B.1
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Güler S., Essigmann B., Benning C. A cyanobacterial gene, sqdX, required for biosynthesis of the sulfolipid sulfoquinovosyldiacylglycerol. J Bacteriol. 182:2000;543-545
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Güler, S.1
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22
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Sanda S., Leustek T., Theisen M.J., Garavito R.M., Benning C. Recombinant Arabidopsis SQD1 converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose in vitro. J Biol Chem. 276:2001;3941-3946
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Sanda, S.1
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23
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0037117493
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Arabidopsis disrupted in SQD2 encoding sulfolipid synthase is impaired in phosphate-limited growth
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The authors identify the SQD2 gene of Arabidopsis, which encodes SQDG synthase. Expression of the single-copy gene SQD2 in Arabidopsis plants is induced appreciably by phosphate starvation. Functional expression studies in E. coli provide direct evidence that SQD1 and SQD2 represent the biosynthetic machinery that is specific to SQDG formation. In addition, analyses of an Arabidopsis mutant that lacks SQDG, because the SQD2 gene had been completely inactivated by T-DNA insertion, revealed that SQDG is predominantly required to substitute for PG under phosphate-limiting conditions.
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Yu B., Xu C., Benning C. Arabidopsis disrupted in SQD2 encoding sulfolipid synthase is impaired in phosphate-limited growth. Proc Natl Acad Sci USA. 99:2002;5732-5737 The authors identify the SQD2 gene of Arabidopsis, which encodes SQDG synthase. Expression of the single-copy gene SQD2 in Arabidopsis plants is induced appreciably by phosphate starvation. Functional expression studies in E. coli provide direct evidence that SQD1 and SQD2 represent the biosynthetic machinery that is specific to SQDG formation. In addition, analyses of an Arabidopsis mutant that lacks SQDG, because the SQD2 gene had been completely inactivated by T-DNA insertion, revealed that SQDG is predominantly required to substitute for PG under phosphate-limiting conditions.
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Proc Natl Acad Sci USA
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Yu, B.1
Xu, C.2
Benning, C.3
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24
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0142152446
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The sulfolipids 2′-O-acyl-sulfoquinovosyldiacylglycerol and sulfoquinovosyldiacylglycerol are absent from a Chlamydomonas reinhardtii mutant deleted in SQD1
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This is the first report to show that the green unicellular algae C. reinhardtii contains a 2′-O-acyl derivative of SQDG. Interestingly, this derivative has a fatty-acid composition that is distinctly different from that of SQDG. Analyses of a C. reinhardtii mutant in which the SQD1 gene is deleted provide evidence that the SQDG derivative is formed by acylation of the 2′-hydroxyl of the sulfoquinovosyl head group of SQDG. These analyses also suggest that not only SQDG but also its 2′-O-acyl derivative plays a role in photosynthesis, particularly under phosphate-limiting conditions. In addition, the authors discuss the evolution of the SQDG biosynthetic pathway in the light of sequence similarities between known and putative UDP-sulfoquinovosyl synthases.
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Riekhof W.R., Ruckle M.E., Lydic T.A., Sears B.B., Benning C. The sulfolipids 2′-O-acyl-sulfoquinovosyldiacylglycerol and sulfoquinovosyldiacylglycerol are absent from a Chlamydomonas reinhardtii mutant deleted in SQD1. Plant Physiol. 133:2003;864-874 This is the first report to show that the green unicellular algae C. reinhardtii contains a 2′-O-acyl derivative of SQDG. Interestingly, this derivative has a fatty-acid composition that is distinctly different from that of SQDG. Analyses of a C. reinhardtii mutant in which the SQD1 gene is deleted provide evidence that the SQDG derivative is formed by acylation of the 2′-hydroxyl of the sulfoquinovosyl head group of SQDG. These analyses also suggest that not only SQDG but also its 2′-O-acyl derivative plays a role in photosynthesis, particularly under phosphate-limiting conditions. In addition, the authors discuss the evolution of the SQDG biosynthetic pathway in the light of sequence similarities between known and putative UDP-sulfoquinovosyl synthases.
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Riekhof, W.R.1
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Identification of a gene for UDP-sulfoquinovose synthase of a green alga, Chlamydomonas reinhardtii, and its phylogeny
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Sato N, Sugimoto K, Meguro A, Tsuzuki M: Identification of a gene for UDP-sulfoquinovose synthase of a green alga, Chlamydomonas reinhardtii, and its phylogeny. DNA Res 2004, in press.
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Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose
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Mulichak A.M., Theisen M.J., Essigmann B., Benning C., Garavito R.M. Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose. Proc Natl Acad Sci USA. 96:1999;13097-13102
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0033199520
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Prediction of the active-site structure and NAD(+) binding in SQD1, a protein essential for sulfolipid biosynthesis in Arabidopsis
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Essigmann B., Hespenheide B.M., Kuhn L.A., Benning C. Prediction of the active-site structure and NAD(+) binding in SQD1, a protein essential for sulfolipid biosynthesis in Arabidopsis. Arch Biochem Biophys. 369:1999;30-41
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Native uridine 5′-diphosphate-sulfoquinovose synthase, SQD1, from spinach purifies as a 250-kDa complex
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Shimojima M., Benning C. Native uridine 5′-diphosphate- sulfoquinovose synthase, SQD1, from spinach purifies as a 250-kDa complex. Arch Biochem Biophys. 413:2003;123-130
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Two types of MGDG synthase genes, found widely in both 16:3 and 18:3 plants, differentially mediate galactolipid syntheses in photosynthetic and nonphotosynthetic tissues in Arabidopsis thaliana
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Awai K., Maréchal E., Block M.A., Brun D., Masuda T., Shimada H., Takamiya K., Ohta H., Joyard J. Two types of MGDG synthase genes, found widely in both 16:3 and 18:3 plants, differentially mediate galactolipid syntheses in photosynthetic and nonphotosynthetic tissues in Arabidopsis thaliana. Proc Natl Acad Sci USA. 98:2001;10960-10965
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Kroll D., Meierhoff K., Bechtold N., Kinoshita M., Westphal S., Vothknecht U.C., Soll J., Westhoff P. VIPP1, a nuclear gene of Arabidopsis thaliana essential for thylakoid membrane formation. Proc Natl Acad Sci USA. 98:2001;4238-4242
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Westphal S., Heins L., Soll J., Vothknecht U.C. Vipp1 deletion mutant of Synechocystis: a connection between bacterial phage shock and thylakoid biogenesis? Proc Natl Acad Sci USA. 98:2001;4243-4248
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A permease-like protein involved in ER to thylakoid lipid transfer in Arabidopsis
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The authors use high-throughput lipid profiling to isolate a new class of Arabidopsis lipid mutants. Analyses carried out on one of these mutants identify a permease-like protein that is a component of an outer-membrane protein complex. This protein mediates the import of diacylglycerol moieties from the ER into chloroplasts. The protein complex might also effect a close association between chloroplasts and certain ER domains, which would appreciably facilitate controlled lipid flux between these organelles according to their respective demands, which can vary appreciably under stress condition such as phosphate deprivation. ER domains that are associated with chloroplasts have recently been isolated from mesophyll cells (AS Sandelius, pers. comm.).
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Xu C., Fan J., Riekhof W., Frohlich J., Benning C. A permease-like protein involved in ER to thylakoid lipid transfer in Arabidopsis. EMBO J. 22:2003;2370-2379 The authors use high-throughput lipid profiling to isolate a new class of Arabidopsis lipid mutants. Analyses carried out on one of these mutants identify a permease-like protein that is a component of an outer-membrane protein complex. This protein mediates the import of diacylglycerol moieties from the ER into chloroplasts. The protein complex might also effect a close association between chloroplasts and certain ER domains, which would appreciably facilitate controlled lipid flux between these organelles according to their respective demands, which can vary appreciably under stress condition such as phosphate deprivation. ER domains that are associated with chloroplasts have recently been isolated from mesophyll cells (AS Sandelius, pers. comm.).
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Role of sulfoquinovosyl diacylglycerol for the maintenance of photosystem II in Chlamydomonas reinhardtii
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