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Volumn 7, Issue 3, 2004, Pages 270-276

Phosphatidylglycerol and sulfoquinovosyldiacylglycerol: Anionic membrane lipids and phosphate regulation

Author keywords

CDP; cytosine 5 diphosphate; DGDG; digalactosyldiacylglycerol; endoplasmic reticulum; ER; MGDG; monogalactosyldiacylglycerol; PG; PG phosphate synthase1 gene; PGP1; phosphatidylglycerol; photosystem; plant UDP sulfoquinovose synthase gene; PS; SQD1; SQDB

Indexed keywords

ARABIDOPSIS PROTEIN; GLYCOLIPID; GLYCOSYLTRANSFERASE; MEMBRANE LIPID; PHOSPHATE; PHOSPHATIDYLGLYCEROL; SQD2 PROTEIN, ARABIDOPSIS; SULFOQUINOVOSYL DIGLYCERIDE;

EID: 2442443097     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbi.2004.03.001     Document Type: Review
Times cited : (121)

References (52)
  • 3
    • 0032539557 scopus 로고    scopus 로고
    • Phosphate availability affects the thylakoid lipid composition and the expression of SQD1, a gene required for sulfolipid biosynthesis in Arabidopsis thaliana
    • Essigmann B., Güler S., Narang R.A., Linke D., Benning C. Phosphate availability affects the thylakoid lipid composition and the expression of SQD1, a gene required for sulfolipid biosynthesis in Arabidopsis thaliana. Proc Natl Acad Sci USA. 95:1998;1950-1955
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1950-1955
    • Essigmann, B.1    Güler, S.2    Narang, R.A.3    Linke, D.4    Benning, C.5
  • 4
    • 0037468511 scopus 로고    scopus 로고
    • Phosphate-deficient oat replaces a major portion of the plasma membrane phospholipids with the galactolipid digalactosyldiacylglycerol
    • Andersson M.X., Stridh M.H., Larsson K.E., Liljenberg C., Sandelius A.S. Phosphate-deficient oat replaces a major portion of the plasma membrane phospholipids with the galactolipid digalactosyldiacylglycerol. FEBS Lett. 537:2003;128-132
    • (2003) FEBS Lett , vol.537 , pp. 128-132
    • Andersson, M.X.1    Stridh, M.H.2    Larsson, K.E.3    Liljenberg, C.4    Sandelius, A.S.5
  • 5
    • 0038018596 scopus 로고    scopus 로고
    • Transient increase of phosphatidylcholine in plant cells in response to phosphate deprivation
    • Jouhet J., Maréchal E., Bligny R., Joyard J., Block M.A. Transient increase of phosphatidylcholine in plant cells in response to phosphate deprivation. FEBS Lett. 544:2003;63-68
    • (2003) FEBS Lett , vol.544 , pp. 63-68
    • Jouhet, J.1    Maréchal, E.2    Bligny, R.3    Joyard, J.4    Block, M.A.5
  • 6
    • 0036512409 scopus 로고    scopus 로고
    • Galactolipids rule in seed plants
    • Dörmann P., Benning C. Galactolipids rule in seed plants. Trends Plant Sci. 7:2002;112-118
    • (2002) Trends Plant Sci , vol.7 , pp. 112-118
    • Dörmann, P.1    Benning, C.2
  • 7
    • 0344514816 scopus 로고    scopus 로고
    • Disruption of the two digalactosyldiacylglycerolsynthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis
    • Kelly A.A., Froehlich J.E., Dörmann P. Disruption of the two digalactosyldiacylglycerolsynthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell. 15:2003;2694-2706
    • (2003) Plant Cell , vol.15 , pp. 2694-2706
    • Kelly, A.A.1    Froehlich, J.E.2    Dörmann, P.3
  • 8
    • 0031765216 scopus 로고    scopus 로고
    • Biosynthesis and function of the sulfolipid sulfoquinovosyl diacylglycerol
    • Benning C. Biosynthesis and function of the sulfolipid sulfoquinovosyl diacylglycerol. Annu Rev Plant Physiol Plant Mol Biol. 49:1998;53-75
    • (1998) Annu Rev Plant Physiol Plant Mol Biol , vol.49 , pp. 53-75
    • Benning, C.1
  • 9
    • 0041328335 scopus 로고    scopus 로고
    • Functional significance of the lipid-protein interface in photosynthetic membranes
    • Páli T., Garab G., Horváth L.I., Kóta Z. Functional significance of the lipid-protein interface in photosynthetic membranes. Cell Mol Life Sci. 60:2003;1591-1606
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1591-1606
    • Páli, T.1    Garab, G.2    Horváth, L.I.3    Kóta, Z.4
  • 10
    • 85051570592 scopus 로고
    • Phospholipid head groups
    • Edited by Moore TS. Boca Raton: CRC Press;
    • Kinney AJ: Phospholipid head groups. In Lipid Metabolism in Plants. Edited by Moore TS. Boca Raton: CRC Press; 1993:259-284.
    • (1993) Lipid Metabolism in Plants , pp. 259-284
    • Kinney, A.J.1
  • 11
    • 0028011616 scopus 로고
    • Biosynthesis of phosphatidylglycerol in isolated mitochondria of etiolated mung bean (Vigna radiata L.) seedlings
    • Griebau R., Frentzen M. Biosynthesis of phosphatidylglycerol in isolated mitochondria of etiolated mung bean (Vigna radiata L.) seedlings. Plant Physiol. 105:1994;1269-1274
    • (1994) Plant Physiol , vol.105 , pp. 1269-1274
    • Griebau, R.1    Frentzen, M.2
  • 12
    • 0028191081 scopus 로고
    • Biosynthesis of cardiolipin in plant mitochondria
    • Frentzen M., Griebau R. Biosynthesis of cardiolipin in plant mitochondria. Plant Physiol. 106:1994;1527-1532
    • (1994) Plant Physiol , vol.106 , pp. 1527-1532
    • Frentzen, M.1    Griebau, R.2
  • 13
    • 0035824852 scopus 로고    scopus 로고
    • Phosphatidylglycerophosphate synthases from Arabidopsis thaliana
    • Müller F., Frentzen M. Phosphatidylglycerophosphate synthases from Arabidopsis thaliana. FEBS Lett. 509:2001;298-302
    • (2001) FEBS Lett , vol.509 , pp. 298-302
    • Müller, F.1    Frentzen, M.2
  • 14
    • 0242669345 scopus 로고    scopus 로고
    • Arabidopsis phosphatidylglycerophosphate synthase 1 is essential for chloroplast differentiation, but is dispensable for mitochondrial function
    • 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.
    • 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.
    • (2003) Plant J , vol.33 , pp. 899-909
    • Babiychuk, E.1    Müller, F.2    Eubel, H.3    Braun, H.P.4    Frentzen, M.5    Kushnir, S.6
  • 15
    • 0032540270 scopus 로고    scopus 로고
    • The PEL1 gene (renamed PGS1) encodes the phosphatidylglycerophosphate synthase of Saccharomyces cerevisiae
    • Chang S.C., Heacock P.N., Clancey C.J., Dowhan W. The PEL1 gene (renamed PGS1) encodes the phosphatidylglycerophosphate synthase of Saccharomyces cerevisiae. J Biol Chem. 273:1998;9829-9836
    • (1998) J Biol Chem , vol.273 , pp. 9829-9836
    • Chang, S.C.1    Heacock, P.N.2    Clancey, C.J.3    Dowhan, W.4
  • 16
    • 0033555937 scopus 로고    scopus 로고
    • 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
    • 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
    • (1999) J Biol Chem , vol.274 , pp. 1828-1834
    • Kawasaki, K.1    Kuge, O.2    Chang, S.C.3    Heacock, P.N.4    Rho, M.5    Suzuki, K.6    Nishijima, M.7    Dowhan, W.8
  • 17
    • 0033792687 scopus 로고    scopus 로고
    • Direct evidence for requirement of phosphatidylglycerol in photosystem II of photosynthesis
    • 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
    • (2000) Plant Physiol , vol.124 , pp. 795-804
    • Hagio, M.1    Gombos, Z.2    Várkonyi, Z.3    Masamoto, K.4    Sato, N.5    Tsuzuki, M.6    Wada, H.7
  • 18
    • 0036949158 scopus 로고    scopus 로고
    • Phosphatidylglycerol is essential for the development of thylakoid membranes in Arabidopsis thaliana
    • 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.
    • 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.
    • (2002) Plant Cell Physiol , vol.43 , pp. 1456-1464
    • Hagio, M.1    Sakurai, I.2    Sato, S.3    Kato, T.4    Tabata, S.5    Wada, H.6
  • 19
    • 0035983626 scopus 로고    scopus 로고
    • The pgp1 mutant locus of Arabidopsis encodes a phosphatidylglycerolphosphate synthase with impaired activity
    • 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.
    • 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.
    • (2002) Plant Physiol , vol.129 , pp. 594-604
    • Xu, C.1    Härtel, H.2    Wada, H.3    Hagio, M.4    Yu, B.5    Eakin, C.6    Benning, C.7
  • 20
    • 0035816562 scopus 로고    scopus 로고
    • Lack of mitochondrial anionic phospholipids causes an inhibition of translation of protein components of the electron transport chain
    • 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
    • (2001) J Biol Chem , vol.276 , pp. 25262-25272
    • Ostrander, D.B.1    Zhang, M.2    Mileykovskaya, E.3    Rho, M.4    Dowhan, W.5
  • 21
    • 0343851738 scopus 로고    scopus 로고
    • A cyanobacterial gene, sqdX, required for biosynthesis of the sulfolipid sulfoquinovosyldiacylglycerol
    • Güler S., Essigmann B., Benning C. A cyanobacterial gene, sqdX, required for biosynthesis of the sulfolipid sulfoquinovosyldiacylglycerol. J Bacteriol. 182:2000;543-545
    • (2000) J Bacteriol , vol.182 , pp. 543-545
    • Güler, S.1    Essigmann, B.2    Benning, C.3
  • 22
    • 0035830866 scopus 로고    scopus 로고
    • Recombinant Arabidopsis SQD1 converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose in vitro
    • 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
    • (2001) J Biol Chem , vol.276 , pp. 3941-3946
    • Sanda, S.1    Leustek, T.2    Theisen, M.J.3    Garavito, R.M.4    Benning, C.5
  • 23
    • 0037117493 scopus 로고    scopus 로고
    • Arabidopsis disrupted in SQD2 encoding sulfolipid synthase is impaired in phosphate-limited growth
    • 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.
    • 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.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5732-5737
    • Yu, B.1    Xu, C.2    Benning, C.3
  • 24
    • 0142152446 scopus 로고    scopus 로고
    • The sulfolipids 2′-O-acyl-sulfoquinovosyldiacylglycerol and sulfoquinovosyldiacylglycerol are absent from a Chlamydomonas reinhardtii mutant deleted in SQD1
    • 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.
    • 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.
    • (2003) Plant Physiol , vol.133 , pp. 864-874
    • Riekhof, W.R.1    Ruckle, M.E.2    Lydic, T.A.3    Sears, B.B.4    Benning, C.5
  • 25
    • 2442512052 scopus 로고    scopus 로고
    • Identification of a gene for UDP-sulfoquinovose synthase of a green alga, Chlamydomonas reinhardtii, and its phylogeny
    • in press.
    • 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.
    • (2004) DNA Res
    • Sato, N.1    Sugimoto, K.2    Meguro, A.3    Tsuzuki, M.4
  • 27
    • 0033539608 scopus 로고    scopus 로고
    • Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose
    • 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
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13097-13102
    • Mulichak, A.M.1    Theisen, M.J.2    Essigmann, B.3    Benning, C.4    Garavito, R.M.5
  • 28
    • 0033199520 scopus 로고    scopus 로고
    • Prediction of the active-site structure and NAD(+) binding in SQD1, a protein essential for sulfolipid biosynthesis in Arabidopsis
    • 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
    • (1999) Arch Biochem Biophys , vol.369 , pp. 30-41
    • Essigmann, B.1    Hespenheide, B.M.2    Kuhn, L.A.3    Benning, C.4
  • 29
    • 0037404147 scopus 로고    scopus 로고
    • Native uridine 5′-diphosphate-sulfoquinovose synthase, SQD1, from spinach purifies as a 250-kDa complex
    • 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
    • (2003) Arch Biochem Biophys , vol.413 , pp. 123-130
    • Shimojima, M.1    Benning, C.2
  • 30
    • 0031857110 scopus 로고    scopus 로고
    • Uridine-diphospho-sulfoquinovose:diacylglycerol sulfoquinovosyltransferase activity is concentrated in the inner membrane of chloroplast envelopes
    • Tietje C., Heinz E. Uridine-diphospho-sulfoquinovose:diacylglycerol sulfoquinovosyltransferase activity is concentrated in the inner membrane of chloroplast envelopes. Planta. 206:1998;72-78
    • (1998) Planta , vol.206 , pp. 72-78
    • Tietje, C.1    Heinz, E.2
  • 31
    • 0034473217 scopus 로고    scopus 로고
    • Environmental effects on acidic lipids of thylakoid membranes
    • Sato N., Hagio M., Wada H., Tsuzuki M. Environmental effects on acidic lipids of thylakoid membranes. Biochem Soc Trans. 28:2000;912-914
    • (2000) Biochem Soc Trans , vol.28 , pp. 912-914
    • Sato, N.1    Hagio, M.2    Wada, H.3    Tsuzuki, M.4
  • 32
    • 0035845574 scopus 로고    scopus 로고
    • 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
    • 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
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10960-10965
    • Awai, K.1    Maréchal, E.2    Block, M.A.3    Brun, D.4    Masuda, T.5    Shimada, H.6    Takamiya, K.7    Ohta, H.8    Joyard, J.9
  • 34
    • 0035957413 scopus 로고    scopus 로고
    • Vipp1 deletion mutant of Synechocystis: A connection between bacterial phage shock and thylakoid biogenesis?
    • 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
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4243-4248
    • Westphal, S.1    Heins, L.2    Soll, J.3    Vothknecht, U.C.4
  • 35
    • 0038242363 scopus 로고    scopus 로고
    • A permease-like protein involved in ER to thylakoid lipid transfer in Arabidopsis
    • 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.).
    • 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.).
    • (2003) EMBO J , vol.22 , pp. 2370-2379
    • Xu, C.1    Fan, J.2    Riekhof, W.3    Frohlich, J.4    Benning, C.5
  • 36
    • 0029071399 scopus 로고
    • Isolation and characterization of mutants affected in lipid metabolism of Chlamydomonas reinhardtii
    • Sato N., Tsuzuki M., Matsuda Y., Ehara T., Osafune T., Kawaguchi A. Isolation and characterization of mutants affected in lipid metabolism of Chlamydomonas reinhardtii. Eur J Biochem. 230:1995;987-993
    • (1995) Eur J Biochem , vol.230 , pp. 987-993
    • Sato, N.1    Tsuzuki, M.2    Matsuda, Y.3    Ehara, T.4    Osafune, T.5    Kawaguchi, A.6
  • 37
    • 0036091099 scopus 로고    scopus 로고
    • Role of sulfoquinovosyl diacylglycerol for the maintenance of photosystem II in Chlamydomonas reinhardtii
    • The authors present genetic, physiological and biochemical analyses that clearly show that the defect in the PS II activity of the C. reinhardtii mutant hf-2, which was obtained by UV irradiation [36], is caused by a defect in SQDG biosynthesis in the mutant cells. They also report that PG cannot substitute for SQDG in maintaining the proper conformation of the PS II complex of C. reinhardtii and that the polar head groups of SQDG play a critical role in this regard.
    • Minoda A., Sato N., Nozaki H., Okada K., Takahashi H., Sonoike K., Tsuzuki M. Role of sulfoquinovosyl diacylglycerol for the maintenance of photosystem II in Chlamydomonas reinhardtii. Eur J Biochem. 269:2002;2353-2358 The authors present genetic, physiological and biochemical analyses that clearly show that the defect in the PS II activity of the C. reinhardtii mutant hf-2, which was obtained by UV irradiation [36], is caused by a defect in SQDG biosynthesis in the mutant cells. They also report that PG cannot substitute for SQDG in maintaining the proper conformation of the PS II complex of C. reinhardtii and that the polar head groups of SQDG play a critical role in this regard.
    • (2002) Eur J Biochem , vol.269 , pp. 2353-2358
    • Minoda, A.1    Sato, N.2    Nozaki, H.3    Okada, K.4    Takahashi, H.5    Sonoike, K.6    Tsuzuki, M.7
  • 38
    • 0347948395 scopus 로고    scopus 로고
    • Anionic lipids are required for chloroplast structure and function in Arabidopsis
    • ••], and of a sqd2 pgp1-1 double mutant were developed by extensive crossing experiments and analyzed in great detail. The sqd2 pgp1-1 double mutant, which carries a T-DNA insertion in the SQD2 gene and a point mutation in the PGP1 gene, lacks SQDG. Its PG level is reduced by 20% in the plastidial membranes, whereas the plastidial membranes of the single mutants contain total levels of anionic lipids that are very similar to those of the wildtype. A reduction in the total level of anionic membrane lipids in the plastidial membranes causes defects in photoautotrophic growth that are more severe than mere alterations in the composition of anionic membrane lipids. Unlike the single mutants, the double mutant also has alterations in its leaf structure, which are very similar to those of the Arabidopsis mutant that lacks plastidial PG [17]
    • ••], and of a sqd2 pgp1-1 double mutant were developed by extensive crossing experiments and analyzed in great detail. The sqd2 pgp1-1 double mutant, which carries a T-DNA insertion in the SQD2 gene and a point mutation in the PGP1 gene, lacks SQDG. Its PG level is reduced by 20% in the plastidial membranes, whereas the plastidial membranes of the single mutants contain total levels of anionic lipids that are very similar to those of the wildtype. A reduction in the total level of anionic membrane lipids in the plastidial membranes causes defects in photoautotrophic growth that are more severe than mere alterations in the composition of anionic membrane lipids. Unlike the single mutants, the double mutant also has alterations in its leaf structure, which are very similar to those of the Arabidopsis mutant that lacks plastidial PG [17]. Under phosphate-limiting conditions, the growth of the sqd1 pgp1-1 double mutant is impaired but not more severely than that of the sqd2 single mutant. Under these conditions, the mutants display very similar glycerolipid compositions in their plastidial membranes that explain their similar growth phenotypes.
    • (2003) Plant J , vol.36 , pp. 762-770
    • Yu, B.1    Benning, C.2
  • 39
    • 0028973107 scopus 로고
    • Impaired photosystem II in a mutant of Chlamydomonas reinhardtii defective in sulfoquinovosyl diacylglycerol
    • Sato N., Sonoike K., Tsuzuki M., Kawaguchi A. Impaired photosystem II in a mutant of Chlamydomonas reinhardtii defective in sulfoquinovosyl diacylglycerol. Eur J Biochem. 234:1995;16-23
    • (1995) Eur J Biochem , vol.234 , pp. 16-23
    • Sato, N.1    Sonoike, K.2    Tsuzuki, M.3    Kawaguchi, A.4
  • 40
    • 0141794511 scopus 로고    scopus 로고
    • Decrease in the efficiency of the electron donation to tyrosine Z of photosystem II in an SQDG-deficient mutant of Chlamydomonas
    • B in the PS II complex of the mutant cells. The severe alterations in the structure of the water-splitting complex caused by the lack of SQDG causes a reduction in PS II activity because electron transport from the Mn-cluster to tyrosine Z of the D1 protein is impaired.
    • B in the PS II complex of the mutant cells. The severe alterations in the structure of the water-splitting complex caused by the lack of SQDG causes a reduction in PS II activity because electron transport from the Mn-cluster to tyrosine Z of the D1 protein is impaired.
    • (2003) FEBS Lett , vol.553 , pp. 109-112
    • Minoda, A.1    Sonoike, K.2    Okada, K.3    Sato, N.4    Tsuzuki, M.5
  • 41
    • 0038082185 scopus 로고    scopus 로고
    • Involvement of sulfoquinovosyl diacylglycerol in the structural integrity and heat-tolerance of photosystem II
    • Sato N., Aoki M., Maru Y., Sonoike K., Minoda A., Tsuzuki M. Involvement of sulfoquinovosyl diacylglycerol in the structural integrity and heat-tolerance of photosystem II. Planta. 217:2003;245-251
    • (2003) Planta , vol.217 , pp. 245-251
    • Sato, N.1    Aoki, M.2    Maru, Y.3    Sonoike, K.4    Minoda, A.5    Tsuzuki, M.6
  • 42
    • 0034641708 scopus 로고    scopus 로고
    • Requirement of phosphatidylglycerol for photosynthetic function in thylakoid membranes
    • Sato N., Hagio M., Wada H., Tsuzuki M. Requirement of phosphatidylglycerol for photosynthetic function in thylakoid membranes. Proc Natl Acad Sci USA. 97:2000;10655-10660
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10655-10660
    • Sato, N.1    Hagio, M.2    Wada, H.3    Tsuzuki, M.4
  • 44
    • 0344961219 scopus 로고    scopus 로고
    • Requirement of phosphatidylglycerol for maintenance of photosynthetic machinery
    • 18 acyl group at the sn-1 and a palmitoyl group at the sn-2 position of the glycerol backbone, are more effective for this purpose than dioleoyl or dipalmitoyl species. Analyses of the restoration process provided evidence for the importance of PG in the dimerization and reactivation of the PS II core complex.
    • 18 acyl group at the sn-1 and a palmitoyl group at the sn-2 position of the glycerol backbone, are more effective for this purpose than dioleoyl or dipalmitoyl species. Analyses of the restoration process provided evidence for the importance of PG in the dimerization and reactivation of the PS II core complex.
    • (2003) Plant Physiol , vol.133 , pp. 1376-1384
    • Sakurai, I.1    Hagio, M.2    Gombos, Z.3    Tyystjärvi, T.4    Paakkarinen, V.5    Aro, E.M.6    Wada, H.7
  • 45
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krauss N. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature. 411:2001;909-917
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 47
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni A., Witt H.T., Kern J., Fromme P., Krauss N., Saenger W., Orth P. Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature. 409:2001;739-743
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 48
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanos at 3.7-Å resolution
    • Kamiya N., Shen J.R. Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanos at 3.7-Å resolution. Proc Natl Acad Sci USA. 100:2003;98-103
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 49
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee A.G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim Biophys Acta. 1612:2003;1-40
    • (2003) Biochim Biophys Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 50
    • 0001436643 scopus 로고
    • Altered regulation of lipid biosynthesis in a mutant Arabidopsis deficient in chloroplast glycerol-3-phosphate acyltransferase activity
    • Kunst L., Browse J., Somerville C. Altered regulation of lipid biosynthesis in a mutant Arabidopsis deficient in chloroplast glycerol-3-phosphate acyltransferase activity. Proc Natl Acad Sci USA. 85:1988;4143-4147
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4143-4147
    • Kunst, L.1    Browse, J.2    Somerville, C.3
  • 51
    • 0033988057 scopus 로고    scopus 로고
    • Viability of an Escherichia coli pgsA null mutant lacking detectable phosphatidylglycerol and cardiolipin
    • Kikuchi S., Shibuya I., Matsumoto K. Viability of an Escherichia coli pgsA null mutant lacking detectable phosphatidylglycerol and cardiolipin. J Bacteriol. 182:2000;371-376
    • (2000) J Bacteriol , vol.182 , pp. 371-376
    • Kikuchi, S.1    Shibuya, I.2    Matsumoto, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.