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Volumn 1636, Issue 2-3, 2004, Pages 205-212

Uptake and remodeling of exogenous phosphatidylethanolamine in E. coli

Author keywords

ACP; acyl carrier protein; CFA; CoA; coenzyme A; cyclopropane fatty acid; Cytosolic leaflet; DCPE; DCPS; dicaproylphosphatidylethanolamine; dicaproylphosphatidylserine; lipopolysaccharide; LPS; PE; Phosphatidylethanolamine; Phosphatidylserine

Indexed keywords

DICAPROYL(DI 6:0)PHOSPHATIDYLETHANOLAMINE; ETHANOLAMINE DERIVATIVE; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLSERINE; PHOSPHOLIPID; UNCLASSIFIED DRUG;

EID: 2942694180     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2004.01.002     Document Type: Review
Times cited : (11)

References (35)
  • 1
    • 0037203313 scopus 로고    scopus 로고
    • Phosphatidylcholine and cell death
    • Cui Z., Houweling M. Phosphatidylcholine and cell death. Biochim. Biophys. Acta. 1585:2002;87-96
    • (2002) Biochim. Biophys. Acta , vol.1585 , pp. 87-96
    • Cui, Z.1    Houweling, M.2
  • 2
    • 0030844660 scopus 로고    scopus 로고
    • Acyltransferases and transacylases involved in fatty acid remodeling of phospholipids and metabolism of bioactive lipids in mammalian cells
    • Yamashita A., Sugiura T., Waku K. Acyltransferases and transacylases involved in fatty acid remodeling of phospholipids and metabolism of bioactive lipids in mammalian cells. J. Biochem. (Tokyo). 122:1997;1-16
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 1-16
    • Yamashita, A.1    Sugiura, T.2    Waku, K.3
  • 4
    • 0033951375 scopus 로고    scopus 로고
    • Outer-membrane phospholipase A: Known structure, unknown biological function
    • Dekker N. Outer-membrane phospholipase A: known structure, unknown biological function. Mol. Microbiol. 35:2000;711-717
    • (2000) Mol. Microbiol. , vol.35 , pp. 711-717
    • Dekker, N.1
  • 6
    • 0019252655 scopus 로고
    • The uptake and acylation of exogenous lysophosphatidylethanolamine by Escherichia coli cells
    • Hellion P., Landry F., Subbaiah P.V., Proulx P. The uptake and acylation of exogenous lysophosphatidylethanolamine by Escherichia coli cells. Can. J. Biochem. 58:1980;1381-1386
    • (1980) Can. J. Biochem. , vol.58 , pp. 1381-1386
    • Hellion, P.1    Landry, F.2    Subbaiah, P.V.3    Proulx, P.4
  • 7
    • 0019966602 scopus 로고
    • Transacylation between diacylphospholipids and 2-acyl lysophospholipids catalyzed by Escherichia coli extract
    • Homma H., Nojima S. Transacylation between diacylphospholipids and 2-acyl lysophospholipids catalyzed by Escherichia coli extract. J. Biochem. (Tokyo). 91:1982;1093-1101
    • (1982) J. Biochem. (Tokyo) , vol.91 , pp. 1093-1101
    • Homma, H.1    Nojima, S.2
  • 8
    • 0021248354 scopus 로고
    • Turnover of fatty acids in the 1-position of phosphatidylethanolamine in Escherichia coli
    • Rock C.O. Turnover of fatty acids in the 1-position of phosphatidylethanolamine in Escherichia coli. J. Biol. Chem. 259:1984;6188-6194
    • (1984) J. Biol. Chem. , vol.259 , pp. 6188-6194
    • Rock, C.O.1
  • 9
    • 0014008387 scopus 로고
    • Acylation of lysophosphoglycerides by Escherichia coli
    • Proulx P.R., van Deenen L.L. Acylation of lysophosphoglycerides by Escherichia coli. Biochim. Biophys. Acta. 125:1966;591-593
    • (1966) Biochim. Biophys. Acta , vol.125 , pp. 591-593
    • Proulx, P.R.1    Van Deenen, L.L.2
  • 10
    • 0030962474 scopus 로고    scopus 로고
    • Quantitative analysis of biological membrane lipids at the low picomole level by nano-electrospray ionization tandem mass spectrometry
    • Brugger B., Erben G., Sandhoff R., Wieland F.T., Lehmann W.D. Quantitative analysis of biological membrane lipids at the low picomole level by nano-electrospray ionization tandem mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 94:1997;2339-2344
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2339-2344
    • Brugger, B.1    Erben, G.2    Sandhoff, R.3    Wieland, F.T.4    Lehmann, W.D.5
  • 11
    • 0346034955 scopus 로고    scopus 로고
    • The two biosynthetic routes leading to phosphatidylcholine in yeast produce different sets of molecular species, evidence for lipid remodeling
    • Boumann H.A., Damen M.J., Versluis C., Heck A.J., de Kruijff B., de Kroon A.I. The two biosynthetic routes leading to phosphatidylcholine in yeast produce different sets of molecular species, evidence for lipid remodeling. Biochemistry. 42:2003;3054-3059
    • (2003) Biochemistry , vol.42 , pp. 3054-3059
    • Boumann, H.A.1    Damen, M.J.2    Versluis, C.3    Heck, A.J.4    De Kruijff, B.5    De Kroon, A.I.6
  • 12
    • 0025881880 scopus 로고
    • Sequence and inactivation of the pss gene of Escherichia coli
    • De Chavigny A., Heacock P.N., Dowhan W. Sequence and inactivation of the pss gene of Escherichia coli. J. Biol. Chem. 266:1991;5323-5332
    • (1991) J. Biol. Chem. , vol.266 , pp. 5323-5332
    • De Chavigny, A.1    Heacock, P.N.2    Dowhan, W.3
  • 13
    • 0027999523 scopus 로고
    • Regulation of lipid polymorphism is essential for the viability of phosphatidylethanolamine-deficient Escherichia coli cells
    • Rietveld A.G., Chupin V.V., Koorengevel M.C., Wienk H.L., Dowhan W., de Kruijff B. Regulation of lipid polymorphism is essential for the viability of phosphatidylethanolamine-deficient Escherichia coli cells. J. Biol. Chem. 269:1994;28670-28675
    • (1994) J. Biol. Chem. , vol.269 , pp. 28670-28675
    • Rietveld, A.G.1    Chupin, V.V.2    Koorengevel, M.C.3    Wienk, H.L.4    Dowhan, W.5    De Kruijff, B.6
  • 14
    • 0023032318 scopus 로고
    • Transfer of fatty acids from the 1-position of phosphatidylethanolamine to the major outer membrane lipoprotein of Escherichia coli
    • Jackowski S., Rock C.O. Transfer of fatty acids from the 1-position of phosphatidylethanolamine to the major outer membrane lipoprotein of Escherichia coli. J. Biol. Chem. 261:1986;11328-11333
    • (1986) J. Biol. Chem. , vol.261 , pp. 11328-11333
    • Jackowski, S.1    Rock, C.O.2
  • 15
    • 0025871351 scopus 로고
    • Phosphatidylethanolamine is not essential for the N-acylation of apolipoprotein in Escherichia coli
    • Gupta S.D., Dowhan W., Wu H.C. Phosphatidylethanolamine is not essential for the N-acylation of apolipoprotein in Escherichia coli. J. Biol. Chem. 266:1991;9983-9986
    • (1991) J. Biol. Chem. , vol.266 , pp. 9983-9986
    • Gupta, S.D.1    Dowhan, W.2    Wu, H.C.3
  • 16
    • 0023654461 scopus 로고
    • Biosynthesis of lipid a precursors in Escherichia coli. a membrane-bound enzyme that transfers a palmitoyl residue from a glycerophospholipid to lipid X
    • Brozek K.A., Bulawa C.E., Raetz C.R. Biosynthesis of lipid A precursors in Escherichia coli. A membrane-bound enzyme that transfers a palmitoyl residue from a glycerophospholipid to lipid X. J. Biol. Chem. 262:1987;5170-5179
    • (1987) J. Biol. Chem. , vol.262 , pp. 5170-5179
    • Brozek, K.A.1    Bulawa, C.E.2    Raetz, C.R.3
  • 17
    • 0034596969 scopus 로고    scopus 로고
    • Transfer of palmitate from phospholipids to lipid a in outer membranes of gram-negative bacteria
    • Bishop R.E., Gibbons H.S., Guina T., Trent M.S., Miller S.I., Raetz C.R. Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. EMBO J. 19:2000;5071-5080
    • (2000) EMBO J. , vol.19 , pp. 5071-5080
    • Bishop, R.E.1    Gibbons, H.S.2    Guina, T.3    Trent, M.S.4    Miller, S.I.5    Raetz, C.R.6
  • 18
    • 0036566310 scopus 로고    scopus 로고
    • A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition
    • Bogdanov M., Heacock P.N., Dowhan W. A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition. EMBO J. 21:2002;2107-2116
    • (2002) EMBO J. , vol.21 , pp. 2107-2116
    • Bogdanov, M.1    Heacock, P.N.2    Dowhan, W.3
  • 19
    • 0035859890 scopus 로고    scopus 로고
    • Effect of nonbilayer lipids on membrane binding and insertion of the catalytic domain of leader peptidase
    • van den Brink-van der Laan E., Dalbey R.E., Demel R.A., Killian J.A., de Kruijff B. Effect of nonbilayer lipids on membrane binding and insertion of the catalytic domain of leader peptidase. Biochemistry. 40:2001;9677-9684
    • (2001) Biochemistry , vol.40 , pp. 9677-9684
    • Van Den Brink-Van Der Laan, E.1    Dalbey, R.E.2    Demel, R.A.3    Killian, J.A.4    De Kruijff, B.5
  • 20
    • 0021943192 scopus 로고
    • Interaction of lipid vesicles with an heptoseless strain of Escherichia coli
    • Proulx P. Interaction of lipid vesicles with an heptoseless strain of Escherichia coli. Exp. Biol. 43:1985;191-199
    • (1985) Exp. Biol. , vol.43 , pp. 191-199
    • Proulx, P.1
  • 23
    • 0022892440 scopus 로고
    • O-antigenic chains of lipopolysaccharide prevent binding of antibody molecules to an outer membrane pore protein in Enterobacteriaceae
    • van der Ley P., Kuipers O., Tommassen J., Lugtenberg B. O-antigenic chains of lipopolysaccharide prevent binding of antibody molecules to an outer membrane pore protein in Enterobacteriaceae. Microb. Pathog. 1:1986;43-49
    • (1986) Microb. Pathog. , vol.1 , pp. 43-49
    • Van Der Ley, P.1    Kuipers, O.2    Tommassen, J.3    Lugtenberg, B.4
  • 24
    • 0020055346 scopus 로고
    • A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels
    • Tsai C.M., Frasch C.E. A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Anal. Biochem. 119:1982;115-119
    • (1982) Anal. Biochem. , vol.119 , pp. 115-119
    • Tsai, C.M.1    Frasch, C.E.2
  • 25
    • 0018135125 scopus 로고
    • Enzymology, genetics, and regulation of membrane phospholipid synthesis in Escherichia coli
    • Raetz C.R. Enzymology, genetics, and regulation of membrane phospholipid synthesis in Escherichia coli. Microbiol. Rev. 42:1978;614-659
    • (1978) Microbiol. Rev. , vol.42 , pp. 614-659
    • Raetz, C.R.1
  • 26
    • 0031457094 scopus 로고    scopus 로고
    • Cyclopropane ring formation in membrane lipids of bacteria
    • Grogan D.W., Cronan J.E. Jr. Cyclopropane ring formation in membrane lipids of bacteria. Microbiol. Mol. Biol. Rev. 61:1997;429-441
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 429-441
    • Grogan, D.W.1    Cronan Jr., J.E.2
  • 27
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:1959;911-917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 28
    • 0019919547 scopus 로고
    • Unidimensional thin-layer chromatography of phospholipids on boric acid-impregnated plates
    • Fine J.B., Sprecher H. Unidimensional thin-layer chromatography of phospholipids on boric acid-impregnated plates. J. Lipid. Res. 23:1982;660-663
    • (1982) J. Lipid. Res. , vol.23 , pp. 660-663
    • Fine, J.B.1    Sprecher, H.2
  • 29
    • 0014779155 scopus 로고
    • Two dimensional thin layer chromatograpic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser G., Fleischer S., Yamamoto A. Two dimensional thin layer chromatograpic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids. 5:1970;494-496
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fleischer, S.2    Yamamoto, A.3
  • 30
    • 0035782884 scopus 로고    scopus 로고
    • Preventing drug access to targets: Cell surface permeability barriers and active efflux in bacteria
    • Nikaido H. Preventing drug access to targets: cell surface permeability barriers and active efflux in bacteria. Semin. Cell Dev. Biol. 12:2001;215-223
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 215-223
    • Nikaido, H.1
  • 31
    • 0017848437 scopus 로고
    • Escherichia coli mutants defective in membrane phospholipid synthesis: Binding and metabolism of 1-oleoylglycerol 3-phosphate by a plsB deep rough mutant
    • McIntyre T.M., Bell R.M. Escherichia coli mutants defective in membrane phospholipid synthesis: binding and metabolism of 1-oleoylglycerol 3-phosphate by a plsB deep rough mutant. J. Bacteriol. 135:1978;215-226
    • (1978) J. Bacteriol. , vol.135 , pp. 215-226
    • McIntyre, T.M.1    Bell, R.M.2
  • 32
    • 0016155281 scopus 로고
    • Purification and properties of phosphatidylserine decarboxylase from Escherichia coli
    • Dowhan W., Wickner W.T., Kennedy E.P. Purification and properties of phosphatidylserine decarboxylase from Escherichia coli. J. Biol. Chem. 249:1974;3079-3084
    • (1974) J. Biol. Chem. , vol.249 , pp. 3079-3084
    • Dowhan, W.1    Wickner, W.T.2    Kennedy, E.P.3
  • 33
    • 0020356830 scopus 로고
    • Membrane assembly: Movement of phosphatidylserine between the cytoplasmic and outer membranes of Escherichia coli
    • Langley K.E., Hawrot E., Kennedy E.P. Membrane assembly: movement of phosphatidylserine between the cytoplasmic and outer membranes of Escherichia coli. J. Bacteriol. 152:1982;1033-1041
    • (1982) J. Bacteriol. , vol.152 , pp. 1033-1041
    • Langley, K.E.1    Hawrot, E.2    Kennedy, E.P.3
  • 34
    • 0024505578 scopus 로고
    • Kinetic characterization of Escherichia coli outer membrane phospholipase a using mixed detergent-lipid micelles
    • Horrevoets A.J., Hackeng T.M., Verheij H.M., Dijkman R., de Haas G.H. Kinetic characterization of Escherichia coli outer membrane phospholipase A using mixed detergent-lipid micelles. Biochemistry. 28:1989;1139-1147
    • (1989) Biochemistry , vol.28 , pp. 1139-1147
    • Horrevoets, A.J.1    Hackeng, T.M.2    Verheij, H.M.3    Dijkman, R.4    De Haas, G.H.5
  • 35
    • 0017052667 scopus 로고
    • Nature of Escherichia coli mutants deficient in detergent-resistant and/or detergent-sensitive phospholipase a
    • Doi O., Nojima S. Nature of Escherichia coli mutants deficient in detergent-resistant and/or detergent-sensitive phospholipase A. J. Biochem. (Tokyo). 80:1976;1247-1258
    • (1976) J. Biochem. (Tokyo) , vol.80 , pp. 1247-1258
    • Doi, O.1    Nojima, S.2


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