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Volumn 1862, Issue 11, 2017, Pages 1287-1299

Bacterial lipid diversity

Author keywords

Lipid cycle; Lipid remodeling; Lipid turn over; Membrane lipid biosynthesis; Phospholipid

Indexed keywords

CARDIOLIPIN; CYTIDINE DIPHOSPHATE DIGLYCERIDE; DIACYLGLYCEROL; DIACYLGLYCERYL N,N,N TRIMETHYLHOMOSERINE; GLYCEROPHOSPHOLIPID; GLYCOLIPID; HOMOSERINE; HOPANOID; ISOPRENOID; MANNOSIDE; MEMBRANE LIPID; ORNITHINE; PHOSPHATIDIC ACID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLGLYCEROL; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL MANNOSIDE; SULFOLIPID SULFOQUINOVOSYL DIACYLGLYCEROL; UNCLASSIFIED DRUG;

EID: 85006117137     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2016.10.007     Document Type: Review
Times cited : (92)

References (134)
  • 1
    • 0004026407 scopus 로고    scopus 로고
    • Lehninger: Principles of Biochemistry
    • Sixth ed. W.H. Freeman and Company New York
    • Nelson, D.L., Cox, M.M., Lehninger: Principles of Biochemistry. Sixth ed., 2013, W.H. Freeman and Company, New York.
    • (2013)
    • Nelson, D.L.1    Cox, M.M.2
  • 2
    • 0001271789 scopus 로고
    • Phylogenetic strucutre of the prokaryotic domain: the primary kingdoms
    • Woese, C.R., Fox, G.E., Phylogenetic strucutre of the prokaryotic domain: the primary kingdoms. Proc. Natl. Acad. Sci. U. S. A. 74 (1977), 5088–5090.
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 5088-5090
    • Woese, C.R.1    Fox, G.E.2
  • 3
    • 79953654173 scopus 로고    scopus 로고
    • Early evolution of membrane lipids: how did the lipid divide occur?
    • Koga, Y., Early evolution of membrane lipids: how did the lipid divide occur?. J. Mol. Evol. 72 (2011), 274–282, 10.1007/s00239-011-9428-5.
    • (2011) J. Mol. Evol. , vol.72 , pp. 274-282
    • Koga, Y.1
  • 4
    • 0036942348 scopus 로고    scopus 로고
    • Analysis of membrane stereochemistry with homology modeling of sn-glycerol-1-phosphate dehydrogenase
    • Daiyasu, H., Hiroike, T., Koga, Y., Toh, H., Analysis of membrane stereochemistry with homology modeling of sn-glycerol-1-phosphate dehydrogenase. Protein Eng. 15 (2002), 987–995.
    • (2002) Protein Eng. , vol.15 , pp. 987-995
    • Daiyasu, H.1    Hiroike, T.2    Koga, Y.3    Toh, H.4
  • 5
    • 0018826602 scopus 로고
    • Regulation of phospholipid biosynthesis in Escherichia coli. Cloning of the structural gene for the biosynthetic sn-glycerol-3-phosphate dehydrogenase
    • Clark, D., Lightner, V., Edgar, R., Modrich, P., Cronan, J.E. Jr., Bell, R.M., Regulation of phospholipid biosynthesis in Escherichia coli. Cloning of the structural gene for the biosynthetic sn-glycerol-3-phosphate dehydrogenase. J. Biol. Chem. 255 (1980), 714–717.
    • (1980) J. Biol. Chem. , vol.255 , pp. 714-717
    • Clark, D.1    Lightner, V.2    Edgar, R.3    Modrich, P.4    Cronan, J.E.5    Bell, R.M.6
  • 6
    • 84873195314 scopus 로고    scopus 로고
    • Phosphatidic acid synthesis in bacteria
    • Yao, Y., Rock, C.O., Phosphatidic acid synthesis in bacteria. Biochim. Biophys. Acta 1831 (2013), 495–502, 10.1016/j.bbalip.2012.08.018.
    • (2013) Biochim. Biophys. Acta , vol.1831 , pp. 495-502
    • Yao, Y.1    Rock, C.O.2
  • 7
    • 0016747351 scopus 로고
    • Mutants of Escherichia coli defective in membrane phospholipid synthesis: properties of wild type and Km defective sn-glycerol-3-phosphate acyltransferase activities
    • Bell, R.M., Mutants of Escherichia coli defective in membrane phospholipid synthesis: properties of wild type and Km defective sn-glycerol-3-phosphate acyltransferase activities. J. Biol. Chem. 250 (1975), 7147–7152.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7147-7152
    • Bell, R.M.1
  • 8
    • 0019200914 scopus 로고
    • Membrane phospholipid synthesis in Escherichia coli: cloning of a structural gene (plsB) of the sn-glycerol-3-phosphate acyltransferase
    • Lightner, V.A., Larson, T.J., Tailleur, P., Kantor, G.D., Raetz, C.R.H., Bell, R.M., Modrich, P., Membrane phospholipid synthesis in Escherichia coli: cloning of a structural gene (plsB) of the sn-glycerol-3-phosphate acyltransferase. J. Biol. Chem. 255 (1980), 9413–9420.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9413-9420
    • Lightner, V.A.1    Larson, T.J.2    Tailleur, P.3    Kantor, G.D.4    Raetz, C.R.H.5    Bell, R.M.6    Modrich, P.7
  • 9
    • 0026459799 scopus 로고
    • Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase
    • (25513-22520)
    • Black, P.N., DiRusso, C.C., Metzger, A.K., Heimert, T.L., Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase. J. Biol. Chem., 267, 1992 (25513-22520).
    • (1992) J. Biol. Chem. , vol.267
    • Black, P.N.1    DiRusso, C.C.2    Metzger, A.K.3    Heimert, T.L.4
  • 10
    • 33747887074 scopus 로고    scopus 로고
    • Acyl phosphates initiate membrane phospholipid synthesis in gram-positive pathogens
    • Lu, Y.-J., Zhang, Y.-M., Grimes, K.D., Qi, J., Lee, R.E., Rock, C.O., Acyl phosphates initiate membrane phospholipid synthesis in gram-positive pathogens. Mol. Cell 23 (2006), 765–772.
    • (2006) Mol. Cell , vol.23 , pp. 765-772
    • Lu, Y.-J.1    Zhang, Y.-M.2    Grimes, K.D.3    Qi, J.4    Lee, R.E.5    Rock, C.O.6
  • 11
    • 0025131925 scopus 로고
    • Characterization of Escherichia coli cells deficient in 1-acyl-sn-glycerol-3-phosphate acyltransferase activity
    • Coleman, J., Characterization of Escherichia coli cells deficient in 1-acyl-sn-glycerol-3-phosphate acyltransferase activity. J. Biol. Chem. 265 (1990), 17215–17221.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17215-17221
    • Coleman, J.1
  • 12
    • 0026548077 scopus 로고
    • Characterization of the gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC)
    • Coleman, J., Characterization of the gene for 1-acyl-sn-glycerol-3-phosphate acyltransferase (plsC). Mol. Gen. Genet. 232 (1992), 295–303.
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 295-303
    • Coleman, J.1
  • 13
    • 0022355903 scopus 로고
    • Molecular cloning and sequencing of the gene for CDP-diglyceride synthetase of Escherichia coli
    • Icho, T., Sparrow, C.P., Raetz, C.R., Molecular cloning and sequencing of the gene for CDP-diglyceride synthetase of Escherichia coli. J. Biol. Chem. 260 (1985), 12078–12083.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12078-12083
    • Icho, T.1    Sparrow, C.P.2    Raetz, C.R.3
  • 14
    • 84875958424 scopus 로고    scopus 로고
    • Bacterial lipids: metabolism and membrane homeostasis
    • Parsons, J.B., Rock, C.O., Bacterial lipids: metabolism and membrane homeostasis. Prog. Lipid Res. 52 (2013), 249–276, 10.1016/j.plipres.2013.02.002.
    • (2013) Prog. Lipid Res. , vol.52 , pp. 249-276
    • Parsons, J.B.1    Rock, C.O.2
  • 15
    • 84962018311 scopus 로고    scopus 로고
    • Bacterial membrane lipids: diversity in structures and pathways
    • Sohlenkamp, C., Geiger, O., Bacterial membrane lipids: diversity in structures and pathways. FEMS Microbiol. Rev. 40 (2016), 133–159, 10.1093/femsre/fuv008.
    • (2016) FEMS Microbiol. Rev. , vol.40 , pp. 133-159
    • Sohlenkamp, C.1    Geiger, O.2
  • 16
    • 0025017436 scopus 로고
    • Biosynthesis and function of phospholipids in Escherichia coli
    • Raetz, C.R., Dowhan, W., Biosynthesis and function of phospholipids in Escherichia coli. J. Biol. Chem. 265 (1990), 1235–1238.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1235-1238
    • Raetz, C.R.1    Dowhan, W.2
  • 17
    • 0022964758 scopus 로고
    • Molecular genetics of membrane phospholipid synthesis
    • Raetz, C.R., Molecular genetics of membrane phospholipid synthesis. Annu. Rev. Genet. 20 (1986), 253–295.
    • (1986) Annu. Rev. Genet. , vol.20 , pp. 253-295
    • Raetz, C.R.1
  • 18
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: why are there so many lipids?
    • Dowhan, W., Molecular basis for membrane phospholipid diversity: why are there so many lipids?. Annu. Rev. Biochem. 66 (1997), 199–232.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 19
    • 84873100800 scopus 로고    scopus 로고
    • A retrospective: use of Escherichia coli as a vehicle to study phospholipid synthesis and function
    • Dowhan, W., A retrospective: use of Escherichia coli as a vehicle to study phospholipid synthesis and function. Biochim. Biophys. Acta 1831 (2013), 471–494, 10.1016/j.bbalip.2012.08.007.
    • (2013) Biochim. Biophys. Acta , vol.1831 , pp. 471-494
    • Dowhan, W.1
  • 20
    • 0025881880 scopus 로고
    • Sequence and inactivation of the pss gene of Escherichia coli. Phosphatidylethanolamine may not be essential for cell viability
    • DeChavigny, A., Heacock, P.N., Dowhan, W., Sequence and inactivation of the pss gene of Escherichia coli. Phosphatidylethanolamine may not be essential for cell viability. J. Biol. Chem. 266 (1991), 5323–5332.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5323-5332
    • DeChavigny, A.1    Heacock, P.N.2    Dowhan, W.3
  • 21
    • 1542286933 scopus 로고    scopus 로고
    • Phosphatidylethanolamine is not essential for growth of Sinorhizobium meliloti on complex culture media
    • Sohlenkamp, C., de Rudder, K.E., Geiger, O., Phosphatidylethanolamine is not essential for growth of Sinorhizobium meliloti on complex culture media. J. Bacteriol. 186 (2004), 1667–1677.
    • (2004) J. Bacteriol. , vol.186 , pp. 1667-1677
    • Sohlenkamp, C.1    de Rudder, K.E.2    Geiger, O.3
  • 22
    • 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
  • 23
    • 0025253340 scopus 로고
    • Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli
    • Li, Q.X., Dowhan, W., Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli. J. Biol. Chem. 265 (1990), 4111–4115.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4111-4115
    • Li, Q.X.1    Dowhan, W.2
  • 24
    • 84901433205 scopus 로고    scopus 로고
    • Discovery of a bifunctional cardiolipin/phosphatidylethanolamine synthase in bacteria
    • Moser, R., Aktas, M., Fritz, C., Narberhaus, F., Discovery of a bifunctional cardiolipin/phosphatidylethanolamine synthase in bacteria. Mol. Microbiol. 92 (2014), 959–972.
    • (2014) Mol. Microbiol. , vol.92 , pp. 959-972
    • Moser, R.1    Aktas, M.2    Fritz, C.3    Narberhaus, F.4
  • 25
    • 0030975483 scopus 로고    scopus 로고
    • Cloning of a human cDNA for CTP-phosphoethanolamine cytidylyltransferase by complementation in vivo of a yeast mutant
    • Nakashima, A., Hosaka, K., Nikawa, J., Cloning of a human cDNA for CTP-phosphoethanolamine cytidylyltransferase by complementation in vivo of a yeast mutant. J. Biol. Chem. 272 (1997), 9567–9572.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9567-9572
    • Nakashima, A.1    Hosaka, K.2    Nikawa, J.3
  • 26
    • 0001530898 scopus 로고
    • Phosphatidylcholine synthesis in Agrobacterium tumefaciens. I. Purification and properties of a phosphatidylethanolamine N-methyltransferase
    • Kaneshiro, T., Law, J.H., Phosphatidylcholine synthesis in Agrobacterium tumefaciens. I. Purification and properties of a phosphatidylethanolamine N-methyltransferase. J. Biol. Chem. 239 (1964), 1705–1713.
    • (1964) J. Biol. Chem. , vol.239 , pp. 1705-1713
    • Kaneshiro, T.1    Law, J.H.2
  • 28
    • 0027282594 scopus 로고
    • Isolation and functional expression in Escherichia coli of a gene encoding phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides
    • Arondel, V., Benning, C., Somerville, C.R., Isolation and functional expression in Escherichia coli of a gene encoding phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. J. Biol. Chem. 268 (1993), 16002–16008.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16002-16008
    • Arondel, V.1    Benning, C.2    Somerville, C.R.3
  • 29
    • 0033868330 scopus 로고    scopus 로고
    • Inactivation of the gene for phospholipid N-methyltransferase in Sinorhizobium meliloti: phosphatidylcholine is required for normal growth
    • de Rudder, K.E., López-Lara, I.M., Geiger, O., Inactivation of the gene for phospholipid N-methyltransferase in Sinorhizobium meliloti: phosphatidylcholine is required for normal growth. Mol. Microbiol. 37 (2000), 763–772.
    • (2000) Mol. Microbiol. , vol.37 , pp. 763-772
    • de Rudder, K.E.1    López-Lara, I.M.2    Geiger, O.3
  • 30
    • 38749145606 scopus 로고    scopus 로고
    • Multiple phospholipid N-methyltransferases with distinct substrate specificities are encoded in Bradyrhizobium japonicum
    • Hacker, S., Sohlenkamp, C., Aktas, M., Geiger, O., Narberhaus, F., Multiple phospholipid N-methyltransferases with distinct substrate specificities are encoded in Bradyrhizobium japonicum. J. Bacteriol. 190 (2008), 571–580.
    • (2008) J. Bacteriol. , vol.190 , pp. 571-580
    • Hacker, S.1    Sohlenkamp, C.2    Aktas, M.3    Geiger, O.4    Narberhaus, F.5
  • 31
    • 0023656673 scopus 로고
    • Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes
    • Kodaki, T., Yamashita, S., Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes. J. Biol. Chem. 262 (1987), 15428–15435.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15428-15435
    • Kodaki, T.1    Yamashita, S.2
  • 32
    • 0031552996 scopus 로고    scopus 로고
    • The phospholipid methyltransferases in yeast
    • Kanipes, M.I., Henry, S.A., The phospholipid methyltransferases in yeast. Biochim. Biophys. Acta 1348 (1997), 134–141.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 134-141
    • Kanipes, M.I.1    Henry, S.A.2
  • 34
    • 0033538510 scopus 로고    scopus 로고
    • Plant-exuded choline is used for rhizobial membrane lipid biosynthesis by phosphatidylcholine synthase
    • de Rudder, K.E., Sohlenkamp, C., Geiger, O., Plant-exuded choline is used for rhizobial membrane lipid biosynthesis by phosphatidylcholine synthase. J. Biol. Chem. 274 (1999), 20011–20016.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20011-20016
    • de Rudder, K.E.1    Sohlenkamp, C.2    Geiger, O.3
  • 36
    • 84873160884 scopus 로고    scopus 로고
    • Phosphatidylcholine biosynthesis and function in bacteria
    • Geiger, O., López-Lara, I.M., Sohlenkamp, C., Phosphatidylcholine biosynthesis and function in bacteria. Biochim. Biophys. Acta 1831 (2013), 503–513, 10.1016/j.bbalip.2012.08.009.
    • (2013) Biochim. Biophys. Acta , vol.1831 , pp. 503-513
    • Geiger, O.1    López-Lara, I.M.2    Sohlenkamp, C.3
  • 37
    • 0942301203 scopus 로고    scopus 로고
    • A CDP-choline pathway for phosphatidylcholine biosynthesis in Treponema denticola
    • Kent, C., Gee, P., Lee, S.Y., Bian, X., Fenno, J.C., A CDP-choline pathway for phosphatidylcholine biosynthesis in Treponema denticola. Mol. Microbiol. 51 (2004), 471–481.
    • (2004) Mol. Microbiol. , vol.51 , pp. 471-481
    • Kent, C.1    Gee, P.2    Lee, S.Y.3    Bian, X.4    Fenno, J.C.5
  • 39
    • 0024465134 scopus 로고
    • The molecular mechanism of phase variation of H. influenzae lipopolysaccharide
    • Weiser, J.N., Love, J.M., Moxon, E.R., The molecular mechanism of phase variation of H. influenzae lipopolysaccharide. Cell 59 (1989), 657–665.
    • (1989) Cell , vol.59 , pp. 657-665
    • Weiser, J.N.1    Love, J.M.2    Moxon, E.R.3
  • 40
  • 41
    • 84893727695 scopus 로고    scopus 로고
    • Phosphatidylcholine biosynthesis in Xanthomonas campestris via a yeast-like acylation pathway
    • Moser, R., Aktas, M., Narberhaus, F., Phosphatidylcholine biosynthesis in Xanthomonas campestris via a yeast-like acylation pathway. Mol. Microbiol. 91 (2014), 736–750.
    • (2014) Mol. Microbiol. , vol.91 , pp. 736-750
    • Moser, R.1    Aktas, M.2    Narberhaus, F.3
  • 42
    • 51449107757 scopus 로고    scopus 로고
    • Identification of a novel GPCAT activity and a new pathway for phosphatidylcholine biosynthesis in S. cerevisiae
    • Stalberg, K., Neal, A.C., Ronne, H., Ståhl, U., Identification of a novel GPCAT activity and a new pathway for phosphatidylcholine biosynthesis in S. cerevisiae. J. Lipid Res. 49 (2008), 1794–1806.
    • (2008) J. Lipid Res. , vol.49 , pp. 1794-1806
    • Stalberg, K.1    Neal, A.C.2    Ronne, H.3    Ståhl, U.4
  • 43
    • 0022346855 scopus 로고
    • Genetic manipulation of membrane phospholipid composition in Escherichia coli: pgsA mutants defective in phosphatidylglycerol synthesis
    • Miyazaki, C., Kuroda, M., Ohta, A., Shibuya, A.I., Genetic manipulation of membrane phospholipid composition in Escherichia coli: pgsA mutants defective in phosphatidylglycerol synthesis. Proc. Natl. Acad. Sci. U. S. A. 82 (1985), 7530–7534.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 7530-7534
    • Miyazaki, C.1    Kuroda, M.2    Ohta, A.3    Shibuya, A.I.4
  • 44
    • 0035056773 scopus 로고    scopus 로고
    • Dispensable nature of phosphatidylglycerol in Escherichia coli: dual roles of anionic phospholipids
    • Matsumoto, K., Dispensable nature of phosphatidylglycerol in Escherichia coli: dual roles of anionic phospholipids. Mol. Microbiol. 39 (2001), 1427–1433.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1427-1433
    • Matsumoto, K.1
  • 45
    • 0033792687 scopus 로고    scopus 로고
    • Direct evidence for requirement of phosphatidylglycerol in photosystem II of photosynthesis
    • Hagio, M., Gombos, Z., Varkonyi, 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    Varkonyi, Z.3    Masamoto, K.4    Sato, N.5    Tsuzuki, M.6    Wada, H.7
  • 46
    • 79953159519 scopus 로고    scopus 로고
    • Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli
    • Lu, Y.H., Guan, Z., Zhao, J., Raetz, C.R., Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli. J. Biol. Chem. 286 (2011), 5506–5518.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5506-5518
    • Lu, Y.H.1    Guan, Z.2    Zhao, J.3    Raetz, C.R.4
  • 47
    • 0014409327 scopus 로고
    • Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. I. Specificity of lysyl phosphatidylglycerol synthetase
    • Nesbitt, J.A. 3rd, Lennarz, W.J., Participation of aminoacyl transfer ribonucleic acid in aminoacyl phosphatidylglycerol synthesis. I. Specificity of lysyl phosphatidylglycerol synthetase. J. Biol. Chem. 243 (1968), 3088–3095.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3088-3095
    • Nesbitt, J.A.1    Lennarz, W.J.2
  • 49
    • 73549084991 scopus 로고    scopus 로고
    • The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion
    • Ernst, C.M., Staubitz, P., Mishra, N.N., Yang, S.J., Hornig, G., Kalbacher, H., Bayer, A.S., Kraus, D., Peschel, A., The bacterial defensin resistance protein MprF consists of separable domains for lipid lysinylation and antimicrobial peptide repulsion. PLoS Pathog., 5, 2009, e1000660, 10.1371/journal.ppat.1000660.
    • (2009) PLoS Pathog. , vol.5
    • Ernst, C.M.1    Staubitz, P.2    Mishra, N.N.3    Yang, S.J.4    Hornig, G.5    Kalbacher, H.6    Bayer, A.S.7    Kraus, D.8    Peschel, A.9
  • 50
    • 35349002810 scopus 로고    scopus 로고
    • The lipid lysyl-phosphatidylglycerol is present in membranes of Rhizobium tropici CIAT899 and confers increased resistance to polymyxin B under acidic growth conditions
    • Sohlenkamp, C., Galindo-Lagunas, K.A., Guan, Z., Vinuesa, P., Robinson, S., Thomas-Oates, J., Raetz, C.R., Geiger, O., The lipid lysyl-phosphatidylglycerol is present in membranes of Rhizobium tropici CIAT899 and confers increased resistance to polymyxin B under acidic growth conditions. Mol. Plant-Microbe Interact. 20 (2007), 1421–1430.
    • (2007) Mol. Plant-Microbe Interact. , vol.20 , pp. 1421-1430
    • Sohlenkamp, C.1    Galindo-Lagunas, K.A.2    Guan, Z.3    Vinuesa, P.4    Robinson, S.5    Thomas-Oates, J.6    Raetz, C.R.7    Geiger, O.8
  • 52
    • 70350417474 scopus 로고    scopus 로고
    • Broad range amino acid specificity of RNA-dependent lipid remodeling by multiple peptide resistance factors
    • Roy, H., Ibba, M., Broad range amino acid specificity of RNA-dependent lipid remodeling by multiple peptide resistance factors. J. Biol. Chem. 284 (2009), 29677–29683.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29677-29683
    • Roy, H.1    Ibba, M.2
  • 53
    • 84900559038 scopus 로고    scopus 로고
    • LysPGS formation in Listeria monocytogenes has broad roles in maintaining membrane integrity beyond antimicrobial peptide resistance
    • Dare, K., Shepherd, J., Roy, H., Seveau, S., Ibba, M., LysPGS formation in Listeria monocytogenes has broad roles in maintaining membrane integrity beyond antimicrobial peptide resistance. Virulence 5 (2014), 534–546.
    • (2014) Virulence , vol.5 , pp. 534-546
    • Dare, K.1    Shepherd, J.2    Roy, H.3    Seveau, S.4    Ibba, M.5
  • 54
    • 0037306656 scopus 로고    scopus 로고
    • Genetic analysis of a pH-regulated operon from Rhizobium tropici CIAT899 involved in acid tolerance and nodulation competitiveness
    • Vinuesa, P., Neumann-Silkow, F., Pacios-Bras, C., Spaink, H.P., Martínez-Romero, E., Werner, D., Genetic analysis of a pH-regulated operon from Rhizobium tropici CIAT899 involved in acid tolerance and nodulation competitiveness. Mol. Plant-Microbe Interact. 16 (2003), 159–168.
    • (2003) Mol. Plant-Microbe Interact. , vol.16 , pp. 159-168
    • Vinuesa, P.1    Neumann-Silkow, F.2    Pacios-Bras, C.3    Spaink, H.P.4    Martínez-Romero, E.5    Werner, D.6
  • 55
    • 84883159992 scopus 로고    scopus 로고
    • Identification and characterization of a periplasmic aminoacyl-phosphatidylglycerol hydrolase responsible for Pseudomonas aeruginosa lipid homeostasis
    • Arendt, W., Groenewold, M.K., Hebecker, S., Dickschat, J.S., Moser, J., Identification and characterization of a periplasmic aminoacyl-phosphatidylglycerol hydrolase responsible for Pseudomonas aeruginosa lipid homeostasis. J. Biol. Chem. 288 (2013), 24717–24730.
    • (2013) J. Biol. Chem. , vol.288 , pp. 24717-24730
    • Arendt, W.1    Groenewold, M.K.2    Hebecker, S.3    Dickschat, J.S.4    Moser, J.5
  • 56
    • 0032511048 scopus 로고    scopus 로고
    • Isolation and characterization of the gene (CLS1) encoding cardiolipin synthase in Saccharomyces cerevisiae
    • Chang, S.C., Heacock, P.N., Mileykovskaya, E., Voelker, D.R., Dowhan, W., Isolation and characterization of the gene (CLS1) encoding cardiolipin synthase in Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998), 14933–14941, 10.1074/jbc.273.24.14933.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14933-14941
    • Chang, S.C.1    Heacock, P.N.2    Mileykovskaya, E.3    Voelker, D.R.4    Dowhan, W.5
  • 57
    • 33748347104 scopus 로고    scopus 로고
    • Identification and functional characterization of hCLS1, a human cardiolipin synthase localized in mitochondria
    • Chen, D., Zhang, X.Y., Shi, Y., Identification and functional characterization of hCLS1, a human cardiolipin synthase localized in mitochondria. Biochem. J. 398 (2006), 169–176, 10.1042/BJ20060303.
    • (2006) Biochem. J. , vol.398 , pp. 169-176
    • Chen, D.1    Zhang, X.Y.2    Shi, Y.3
  • 58
    • 0023955825 scopus 로고
    • Disruption of the Escherichia coli cls gene responsible for cardiolipin synthesis
    • Nishijima, S., Asami, Y., Uetake, N., Yamagoe, S., Ohta, A., Shibuya, I., Disruption of the Escherichia coli cls gene responsible for cardiolipin synthesis. J. Bacteriol. 170 (1988), 775–780.
    • (1988) J. Bacteriol. , vol.170 , pp. 775-780
    • Nishijima, S.1    Asami, Y.2    Uetake, N.3    Yamagoe, S.4    Ohta, A.5    Shibuya, I.6
  • 59
    • 67650513311 scopus 로고    scopus 로고
    • A eukaryote-like cardiolipin synthase is present in Streptomyces coelicolor and in most actinobacteria
    • Sandoval-Calderón, M., Geiger, O., Guan, Z., Barona-Gómez, F., Sohlenkamp, C., A eukaryote-like cardiolipin synthase is present in Streptomyces coelicolor and in most actinobacteria. J. Biol. Chem. 284 (2009), 17383–17390.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17383-17390
    • Sandoval-Calderón, M.1    Geiger, O.2    Guan, Z.3    Barona-Gómez, F.4    Sohlenkamp, C.5
  • 60
    • 84859984887 scopus 로고    scopus 로고
    • An essential bacterial-type cardiolipin synthase mediates cardiolipin formation in a eukaryote
    • Serricchio, M., Butikofer, P., An essential bacterial-type cardiolipin synthase mediates cardiolipin formation in a eukaryote. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), E954–E961.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. E954-E961
    • Serricchio, M.1    Butikofer, P.2
  • 61
    • 84867362614 scopus 로고    scopus 로고
    • Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates
    • Tan, B.K., Bogdanov, M., Zhao, J., Dowhan, W., Raetz, C.R., Guan, Z., Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates. Proc. Natl. Acad. Sci. U. S. A. 109 (2012), 16504–16509.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 16504-16509
    • Tan, B.K.1    Bogdanov, M.2    Zhao, J.3    Dowhan, W.4    Raetz, C.R.5    Guan, Z.6
  • 62
    • 85014781334 scopus 로고    scopus 로고
    • Two distinct cardiolipin synthases operate in Agrobacterium tumefaciens
    • Czolkoss, S., Fritz, C., Hölzl, G., Aktas, M., Two distinct cardiolipin synthases operate in Agrobacterium tumefaciens. PLoS One, 11, 2016, e0160373, 10.1371/journal.pone.0160373.
    • (2016) PLoS One , vol.11
    • Czolkoss, S.1    Fritz, C.2    Hölzl, G.3    Aktas, M.4
  • 63
    • 0031553023 scopus 로고    scopus 로고
    • Phosphatidylinositol synthase from yeast
    • Nikawa, J., Yamashita, S., Phosphatidylinositol synthase from yeast. Biochim. Biophys. Acta 1348 (1997), 173–178.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 173-178
    • Nikawa, J.1    Yamashita, S.2
  • 64
    • 78049479263 scopus 로고    scopus 로고
    • A revised biosynthetic pathway for phosphatidylinositol in Mycobacteria
    • Morii, H., Ogawa, M., Fukuda, K., Taniguchi, H., Koga, Y., A revised biosynthetic pathway for phosphatidylinositol in Mycobacteria. J. Biochem. 148 (2010), 593–602.
    • (2010) J. Biochem. , vol.148 , pp. 593-602
    • Morii, H.1    Ogawa, M.2    Fukuda, K.3    Taniguchi, H.4    Koga, Y.5
  • 65
    • 84890856062 scopus 로고    scopus 로고
    • Ubiquitous distribution of phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase in bacteria and archaea, which contain inositol phospholipid
    • Morii, H., Ogawa, M., Fukuda, K., Taniguchi, H., Ubiquitous distribution of phosphatidylinositol phosphate synthase and archaetidylinositol phosphate synthase in bacteria and archaea, which contain inositol phospholipid. Biochem. Biophys. Res. Commun. 443 (2014), 86–90.
    • (2014) Biochem. Biophys. Res. Commun. , vol.443 , pp. 86-90
    • Morii, H.1    Ogawa, M.2    Fukuda, K.3    Taniguchi, H.4
  • 66
    • 0034730751 scopus 로고    scopus 로고
    • Phosphatidylinositol is an essential phospholipid of mycobacteria
    • Jackson, M., Crick, D.C., Brennan, P.J., Phosphatidylinositol is an essential phospholipid of mycobacteria. J. Biol. Chem. 275 (2000), 30092–30099.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30092-30099
    • Jackson, M.1    Crick, D.C.2    Brennan, P.J.3
  • 67
    • 0015014476 scopus 로고
    • The phospholipid composition of Rhizobium japonicum
    • Bunn, C.R., Elkan, G.H., The phospholipid composition of Rhizobium japonicum. Can. J. Microbiol. 17 (1971), 291–295.
    • (1971) Can. J. Microbiol. , vol.17 , pp. 291-295
    • Bunn, C.R.1    Elkan, G.H.2
  • 68
    • 0025042856 scopus 로고
    • The phospholipid composition of Bradyrhizobium spp.
    • Miller, K.J., Shon, B.C., Gore, R.S., Hunt, W.P., The phospholipid composition of Bradyrhizobium spp. Curr. Microbiol. 21 (1990), 205–210, 10.1007/BF02092123.
    • (1990) Curr. Microbiol. , vol.21 , pp. 205-210
    • Miller, K.J.1    Shon, B.C.2    Gore, R.S.3    Hunt, W.P.4
  • 69
    • 84937073217 scopus 로고    scopus 로고
    • A novel pathway for the synthesis of inositol phospholipids uses cytidine diphosphate (CDP)-inositol as donor of the polar head group
    • Jorge, C.D., Borges, N., Santos, H., A novel pathway for the synthesis of inositol phospholipids uses cytidine diphosphate (CDP)-inositol as donor of the polar head group. Environ. Microbiol. 17 (2015), 2492–2504, 10.1111/1462-2920.12734.
    • (2015) Environ. Microbiol. , vol.17 , pp. 2492-2504
    • Jorge, C.D.1    Borges, N.2    Santos, H.3
  • 70
    • 84940499894 scopus 로고    scopus 로고
    • Chlamydia trachomatis relies on autonomous phospholipid synthesis for membrane biogenesis
    • Yao, J., Cherian, P.T., Frank, M.W., Rock, C.O., Chlamydia trachomatis relies on autonomous phospholipid synthesis for membrane biogenesis. J. Biol. Chem. 290 (2015), 18874–18888, 10.1074/jbc.M115.657148.
    • (2015) J. Biol. Chem. , vol.290 , pp. 18874-18888
    • Yao, J.1    Cherian, P.T.2    Frank, M.W.3    Rock, C.O.4
  • 72
    • 84941022865 scopus 로고    scopus 로고
    • Unconventional membrane lipid biosynthesis in Xanthomonas campestris
    • Aktas, M., Narberhaus, F., Unconventional membrane lipid biosynthesis in Xanthomonas campestris. Environ. Microbiol. 17 (2015), 3116–3124, 10.1111/1462-2920.12956.
    • (2015) Environ. Microbiol. , vol.17 , pp. 3116-3124
    • Aktas, M.1    Narberhaus, F.2
  • 74
    • 84924939876 scopus 로고    scopus 로고
    • How bacterial pathogens eat host lipids: implications for the development of fatty acid synthesis therapeutics
    • Yao, J., Rock, C.O., How bacterial pathogens eat host lipids: implications for the development of fatty acid synthesis therapeutics. J. Biol. Chem. 290 (2015), 5940–5946, 10.1074/jbc.R114.636241.
    • (2015) J. Biol. Chem. , vol.290 , pp. 5940-5946
    • Yao, J.1    Rock, C.O.2
  • 75
    • 0031848910 scopus 로고    scopus 로고
    • A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products
    • Jorasch, P., Wolter, W.P., Zähringer, U., Heinz, E., A UDP glucosyltransferase from Bacillus subtilis successively transfers up to four glucose residues to 1,2-diacylglycerol: expression of ypfP in Escherichia coli and structural analysis of its reaction products. Mol. Microbiol. 29 (1998), 419–430.
    • (1998) Mol. Microbiol. , vol.29 , pp. 419-430
    • Jorasch, P.1    Wolter, W.P.2    Zähringer, U.3    Heinz, E.4
  • 76
    • 79952422504 scopus 로고    scopus 로고
    • A processive glycosyltransferase involved in glycolipid synthesis during phosphate deprivation in Mesorhizobium loti
    • Devers, E.A., Wewer, V., Dombrink, I., Dörmann, P., Hölzl, G., A processive glycosyltransferase involved in glycolipid synthesis during phosphate deprivation in Mesorhizobium loti. J. Bacteriol. 193 (2011), 1377–1384, 10.1128/JB.00768-10.
    • (2011) J. Bacteriol. , vol.193 , pp. 1377-1384
    • Devers, E.A.1    Wewer, V.2    Dombrink, I.3    Dörmann, P.4    Hölzl, G.5
  • 77
    • 34447637768 scopus 로고    scopus 로고
    • Structure and function of glycoglycerolipids in plants and bacteria
    • Hölzl, G., Dörmann, P., Structure and function of glycoglycerolipids in plants and bacteria. Prog. Lipid Res. 46 (2007), 225–243.
    • (2007) Prog. Lipid Res. , vol.46 , pp. 225-243
    • Hölzl, G.1    Dörmann, P.2
  • 80
    • 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
  • 81
    • 0343851738 scopus 로고    scopus 로고
    • A cyanobacterial gene, sqdX, required for biosynthesis of the sulfolipid sulfoquinovosyldiacylglycerol
    • Güler, S., Essigmann, S.B., Benning, B.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, S.B.2    Benning, B.C.3
  • 82
    • 79952859874 scopus 로고    scopus 로고
    • Biosynthesis and functions of the plant sulfolipid
    • Shimojima, M., Biosynthesis and functions of the plant sulfolipid. Prog. Lipid Res. 50 (2011), 234–239, 10.1016/j.plipres.2011.02.003.
    • (2011) Prog. Lipid Res. , vol.50 , pp. 234-239
    • Shimojima, M.1
  • 83
    • 84956751521 scopus 로고    scopus 로고
    • Identification of genes for sulfolipid synthesis in primitive red alga Cyanidioschyzon merolae
    • Sato, N., Kobayashi, S., Aoki, M., Umemura, T., Kobayashi, I., Tsuzuki, M., Identification of genes for sulfolipid synthesis in primitive red alga Cyanidioschyzon merolae. Biochem. Biophys. Res. Commun. 470 (2016), 123–129, 10.1016/j.bbrc.2016.01.006.
    • (2016) Biochem. Biophys. Res. Commun. , vol.470 , pp. 123-129
    • Sato, N.1    Kobayashi, S.2    Aoki, M.3    Umemura, T.4    Kobayashi, I.5    Tsuzuki, M.6
  • 84
    • 0032910352 scopus 로고    scopus 로고
    • The regulator gene phoB mediates phosphate stress-controlled synthesis of the membrane lipid diacylglyceryl-N,N,N-trimethylhomoserine in Rhizobium (Sinorhizobium) meliloti
    • Geiger, O., Röhrs, V., Weissenmayer, B., Finan, T.M., Thomas-Oates, J.E., The regulator gene phoB mediates phosphate stress-controlled synthesis of the membrane lipid diacylglyceryl-N,N,N-trimethylhomoserine in Rhizobium (Sinorhizobium) meliloti. Mol. Microbiol. 32 (1999), 63–73.
    • (1999) Mol. Microbiol. , vol.32 , pp. 63-73
    • Geiger, O.1    Röhrs, V.2    Weissenmayer, B.3    Finan, T.M.4    Thomas-Oates, J.E.5
  • 86
    • 0035826862 scopus 로고    scopus 로고
    • Two enzymes of diacylglyceryl-O-4′-(N,N,N,-trimethyl)homoserine biosynthesis are encoded by btaA and btaB in the purple bacterium Rhodobacter sphaeroides
    • Klug, R.M., Benning, C., Two enzymes of diacylglyceryl-O-4′-(N,N,N,-trimethyl)homoserine biosynthesis are encoded by btaA and btaB in the purple bacterium Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 5910–5915.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 5910-5915
    • Klug, R.M.1    Benning, C.2
  • 87
    • 23844473772 scopus 로고    scopus 로고
    • Phosphorus-free membrane lipids of Sinorhizobium meliloti are not required for the symbiosis with alfalfa but contribute to increased cell yields under phosphorus-limiting conditions of growth
    • López-Lara, I.M., Gao, J.L., Soto, M.J., Solares-Pérez, A., Weissenmayer, B., Sohlenkamp, C., Verroios, G.P., Thomas-Oates, J., Geiger, O., Phosphorus-free membrane lipids of Sinorhizobium meliloti are not required for the symbiosis with alfalfa but contribute to increased cell yields under phosphorus-limiting conditions of growth. Mol. Plant-Microbe Interact. 18 (2005), 973–982.
    • (2005) Mol. Plant-Microbe Interact. , vol.18 , pp. 973-982
    • López-Lara, I.M.1    Gao, J.L.2    Soto, M.J.3    Solares-Pérez, A.4    Weissenmayer, B.5    Sohlenkamp, C.6    Verroios, G.P.7    Thomas-Oates, J.8    Geiger, O.9
  • 89
    • 0001126536 scopus 로고
    • Metabolism of glycerolipides; a comparison of lecithin and triglyceride synthesis
    • Lands, W.E., Metabolism of glycerolipides; a comparison of lecithin and triglyceride synthesis. J. Biol. Chem. 231 (1958), 883–888.
    • (1958) J. Biol. Chem. , vol.231 , pp. 883-888
    • Lands, W.E.1
  • 90
    • 84926637728 scopus 로고    scopus 로고
    • Delivery of cardiolipins to the Salmonella outer membrane is necessary for survival within host tissues and virulence
    • Dalebroux, Z.D., Edrozo, M.B., Pfuetzner, R.A., Ressl, S., Kulasekara, B.R., Blanc, M.P., Miller, S.I., Delivery of cardiolipins to the Salmonella outer membrane is necessary for survival within host tissues and virulence. Cell Host Microbe 17 (2015), 441–451, 10.1016/j.chom.2015.03.003.
    • (2015) Cell Host Microbe , vol.17 , pp. 441-451
    • Dalebroux, Z.D.1    Edrozo, M.B.2    Pfuetzner, R.A.3    Ressl, S.4    Kulasekara, B.R.5    Blanc, M.P.6    Miller, S.I.7
  • 91
    • 84962526314 scopus 로고    scopus 로고
    • Disruption of lipid homeostasis in the gram-negative cell envelope activates a novel cell death pathway
    • Sutterlin, H.A., Shi, H., May, K.L., Miguel, A., Khare, S., Huang, K.C., Silhavy, T.J., Disruption of lipid homeostasis in the gram-negative cell envelope activates a novel cell death pathway. Proc. Natl. Acad. Sci. U. S. A. 113 (2016), E1565–E1574, 10.1073/pnas.1601375113.
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. E1565-E1574
    • Sutterlin, H.A.1    Shi, H.2    May, K.L.3    Miguel, A.4    Khare, S.5    Huang, K.C.6    Silhavy, T.J.7
  • 92
    • 84882460199 scopus 로고    scopus 로고
    • Fatty acid and phospholipid metabolism in prokaryotes
    • D.E. Vance J.E. Vance Fifth ed. Elsevier Amsterdam
    • Rock, C.O., Fatty acid and phospholipid metabolism in prokaryotes. Vance, D.E., Vance, J.E., (eds.) Biochemistry of Lipids, Lipoproteins and Membranes, Fifth ed., 2008, Elsevier, Amsterdam, 59–96.
    • (2008) Biochemistry of Lipids, Lipoproteins and Membranes , pp. 59-96
    • Rock, C.O.1
  • 93
    • 15744371593 scopus 로고    scopus 로고
    • Lysophospholipid flipping across the Escherichia coli inner membrane catalyzed by a transporter (LplT) belonging to the major facilitator superfamily
    • Harvat, E.M., Zhang, Y.M., Tran, C.V., Zhang, Z., Frank, M.W., Rock, R.O., Saier, M.H. Jr., Lysophospholipid flipping across the Escherichia coli inner membrane catalyzed by a transporter (LplT) belonging to the major facilitator superfamily. J. Biol. Chem. 280 (2005), 12028–12034, 10.1074/jbc.M414368200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12028-12034
    • Harvat, E.M.1    Zhang, Y.M.2    Tran, C.V.3    Zhang, Z.4    Frank, M.W.5    Rock, R.O.6    Saier, M.H.7
  • 94
    • 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
  • 95
    • 84957014375 scopus 로고    scopus 로고
    • Substrate selectivity of lysophospholipid transporter LplT involved in membrane phospholipid remodeling in Escherichia coli
    • Lin, Y., Bogdanov, M., Tong, S., Guan, Z., Zheng, L., Substrate selectivity of lysophospholipid transporter LplT involved in membrane phospholipid remodeling in Escherichia coli. J. Biol. Chem. 291 (2016), 2136–2149, 10.1074/jbc.M115.700419.
    • (2016) J. Biol. Chem. , vol.291 , pp. 2136-2149
    • Lin, Y.1    Bogdanov, M.2    Tong, S.3    Guan, Z.4    Zheng, L.5
  • 96
    • 59149094865 scopus 로고    scopus 로고
    • Phosphatidic acid and N-acylphosphatidylethanolamine form membrane domains in Escherichia coli mutant lacking cardiolipin and phosphatidylglycerol
    • Mileykovskaya, E., Ryan, A.C., Mo, X., Lin, C.C., Khalaf, K.I., Dowhan, W., Garrett, T.A., Phosphatidic acid and N-acylphosphatidylethanolamine form membrane domains in Escherichia coli mutant lacking cardiolipin and phosphatidylglycerol. J. Biol. Chem. 284 (2009), 2990–3000, 10.1074/jbc.M805189200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2990-3000
    • Mileykovskaya, E.1    Ryan, A.C.2    Mo, X.3    Lin, C.C.4    Khalaf, K.I.5    Dowhan, W.6    Garrett, T.A.7
  • 97
    • 0034192848 scopus 로고    scopus 로고
    • Osmoregulated periplasmic glucans in proteobacteria
    • Bohin, J.P., Osmoregulated periplasmic glucans in proteobacteria. FEMS Microbiol. Lett. 186 (2000), 11–19.
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 11-19
    • Bohin, J.P.1
  • 98
    • 0015788196 scopus 로고
    • Metabolism of membrane phospholipids and its relation to a novel class of oligosaccharides in Escherichia coli
    • van Golde, L.M.G., Schulman, H., Kennedy, E.P., Metabolism of membrane phospholipids and its relation to a novel class of oligosaccharides in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 70 (1973), 1368–1372.
    • (1973) Proc. Natl. Acad. Sci. U. S. A. , vol.70 , pp. 1368-1372
    • van Golde, L.M.G.1    Schulman, H.2    Kennedy, E.P.3
  • 101
    • 0024094914 scopus 로고
    • Phosphoglycerol substituents present on the cyclic β-1,2-glucans of Rhizobium meliloti 1021 are derived from phosphatidylglycerol
    • Miller, K.J., Gore, R.S., Benesi, A.J., Phosphoglycerol substituents present on the cyclic β-1,2-glucans of Rhizobium meliloti 1021 are derived from phosphatidylglycerol. J. Bacteriol. 170 (1988), 4569–4575.
    • (1988) J. Bacteriol. , vol.170 , pp. 4569-4575
    • Miller, K.J.1    Gore, R.S.2    Benesi, A.J.3
  • 102
    • 0032793687 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of the cgmB gene of Sinorhizobium meliloti involved in cyclic β-glucan biosynthesis
    • Wang, P., Ingram-Smith, C., Hadley, J.A., Miller, K.J., Cloning, sequencing, and characterization of the cgmB gene of Sinorhizobium meliloti involved in cyclic β-glucan biosynthesis. J. Bacteriol. 181 (1999), 4576–4583.
    • (1999) J. Bacteriol. , vol.181 , pp. 4576-4583
    • Wang, P.1    Ingram-Smith, C.2    Hadley, J.A.3    Miller, K.J.4
  • 103
    • 33646111710 scopus 로고    scopus 로고
    • Identification of Sinorhizobium meliloti early symbiotic genes by use of a positive functional screen
    • Zhang, X.S., Cheng, H.P., Identification of Sinorhizobium meliloti early symbiotic genes by use of a positive functional screen. Appl. Environ. Microbiol. 72 (2006), 2738–2748.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2738-2748
    • Zhang, X.S.1    Cheng, H.P.2
  • 108
    • 84876910795 scopus 로고    scopus 로고
    • Metabolic plasticity for isoprenoid biosynthesis in bacteria
    • Pérez-Gil, J., Rodríguez-Concepción, M., Metabolic plasticity for isoprenoid biosynthesis in bacteria. Biochem. J. 452 (2013), 19–25, 10.1042/BJ20121899.
    • (2013) Biochem. J. , vol.452 , pp. 19-25
    • Pérez-Gil, J.1    Rodríguez-Concepción, M.2
  • 109
    • 84902143379 scopus 로고    scopus 로고
    • Deciphering the metabolism of undecaprenyl-phosphate: the bacterial cell-wall unit carrier at the membrane frontier
    • Manat, G., Roure, S., Auger, R., Bouhss, A., Barreteau, H., Mengin-Lecreulx, D., Touzé, T., Deciphering the metabolism of undecaprenyl-phosphate: the bacterial cell-wall unit carrier at the membrane frontier. Microb. Drug Resist. 20 (2014), 199–214, 10.1089/mdr.2014.0035.
    • (2014) Microb. Drug Resist. , vol.20 , pp. 199-214
    • Manat, G.1    Roure, S.2    Auger, R.3    Bouhss, A.4    Barreteau, H.5    Mengin-Lecreulx, D.6    Touzé, T.7
  • 110
    • 4644364774 scopus 로고    scopus 로고
    • Identification of a gene required for the formation of lyso-ornithine lipid, an intermediate in the biosynthesis of ornithine-containing lipids
    • Gao, J.L., Weissenmayer, B., Taylor, A.M., Thomas-Oates, J., López-Lara, I.M., Geiger, O., Identification of a gene required for the formation of lyso-ornithine lipid, an intermediate in the biosynthesis of ornithine-containing lipids. Mol. Microbiol. 53 (2004), 1757–1770.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1757-1770
    • Gao, J.L.1    Weissenmayer, B.2    Taylor, A.M.3    Thomas-Oates, J.4    López-Lara, I.M.5    Geiger, O.6
  • 111
    • 0034112448 scopus 로고    scopus 로고
    • Disruption of a gene essential for sulfoquinosyldiacylglycerol biosynthesis in Sinorhizobium meliloti has no detectable effect on root nodule symbiosis
    • Weissenmayer, B., Geiger, O., Benning, C., Disruption of a gene essential for sulfoquinosyldiacylglycerol biosynthesis in Sinorhizobium meliloti has no detectable effect on root nodule symbiosis. Mol. Plant-Microbe Interact. 13 (2000), 666–672.
    • (2000) Mol. Plant-Microbe Interact. , vol.13 , pp. 666-672
    • Weissenmayer, B.1    Geiger, O.2    Benning, C.3
  • 114
    • 79960529850 scopus 로고    scopus 로고
    • The dioxygenase-encoding olsD gene from Burkholderia cenocepacia causes the hydroxylation of the amide-linked fatty acyl moiety of ornithine-containing membrane lipids
    • González-Silva, N., López-Lara, I.M., Reyes-Lamothe, R., Taylor, A.M., Sumpton, D., Thomas-Oates, J., Geiger, O., The dioxygenase-encoding olsD gene from Burkholderia cenocepacia causes the hydroxylation of the amide-linked fatty acyl moiety of ornithine-containing membrane lipids. Biochemistry 50 (2011), 6396–6408.
    • (2011) Biochemistry , vol.50 , pp. 6396-6408
    • González-Silva, N.1    López-Lara, I.M.2    Reyes-Lamothe, R.3    Taylor, A.M.4    Sumpton, D.5    Thomas-Oates, J.6    Geiger, O.7
  • 115
    • 26944494517 scopus 로고    scopus 로고
    • A ClC chloride channel homolog and ornithine-containing membrane lipids of Rhizobium tropici CIAT899 are involved in symbiotic efficiency and acid tolerance
    • Rojas-Jiménez, K., Sohlenkamp, C., Geiger, O., Martínez-Romero, E., Werner, D., Vinuesa, P., A ClC chloride channel homolog and ornithine-containing membrane lipids of Rhizobium tropici CIAT899 are involved in symbiotic efficiency and acid tolerance. Mol. Plant-Microbe Interact. 18 (2005), 1175–1185.
    • (2005) Mol. Plant-Microbe Interact. , vol.18 , pp. 1175-1185
    • Rojas-Jiménez, K.1    Sohlenkamp, C.2    Geiger, O.3    Martínez-Romero, E.4    Werner, D.5    Vinuesa, P.6
  • 116
    • 84866159077 scopus 로고    scopus 로고
    • Ornithine lipids and their structural modifications: from A to E and beyond
    • Vences-Guzmán, M.A., Geiger, O., Sohlenkamp, C., Ornithine lipids and their structural modifications: from A to E and beyond. FEMS Microbiol. Lett. 335 (2012), 1–10, 10.1111/j.1574-6968.2012.02623.x.
    • (2012) FEMS Microbiol. Lett. , vol.335 , pp. 1-10
    • Vences-Guzmán, M.A.1    Geiger, O.2    Sohlenkamp, C.3
  • 118
    • 84920811193 scopus 로고    scopus 로고
    • Accumulation of novel glycolipids and ornithine lipids in Mesorhizobium loti under phosphate deprivation
    • Diercks, H., Semeniuk, H.A., Gisch, A.N., Moll, H., Duda, K.A., Holzl, G., Accumulation of novel glycolipids and ornithine lipids in Mesorhizobium loti under phosphate deprivation. J. Bacteriol. 197 (2015), 497–509.
    • (2015) J. Bacteriol. , vol.197 , pp. 497-509
    • Diercks, H.1    Semeniuk, H.A.2    Gisch, A.N.3    Moll, H.4    Duda, K.A.5    Holzl, G.6
  • 120
    • 0020081836 scopus 로고
    • Localization and quantitation of the ornithine lipid of Thiobacillus thiooxidans
    • Dees, C., Shively, J.M., Localization and quantitation of the ornithine lipid of Thiobacillus thiooxidans. J. Bacteriol. 149 (1982), 798–799.
    • (1982) J. Bacteriol. , vol.149 , pp. 798-799
    • Dees, C.1    Shively, J.M.2
  • 121
    • 0017096022 scopus 로고
    • A new lysine-containing lipid isolated from Agrobacterium tumefaciens
    • Tahara, Y., Yamada, Y., Kondo, K., A new lysine-containing lipid isolated from Agrobacterium tumefaciens. Agric. Biol. Chem. 40 (1976), 1449–1450, 10.1271/bbb1961.40.1449.
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 1449-1450
    • Tahara, Y.1    Yamada, Y.2    Kondo, K.3
  • 122
    • 0024215713 scopus 로고
    • Isolation and structural characterization of a new non-phospharylated lipoamino acid from Mycobacterium phlei
    • Lerouge, P., Lebas, M.H., Agapakis-Caussé, G., Promé, J.C., Isolation and structural characterization of a new non-phospharylated lipoamino acid from Mycobacterium phlei. Chem. Phys. Lipids 49 (1988), 161–166, 10.1016/0009-3084(88)90003-5.
    • (1988) Chem. Phys. Lipids , vol.49 , pp. 161-166
    • Lerouge, P.1    Lebas, M.H.2    Agapakis-Caussé, G.3    Promé, J.C.4
  • 125
    • 85007623250 scopus 로고    scopus 로고
    • Plasticity of Streptomyces coelicolor membrane composition under different growth conditions and during development
    • Sandoval-Calderón, M., Nguyen, D.D., Kapono, C.A., Herron, P., Dorrestein, P.C., Sohlenkamp, C., Plasticity of Streptomyces coelicolor membrane composition under different growth conditions and during development. Front. Microbiol., 6, 2015, 1465, 10.3389/fmicb.2015.01465.
    • (2015) Front. Microbiol. , vol.6 , pp. 1465
    • Sandoval-Calderón, M.1    Nguyen, D.D.2    Kapono, C.A.3    Herron, P.4    Dorrestein, P.C.5    Sohlenkamp, C.6
  • 126
    • 0016642484 scopus 로고
    • Encystment and germination in Azotobacter vinelandii
    • Sadoff, H.L., Encystment and germination in Azotobacter vinelandii. Bacteriol. Rev. 39 (1975), 516–539.
    • (1975) Bacteriol. Rev. , vol.39 , pp. 516-539
    • Sadoff, H.L.1
  • 127
    • 33646557702 scopus 로고    scopus 로고
    • Phenolic lipid synthesis by type III polyketide synthases is essential for cyst formation in Azotobacter vinelandii
    • Funa, N., Ozawa, H., Hirata, A., Horinouchi, S., Phenolic lipid synthesis by type III polyketide synthases is essential for cyst formation in Azotobacter vinelandii. Proc. Natl. Acad. Sci. U. S. A. 103 (2006), 6356–6361.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 6356-6361
    • Funa, N.1    Ozawa, H.2    Hirata, A.3    Horinouchi, S.4
  • 128
    • 38949095007 scopus 로고    scopus 로고
    • Direct transfer of starter substrates from type I fatty acid synthase to type III polyketide synthases in phenolic lipid synthesis
    • Miyanaga, A., Funa, N., Awakawa, T., Horinouchi, S., Direct transfer of starter substrates from type I fatty acid synthase to type III polyketide synthases in phenolic lipid synthesis. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 871–876.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 871-876
    • Miyanaga, A.1    Funa, N.2    Awakawa, T.3    Horinouchi, S.4
  • 129
    • 27144551296 scopus 로고    scopus 로고
    • Intracellular compartmentation in plactomycetes
    • Fuerst, J.A., Intracellular compartmentation in plactomycetes. Annu. Rev. Microbiol. 59 (2005), 299–328, 10.1146/annurev.micro.59.030804.121258.
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 299-328
    • Fuerst, J.A.1
  • 132
    • 62249157789 scopus 로고    scopus 로고
    • A comparative genomics study of genetic products potentiall encoding ladderane lipid biosynthesis
    • Rattray, J.E., Strous, M., Op den Kamp, H.J.M., Schouten, S., Jetten, M.S.M., Damsté, J.S.S., A comparative genomics study of genetic products potentiall encoding ladderane lipid biosynthesis. Biol. Direct, 4, 2009, 8, 10.1186/1745-6150-4-8.
    • (2009) Biol. Direct , vol.4 , pp. 8
    • Rattray, J.E.1    Strous, M.2    Op den Kamp, H.J.M.3    Schouten, S.4    Jetten, M.S.M.5    Damsté, J.S.S.6
  • 133
    • 84961844710 scopus 로고    scopus 로고
    • Investigation of proposed ladderane biosynthetic genes from anammox bacteria by heterologous expression in E. coli
    • Javipour, P., Deutsch, S., Mutalik, V.K., Hillson, N.J., Petzold, C.J., Keasling, J.D., Beller, H.R., Investigation of proposed ladderane biosynthetic genes from anammox bacteria by heterologous expression in E. coli. PLoS ONE, 11, 2016, e0151087, 10.1371/journal.pone.151087.
    • (2016) PLoS ONE , vol.11
    • Javipour, P.1    Deutsch, S.2    Mutalik, V.K.3    Hillson, N.J.4    Petzold, C.J.5    Keasling, J.D.6    Beller, H.R.7


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