메뉴 건너뛰기




Volumn 185, Issue 13, 2003, Pages 3773-3779

Membrane interaction of the glycosyltransferase MurG: A special role for cardiolipin

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOLIPIN; DETERGENT; GLYCOSYLTRANSFERASE; LIPID; LIPID I; MEMBRANE PROTEIN; PEPTIDOGLYCAN; PHOSPHATIDYLGLYCEROL; PHOSPHOLIPID; PROTEIN MURG; UNCLASSIFIED DRUG;

EID: 0037701593     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.13.3773-3779.2003     Document Type: Article
Times cited : (70)

References (35)
  • 2
    • 0025249980 scopus 로고
    • Membrane morphogenesis from cloned fragments of bacteriophage PM2 DNA that contain the sp6.6 gene
    • Armour, G. A., and G. J. Brewer. 1990. Membrane morphogenesis from cloned fragments of bacteriophage PM2 DNA that contain the sp6.6 gene. FASEB J. 4:1488-1493.
    • (1990) FASEB J. , vol.4 , pp. 1488-1493
    • Armour, G.A.1    Brewer, G.J.2
  • 3
    • 0036629192 scopus 로고    scopus 로고
    • A multitarget assay for inhibitors of membrane-associated steps of peptidoglycan biosynthesis
    • Barbosa, M. D., H. O. Ross, M. C. Hillman, R. P. Meade, M. G. Kurilla, and D. L. Pompliano. 2002. A multitarget assay for inhibitors of membrane-associated steps of peptidoglycan biosynthesis. Anal. Biochem. 306:17-22.
    • (2002) Anal. Biochem. , vol.306 , pp. 17-22
    • Barbosa, M.D.1    Ross, H.O.2    Hillman, M.C.3    Meade, R.P.4    Kurilla, M.G.5    Pompliano, D.L.6
  • 4
    • 0017332750 scopus 로고
    • Effects of lipid phase transition of the freeze-cleaved envelope of Escherichia coli
    • Bayer, M. E., M. Dolack, and E. Houser. 1977. Effects of lipid phase transition of the freeze-cleaved envelope of Escherichia coli. J. Bacteriol. 129:1563-1573.
    • (1977) J. Bacteriol. , vol.129 , pp. 1563-1573
    • Bayer, M.E.1    Dolack, M.2    Houser, E.3
  • 5
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0031784281 scopus 로고    scopus 로고
    • Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
    • Brotz, H., M. Josten, I. Wiedemann, U. Schnelder, F. Gotz, G. Bierbaum, and H. G. Sahl. 1998. Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics. Mol. Microbiol. 30:317-327.
    • (1998) Mol. Microbiol. , vol.30 , pp. 317-327
    • Brotz, H.1    Josten, M.2    Wiedemann, I.3    Schnelder, U.4    Gotz, F.5    Bierbaum, G.6    Sahl, H.G.7
  • 10
    • 0027405768 scopus 로고
    • The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm
    • Bupp, K., and J. van Heijenoort. 1993. The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. J. Bacteriol. 175:1841-1843.
    • (1993) J. Bacteriol. , vol.175 , pp. 1841-1843
    • Bupp, K.1    Van Heijenoort, J.2
  • 11
    • 0017056888 scopus 로고
    • Lipid-protein interactions in Escherichia coli. Membrane-associated f1 bacteriophage coat protein and phospholipid metabolism
    • Chamberlain, B. K., and R. E. Webster. 1976. Lipid-protein interactions in Escherichia coli. Membrane-associated f1 bacteriophage coat protein and phospholipid metabolism. J. Biol. Chem. 251:7739-7745.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7739-7745
    • Chamberlain, B.K.1    Webster, R.E.2
  • 12
    • 0020028268 scopus 로고
    • Simple procedures for evaluating the cryofixation of biological samples
    • Costello, M. J., R. Fetter, and M. Hochli. 1982. Simple procedures for evaluating the cryofixation of biological samples. J. Microsc. 125:125-136.
    • (1982) J. Microsc. , vol.125 , pp. 125-136
    • Costello, M.J.1    Fetter, R.2    Hochli, M.3
  • 13
    • 0032930890 scopus 로고    scopus 로고
    • UDP-N-acetylglucosamine:N-acetylmuramoyl-(pentapeptide) pyrophosphoryl unde-caprenol N-acetylglucosamine transferase from Escherichia coli: Overproduction, solubilization, and purification
    • Crouvolsier, M., D. Mengin-Lecreulx, and J. van Heijenoort. 1999. UDP-N-acetylglucosamine:N-acetylmuramoyl-(pentapeptide) pyrophosphoryl unde-caprenol N-acetylglucosamine transferase from Escherichia coli: overproduction, solubilization, and purification. FEBS Lett. 449:289-292.
    • (1999) FEBS Lett. , vol.449 , pp. 289-292
    • Crouvolsier, M.1    Mengin-Lecreulx, D.2    Van Heijenoort, J.3
  • 14
    • 0033623762 scopus 로고    scopus 로고
    • The 1.9 Å crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis
    • Ha, S., D. Walker, Y. Shi, and S. Walker. 2000. The 1.9 Å crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis. Protein Sci. 9:1045-1052.
    • (2000) Protein Sci. , vol.9 , pp. 1045-1052
    • Ha, S.1    Walker, D.2    Shi, Y.3    Walker, S.4
  • 15
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Holtje, J. V. 1998. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62:181-203.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 181-203
    • Holtje, J.V.1
  • 16
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potentialq 18
    • Hope, M. J., M. B. Bally, G. Webb, and P. R. Cullis. 1985. Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochim. Biophys. Acta 812:55-65.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 17
    • 0026094952 scopus 로고
    • Effect of thyroxine on the activity of mitochondrial cardiolipin synthase in rat liver
    • Hostetler, K. Y. 1991. Effect of thyroxine on the activity of mitochondrial cardiolipin synthase in rat liver. Biochim. Biophys. Acta 1086:139-140.
    • (1991) Biochim. Biophys. Acta , vol.1086 , pp. 139-140
    • Hostetler, K.Y.1
  • 19
    • 0025833399 scopus 로고
    • The murG gene of Escherichia coli codes for the UDP-N-acetylglucosamine: N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis
    • Mengin-Lecreulx, D., L. Texier, M. Rousseau, and J. van Heijenoort. 1991. The murG gene of Escherichia coli codes for the UDP-N-acetylglucosamine: N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis. J. Bacteriol. 173:4625-4636.
    • (1991) J. Bacteriol. , vol.173 , pp. 4625-4636
    • Mengin-Lecreulx, D.1    Texier, L.2    Rousseau, M.3    Van Heijenoort, J.4
  • 20
    • 0033956407 scopus 로고    scopus 로고
    • Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange
    • Mlieykovskaya, E., and W. Dowhan. 2000. Visualization of phospholipid domains in Escherichia coli by using the cardiolipin-specific fluorescent dye 10-N-nonyl acridine orange. J. Bacteriol. 182:1172-1175.
    • (2000) J. Bacteriol. , vol.182 , pp. 1172-1175
    • Mlieykovskaya, E.1    Dowhan, W.2
  • 21
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor
    • Paetzel, M., R. E. Dalbey, and N. C. Strynadka. 1998. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature 396:186-190.
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 22
    • 0027489678 scopus 로고
    • Decreased cytochrome oxidase activity and changes in phospholipids in heart mitochondria from hypothyroid rats
    • Paradies, G., F. M. Ruggiero, P. Dinoi, G. Petrosillo, and E. Quagliariello. 1993. Decreased cytochrome oxidase activity and changes in phospholipids in heart mitochondria from hypothyroid rats. Arch. Biochem. Biophys. 307:91-95.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 91-95
    • Paradies, G.1    Ruggiero, F.M.2    Dinoi, P.3    Petrosillo, G.4    Quagliariello, E.5
  • 23
    • 0023660851 scopus 로고
    • Interactions of mitochondrial precursor protein apocytochrome c with phosphatidylserine in model membranes. A monolayer study
    • Pilon, M., W. Jordi, B. De Kruijff, and R. A. Demel. 1987. Interactions of mitochondrial precursor protein apocytochrome c with phosphatidylserine in model membranes. A monolayer study. Biochim. Biophys. Acta 902:207-216.
    • (1987) Biochim. Biophys. Acta , vol.902 , pp. 207-216
    • Pilon, M.1    Jordi, W.2    De Kruijff, B.3    Demel, R.A.4
  • 24
    • 0014779155 scopus 로고
    • Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser, G., S. Fkeischer, and A. Yamamoto. 1970. Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids 5:494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fkeischer, S.2    Yamamoto, A.3
  • 25
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame, M., D. Rua, and M. L. Greenberg. 2000. The biosynthesis and functional role of cardiolipin. Prog. Lipid Res. 39:257-288.
    • (2000) Prog. Lipid Res. , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 26
    • 0021992333 scopus 로고
    • Alteration of phospholipid composition by combined defects in phosphatidylserine and cardiolipin synthases and physiological consequences in Escherichia coli
    • Shibuya, I., C. Miyazaki, and A. Ohta. 1985. Alteration of phospholipid composition by combined defects in phosphatidylserine and cardiolipin synthases and physiological consequences in Escherichia coli. J. Bacteriol. 161:1086-1092.
    • (1985) J. Bacteriol. , vol.161 , pp. 1086-1092
    • Shibuya, I.1    Miyazaki, C.2    Ohta, A.3
  • 27
    • 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., R. E. Dalbey, R. A. Demel, J. A. Killian, and B. De Kruijff. 2001. Effect of nonbilayer lipids on membrane binding and insertion of the catalytic domain of leader peptidase. Biochemistry 40:9677-9684.
    • (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
  • 29
    • 0020074516 scopus 로고
    • Polymorphic phase behaviour of cardiolipin from bovine heart and from Bacillus subtilis as detected by 31P-NMR and freeze-fracture techniques. Effects of Ca2+, Mg2+, Ba2+ and temperature
    • Vasilenko, I., B. De Kruijff, and A. J. Verkleij. 1982. Polymorphic phase behaviour of cardiolipin from bovine heart and from Bacillus subtilis as detected by 31P-NMR and freeze-fracture techniques. Effects of Ca2+, Mg2+, Ba2+ and temperature. Biochim. Biophys. Acta 684:282-286.
    • (1982) Biochim. Biophys. Acta , vol.684 , pp. 282-286
    • Vasilenko, I.1    De Kruijff, B.2    Verkleij, A.J.3
  • 31
  • 32
    • 0021473099 scopus 로고
    • Physiological and morphological effects of overproduction of membrane-bound ATP synthase in Escherichia coli K-12
    • von Meyenburg, K., B. B. Jorgensen, and B. van Deurs. 1984. Physiological and morphological effects of overproduction of membrane-bound ATP synthase in Escherichia coli K-12. EMBO J. 3:1791-1797.
    • (1984) EMBO J. , vol.3 , pp. 1791-1797
    • Von Meyenburg, K.1    Jorgensen, B.B.2    Van Deurs, B.3
  • 33
    • 0023975771 scopus 로고
    • Accumulation of LamB-LacZ hybrid proteins in intracytoplasmic membrane-like structures in Escherichia coli K12
    • Voorbout, W., T. De Kroon, J. Leunissen-Bijvelt, A. Verkleij, and J. Tommassen. 1988. Accumulation of LamB-LacZ hybrid proteins in intracytoplasmic membrane-like structures in Escherichia coli K12. J. Gen. Microbiol. 134:599-604.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 599-604
    • Voorbout, W.1    De Kroon, T.2    Leunissen-Bijvelt, J.3    Verkleij, A.4    Tommassen, J.5
  • 34
    • 0021324648 scopus 로고
    • Overproduction of fumarate reductase in Escherichia coli induces a novel intracellular lipid-protein organelle
    • Weiner, J. H., B. D. Lemire, M. L. Elmes, R. D. Bradley, and D. G. Scraba. 1984. Overproduction of fumarate reductase in Escherichia coli induces a novel intracellular lipid-protein organelle. J. Bacteriol. 158:590-596.
    • (1984) J. Bacteriol. , vol.158 , pp. 590-596
    • Weiner, J.H.1    Lemire, B.D.2    Elmes, M.L.3    Bradley, R.D.4    Scraba, D.G.5
  • 35
    • 0023001152 scopus 로고
    • Crystalline arrays of the Escherichia coli sn-glycerol-3-phosphate acyltransferase, an integral membrane protein
    • Wilkison, W. O., J. P. Walsb, J. M. Corless, and R. M. Bell. 1986. Crystalline arrays of the Escherichia coli sn-glycerol-3-phosphate acyltransferase, an integral membrane protein. J. Biol. Chem. 261:9951-9958.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9951-9958
    • Wilkison, W.O.1    Walsb, J.P.2    Corless, J.M.3    Bell, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.