메뉴 건너뛰기




Volumn 194, Issue 9, 2012, Pages 2142-2151

Phosphatidylglycerol:: Prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; ENZYME VARIANT; ESCHERICHIA COLI PROTEIN; LIPOPROTEIN; MEMBRANE ENZYME; PHOSPHATIDYLGLYCEROL; PHOSPHATIDYLGLYCEROL::PROLIPOPROTEIN DIACYLGLYCERYL TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84861220038     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06641-11     Document Type: Article
Times cited : (40)

References (65)
  • 1
    • 33846275257 scopus 로고    scopus 로고
    • Structural basis for intramembrane proteolysis by rhomboid serine proteases
    • Ben-Shem A, Fass D, Bibi E. 2007. Structural basis for intramembrane proteolysis by rhomboid serine proteases. Proc. Natl. Acad. Sci. U. S. A. 104:462-466.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 462-466
    • Ben-Shem, A.1    Fass, D.2    Bibi, E.3
  • 2
    • 33847218318 scopus 로고    scopus 로고
    • Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis
    • Bhatt K, Gurcha SS, Bhatt A, Besra GS, Jacobs WR, Jr. 2007. Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis. Microbiology 153:513-520.
    • (2007) Microbiology , vol.153 , pp. 513-520
    • Bhatt, K.1    Gurcha, S.S.2    Bhatt, A.3    Besra, G.S.4    Jacobs Jr., W.R.5
  • 3
    • 0029056415 scopus 로고
    • Protein secretion by hybrid bacterial ABC-transporters: specific functions of the membrane ATPase and the membrane fusion protein
    • Binet R, Wandersman C. 1995. Protein secretion by hybrid bacterial ABC-transporters: specific functions of the membrane ATPase and the membrane fusion protein. EMBO J. 14:2298-2306.
    • (1995) EMBO J , vol.14 , pp. 2298-2306
    • Binet, R.1    Wandersman, C.2
  • 4
    • 19444377006 scopus 로고    scopus 로고
    • Transmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM(TM)): application to lipid-specific membrane protein topogenesis
    • Bogdanov M, Zhang W, Xie J, Dowhan W. 2005. Transmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM(TM)): application to lipid-specific membrane protein topogenesis. Methods 36:148-171.
    • (2005) Methods , vol.36 , pp. 148-171
    • Bogdanov, M.1    Zhang, W.2    Xie, J.3    Dowhan, W.4
  • 5
    • 33748783783 scopus 로고    scopus 로고
    • Host defenses against Staphylococcus aureus infection require recognition of bacterial lipoproteins
    • Bubeck Wardenburg J, Williams WA, Missiakas D. 2006. Host defenses against Staphylococcus aureus infection require recognition of bacterial lipoproteins. Proc. Natl. Acad. Sci. U. S. A. 103:13831-13836.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 13831-13836
    • Bubeck Wardenburg, J.1    Williams, W.A.2    Missiakas, D.3
  • 6
    • 75349096668 scopus 로고    scopus 로고
    • The essential Escherichia coli apolipoprotein N-acyltransferase (Lnt) exists as an extracytoplasmic thioester acyl-enzyme intermediate
    • Buddelmeijer N, Young R. 2010. The essential Escherichia coli apolipoprotein N-acyltransferase (Lnt) exists as an extracytoplasmic thioester acyl-enzyme intermediate. Biochemistry 49:341-346.
    • (2010) Biochemistry , vol.49 , pp. 341-346
    • Buddelmeijer, N.1    Young, R.2
  • 7
    • 0036180995 scopus 로고    scopus 로고
    • Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity
    • Cascales E, Bernadac A, Gavioli M, Lazzaroni JC, Lloubes R. 2002. Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity. J. Bacteriol. 184:754-759.
    • (2002) J. Bacteriol. , vol.184 , pp. 754-759
    • Cascales, E.1    Bernadac, A.2    Gavioli, M.3    Lazzaroni, J.C.4    Lloubes, R.5
  • 8
    • 0022999829 scopus 로고
    • Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli
    • Choi D-S, Yamada H, Mizuno T, Mizushima S. 1986. Trimeric structure and localization of the major lipoprotein in the cell surface of Escherichia coli. J. Biol. Chem. 261:8953-8957.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8953-8957
    • Choi, D.-S.1    Yamada, H.2    Mizuno, T.3    Mizushima, S.4
  • 9
    • 0028568176 scopus 로고
    • TopPred II: an improved software for membrane protein structure predictions
    • Claros MG, von Heijne G. 1994. TopPred II: an improved software for membrane protein structure predictions. Comput. Appl. Biosci. 10:685-686.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    von Heijne, G.2
  • 10
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley DO, et al. 2005. Global topology analysis of the Escherichia coli inner membrane proteome. Science 308:1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1
  • 11
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 12
    • 0036146905 scopus 로고    scopus 로고
    • Fast lysis of Escherichia coli filament cells requires differentiation of potential division sites
    • de Pedro MA, Höltje JV, Schwarz H. 2002. Fast lysis of Escherichia coli filament cells requires differentiation of potential division sites. Microbiology 148:79-86.
    • (2002) Microbiology , vol.148 , pp. 79-86
    • de Pedro, M.A.1    Höltje, J.V.2    Schwarz, H.3
  • 14
    • 66249133368 scopus 로고    scopus 로고
    • How intramembrane proteases bury hydrolytic reactions in the membrane
    • Erez E, Fass D, Bibi E. 2009. How intramembrane proteases bury hydrolytic reactions in the membrane. Nature 459:371-378.
    • (2009) Nature , vol.459 , pp. 371-378
    • Erez, E.1    Fass, D.2    Bibi, E.3
  • 15
    • 0027296627 scopus 로고
    • Isolation and characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in prolipoprotein modification
    • Gan K, Gupta SD, Sankaran K, Schmid MB, Wu HC. 1993. Isolation and characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in prolipoprotein modification. J. Biol. Chem. 268: 16544-16550.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16544-16550
    • Gan, K.1    Gupta, S.D.2    Sankaran, K.3    Schmid, M.B.4    Wu, H.C.5
  • 16
    • 0028932215 scopus 로고
    • The umpA gene of Escherichia coli encodes phosphatidylglycerol: prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling
    • Gan K, et al. 1995. The umpA gene of Escherichia coli encodes phosphatidylglycerol: prolipoprotein diacylglyceryl transferase (lgt) and regulates thymidylate synthase levels through translational coupling. J. Bacteriol. 177:1879-1882.
    • (1995) J. Bacteriol. , vol.177 , pp. 1879-1882
    • Gan, K.1
  • 17
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 18
    • 33845499019 scopus 로고    scopus 로고
    • Mutation of the maturase lipoprotein attenuates the virulence of Streptococcus equi to a greater extent than does loss of general lipoprotein lipidation
    • Hamilton A, et al. 2006. Mutation of the maturase lipoprotein attenuates the virulence of Streptococcus equi to a greater extent than does loss of general lipoprotein lipidation. Infect. Immun. 74:6907-6919.
    • (2006) Infect. Immun. , vol.74 , pp. 6907-6919
    • Hamilton, A.1
  • 19
    • 0031941001 scopus 로고    scopus 로고
    • A conserved histidine is essential for glycerolipid acyltransferase catalysis
    • Heath RJ, Rock CO. 1998. A conserved histidine is essential for glycerolipid acyltransferase catalysis. J. Bacteriol. 180:1425-1430.
    • (1998) J. Bacteriol. , vol.180 , pp. 1425-1430
    • Heath, R.J.1    Rock, C.O.2
  • 20
    • 44449155448 scopus 로고    scopus 로고
    • Lipoproteins are critical TLR2 activating toxins in group B streptococcal sepsis
    • Henneke P, et al. 2008. Lipoproteins are critical TLR2 activating toxins in group B streptococcal sepsis. J. Immunol. 180:6149-6158.
    • (2008) J. Immunol. , vol.180 , pp. 6149-6158
    • Henneke, P.1
  • 21
    • 80051503015 scopus 로고    scopus 로고
    • Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase
    • Hillmann F, Argentini M, Buddelmeijer N. 2011. Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase. J. Biol. Chem. 286: 27936-27946.
    • (2011) J. Biol. Chem. , vol.286 , pp. 27936-27946
    • Hillmann, F.1    Argentini, M.2    Buddelmeijer, N.3
  • 22
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: classification and secondary structure prediction system for membrane proteins
    • Hirokawa T, Boon-Chieng S, Mitaku S. 1998. SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics 14:378-379.
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 23
    • 0020449598 scopus 로고
    • Signal peptide digestion in Escherichia coli Effect of protease inhibitors on hydrolysis of the cleaved signal peptide of the major outer-membrane lipoprotein
    • Hussain M, Ozawa Y, Ichihara S, Mizushima S. 1982. Signal peptide digestion in Escherichia coli. Effect of protease inhibitors on hydrolysis of the cleaved signal peptide of the major outer-membrane lipoprotein. Eur. J. Biochem. 129:233-239.
    • (1982) Eur. J. Biochem. , vol.129 , pp. 233-239
    • Hussain, M.1    Ozawa, Y.2    Ichihara, S.3    Mizushima, S.4
  • 24
    • 77953985332 scopus 로고    scopus 로고
    • Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis
    • Hyyryläinen HL, et al. 2010. Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis. Mol. Microbiol. 77:108-127.
    • (2010) Mol. Microbiol. , vol.77 , pp. 108-127
    • Hyyryläinen, H.L.1
  • 25
    • 0021135713 scopus 로고
    • Protease IV, a cytoplasmic membrane protein of Escherichia coli, has signal peptide peptidase activity
    • Ichihara S, Beppu N, Mizushima S. 1984. Protease IV, a cytoplasmic membrane protein of Escherichia coli, has signal peptide peptidase activity. J. Biol. Chem. 259:9853-9857.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9853-9857
    • Ichihara, S.1    Beppu, N.2    Mizushima, S.3
  • 26
    • 34047151404 scopus 로고    scopus 로고
    • Improving the accuracy of transmembrane protein topology prediction using evolutionary information
    • Jones DT. 2007. Improving the accuracy of transmembrane protein topology prediction using evolutionary information. Bioinformatics 23: 538-544.
    • (2007) Bioinformatics , vol.23 , pp. 538-544
    • Jones, D.T.1
  • 27
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Kall L, Krogh A, Sonnhammer EL. 2004. A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol. 338:1027-1036.
    • (2004) J. Mol. Biol. , vol.338 , pp. 1027-1036
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 28
    • 0031668304 scopus 로고    scopus 로고
    • Lyme disease-causing Borrelia species encode multiple lipoproteins homologous to peptide-binding proteins of ABC-type transporters
    • Kornacki JA, Oliver DB. 1998. Lyme disease-causing Borrelia species encode multiple lipoproteins homologous to peptide-binding proteins of ABC-type transporters. Infect. Immun. 66:4115-4122.
    • (1998) Infect. Immun. , vol.66 , pp. 4115-4122
    • Kornacki, J.A.1    Oliver, D.B.2
  • 30
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer E. 2001. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.4
  • 32
    • 67649763474 scopus 로고    scopus 로고
    • The triacylated ATP binding cluster transporter substrate-binding lipoprotein of Staphylococcus aureus functions as a native ligand for Toll-like receptor 2
    • Kurokawa K, Lee H, Roh et al. 2009. The triacylated ATP binding cluster transporter substrate-binding lipoprotein of Staphylococcus aureus functions as a native ligand for Toll-like receptor 2. J. Biol. Chem. 284:8406-8411.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8406-8411
    • Kurokawa, K.1    Lee, H.2    Roh, K.B.3
  • 33
    • 0033522379 scopus 로고    scopus 로고
    • Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate acyltransferase reaction
    • Lewin TM, Wang P, Coleman RA. 1999. Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate acyltransferase reaction. Biochemistry 38:5764-5771.
    • (1999) Biochemistry , vol.38 , pp. 5764-5771
    • Lewin, T.M.1    Wang, P.2    Coleman, R.A.3
  • 34
    • 34249740681 scopus 로고    scopus 로고
    • Topology and active site of PlsY: the bacterial acylphosphate:glycerol-3-phosphate acyltransferase
    • Lu YJ, Zhang F, Grimes KD, Lee RE, Rock CO. 2007. Topology and active site of PlsY: the bacterial acylphosphate:glycerol-3-phosphate acyltransferase. J. Biol. Chem. 282:11339-11346.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11339-11346
    • Lu, Y.J.1    Zhang, F.2    Grimes, K.D.3    Lee, R.E.4    Rock, C.O.5
  • 35
    • 49649123115 scopus 로고    scopus 로고
    • Lipoproteins of Listeria monocytogenes are critical for virulence and TLR2-mediated immune activation
    • Machata S, et al. 2008. Lipoproteins of Listeria monocytogenes are critical for virulence and TLR2-mediated immune activation. J. Immunol. 181: 2028-2035.
    • (2008) J. Immunol. , vol.181 , pp. 2028-2035
    • Machata, S.1
  • 36
    • 37049184497 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil C, Beckwith J. 1986. A genetic approach to analyzing membrane protein topology. Science 233:1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 37
    • 0026063242 scopus 로고
    • Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II)
    • Munoa FJ, Miller KW, Beers R, Graham M, Wu HC. 1991. Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II). J. Biol. Chem. 266:17667-17672.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17667-17672
    • Munoa, F.J.1    Miller, K.W.2    Beers, R.3    Graham, M.4    Wu, H.C.5
  • 38
    • 0034672544 scopus 로고    scopus 로고
    • Consensus predictions of membrane protein topology
    • Nilsson J, Persson B, von Heijne G. 2000. Consensus predictions of membrane protein topology. FEBS Lett. 486:267-269.
    • (2000) FEBS Lett. , vol.486 , pp. 267-269
    • Nilsson, J.1    Persson, B.2    von Heijne, G.3
  • 39
    • 84155164753 scopus 로고    scopus 로고
    • Lipoprotein biosynthesis by prolipoprotein diacylglyceryl transferase is required for efficient spore germination and full virulence of Bacillus anthracis
    • Okugawa S, et al. 2012. Lipoprotein biosynthesis by prolipoprotein diacylglyceryl transferase is required for efficient spore germination and full virulence of Bacillus anthracis. Mol. Microbiol. 83:96-109.
    • (2012) Mol. Microbiol. , vol.83 , pp. 96-109
    • Okugawa, S.1
  • 40
    • 17444392068 scopus 로고    scopus 로고
    • Characterization of six lipoproteins in the sigmaE regulon
    • Onufryk C, Crouch ML, Fang FC, Gross CA. 2005. Characterization of six lipoproteins in the sigmaE regulon. J. Bacteriol. 187:4552-4561.
    • (2005) J. Bacteriol. , vol.187 , pp. 4552-4561
    • Onufryk, C.1    Crouch, M.L.2    Fang, F.C.3    Gross, C.A.4
  • 41
    • 78650497005 scopus 로고    scopus 로고
    • Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases
    • Paradis-Bleau C, et al. 2010. Lipoprotein cofactors located in the outer membrane activate bacterial cell wall polymerases. Cell 143:1110-1120.
    • (2010) Cell , vol.143 , pp. 1110-1120
    • Paradis-Bleau, C.1
  • 42
    • 0023406272 scopus 로고
    • An unmodified form of the ColE2 lysis protein, an envelope lipoprotein, retains reduced ability to promote colicin E2 release and lysis of producing cells
    • Pugsley AP, Cole ST. 1987. An unmodified form of the ColE2 lysis protein, an envelope lipoprotein, retains reduced ability to promote colicin E2 release and lysis of producing cells. J. Gen. Microbiol. 133:2411-2420.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 2411-2420
    • Pugsley, A.P.1    Cole, S.T.2
  • 43
    • 0028817888 scopus 로고
    • Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions
    • Qi HY, Sankaran K, Gan K, Wu HC. 1995. Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions. J. Bacteriol. 177:6820-6824.
    • (1995) J. Bacteriol. , vol.177 , pp. 6820-6824
    • Qi, H.Y.1    Sankaran, K.2    Gan, K.3    Wu, H.C.4
  • 44
    • 12544257510 scopus 로고    scopus 로고
    • Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli
    • Robichon C, Vidal-Ingigliardi D, Pugsley AP. 2005. Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. J. Biol. Chem. 280:974-983.
    • (2005) J. Biol. Chem. , vol.280 , pp. 974-983
    • Robichon, C.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 45
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 46
    • 0031002075 scopus 로고    scopus 로고
    • Roles of histidine-103 and tyrosine-235 in the function of the prelipoprotein diacylglyceryl transferase of Escherichia coli
    • Sankaran K, et al. 1997. Roles of histidine-103 and tyrosine-235 in the function of the prelipoprotein diacylglyceryl transferase of Escherichia coli. J. Bacteriol. 179:2944-2948.
    • (1997) J. Bacteriol. , vol.179 , pp. 2944-2948
    • Sankaran, K.1
  • 47
    • 0029000609 scopus 로고
    • Modification of bacterial lipoproteins
    • Sankaran K, Gupta SD, Wu HC. 1995. Modification of bacterial lipoproteins. Methods Enzymol. 250:683-697.
    • (1995) Methods Enzymol , vol.250 , pp. 683-697
    • Sankaran, K.1    Gupta, S.D.2    Wu, H.C.3
  • 48
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran K, Wu HC. 1994. Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 269:19701-19706.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 49
    • 55349122529 scopus 로고    scopus 로고
    • Localization and characterization of prolipoprotein diacylglyceryl transferase (Lgt) critical in bacterial lipoprotein biosynthesis
    • Selvan AT, Sankaran K. 2008. Localization and characterization of prolipoprotein diacylglyceryl transferase (Lgt) critical in bacterial lipoprotein biosynthesis. Biochimie 90:1647-1655.
    • (2008) Biochimie , vol.90 , pp. 1647-1655
    • Selvan, A.T.1    Sankaran, K.2
  • 50
    • 79959565162 scopus 로고    scopus 로고
    • The acylation state of surface lipoproteins of mollicute Acholeplasma laidlawii
    • Serebryakova MV, et al. 2011. The acylation state of surface lipoproteins of mollicute Acholeplasma laidlawii. J. Biol. Chem. 286:22769-22776.
    • (2011) J. Biol. Chem. , vol.286 , pp. 22769-22776
    • Serebryakova, M.V.1
  • 51
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner NC, et al. 2004. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22:1567-1572.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1567-1572
    • Shaner, N.C.1
  • 52
    • 0026623526 scopus 로고
    • Export of the outer membrane lipoprotein is defective in secD, secE, and secF mutants of Escherichia coli
    • Sugai M, Wu HC. 1992. Export of the outer membrane lipoprotein is defective in secD, secE, and secF mutants of Escherichia coli. J. Bacteriol. 174:2511-2516.
    • (1992) J. Bacteriol. , vol.174 , pp. 2511-2516
    • Sugai, M.1    Wu, H.C.2
  • 53
    • 77955372826 scopus 로고    scopus 로고
    • Investigating lipoprotein biogenesis and function in the model Gram-positive bacterium Streptomyces coelicolor
    • Thompson BJ, et al. 2010. Investigating lipoprotein biogenesis and function in the model Gram-positive bacterium Streptomyces coelicolor. Mol. Microbiol. 77:943-957.
    • (2010) Mol. Microbiol. , vol.77 , pp. 943-957
    • Thompson, B.J.1
  • 54
    • 0021322854 scopus 로고
    • Prolipoprotein modification and processing enzymes in Escherichia coli
    • Tokunaga M, Loranger JM, Wu HC. 1984. Prolipoprotein modification and processing enzymes in Escherichia coli. J. Biol. Chem. 259:3825-3830.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3825-3830
    • Tokunaga, M.1    Loranger, J.M.2    Wu, H.C.3
  • 55
    • 0027478779 scopus 로고
    • The topological analysis of integral cytoplasmic membrane proteins
    • Traxler B, Boyd D, Beckwith J. 1993. The topological analysis of integral cytoplasmic membrane proteins. J. Membr. Biol. 132:1-11.
    • (1993) J. Membr. Biol. , vol.132 , pp. 1-11
    • Traxler, B.1    Boyd, D.2    Beckwith, J.3
  • 56
    • 70350437568 scopus 로고    scopus 로고
    • Identification of apolipoprotein N-acyltransferase (Lnt) in Mycobacteria
    • Tschumi A, et al. 2009. Identification of apolipoprotein N-acyltransferase (Lnt) in Mycobacteria. J. Biol. Chem. 284:27146-27156.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27146-27156
    • Tschumi, A.1
  • 57
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady GE, Simon I. 2001. The HMMTOP transmembrane topology prediction server. Bioinformatics 17:849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 58
    • 78650431707 scopus 로고    scopus 로고
    • Regulation of peptidoglycan synthesis by outermembrane proteins
    • Typas A, et al. 2010. Regulation of peptidoglycan synthesis by outermembrane proteins. Cell 143:1097-1109.
    • (2010) Cell , vol.143 , pp. 1097-1109
    • Typas, A.1
  • 59
    • 74349127184 scopus 로고    scopus 로고
    • Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis
    • Urban S. 2010. Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis. Biochem. J. 425:501-512.
    • (2010) Biochem. J. , vol.425 , pp. 501-512
    • Urban, S.1
  • 60
    • 34250303119 scopus 로고    scopus 로고
    • Identification of essential residues in apolipoprotein N-acyltransferase, a member of the CN hydrolase family
    • Vidal-Ingigliardi D, Lewenza S, Buddelmeijer N. 2007. Identification of essential residues in apolipoprotein N-acyltransferase, a member of the CN hydrolase family. J. Bacteriol. 189:4456-4464.
    • (2007) J. Bacteriol. , vol.189 , pp. 4456-4464
    • Vidal-Ingigliardi, D.1    Lewenza, S.2    Buddelmeijer, N.3
  • 61
    • 48249151108 scopus 로고    scopus 로고
    • OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar
    • Viklund H, Elofsson A. 2008. OCTOPUS: improving topology prediction by two-track ANN-based preference scores and an extended topological grammar. Bioinformatics 24:1662-1668.
    • (2008) Bioinformatics , vol.24 , pp. 1662-1668
    • Viklund, H.1    Elofsson, A.2
  • 62
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Wang Y, Zhang Y, Ha Y. 2006. Crystal structure of a rhomboid family intramembrane protease. Nature 444:179-180.
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 63
    • 79957509555 scopus 로고    scopus 로고
    • Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies
    • Widdick DA, et al. 2011. Dissecting the complete lipoprotein biogenesis pathway in Streptomyces scabies. Mol. Microbiol. 80:1395-1412.
    • (2011) Mol. Microbiol. , vol.80 , pp. 1395-1412
    • Widdick, D.A.1
  • 64
    • 0024573089 scopus 로고
    • Identification and genetic mapping of the structural gene for an essential Escherichia coli membrane protein
    • Williams MG, Fortson M, Dykstra CC, Jensen P, Kushner SR. 1989. Identification and genetic mapping of the structural gene for an essential Escherichia coli membrane protein. J. Bacteriol. 171:565-568.
    • (1989) J. Bacteriol. , vol.171 , pp. 565-568
    • Williams, M.G.1    Fortson, M.2    Dykstra, C.C.3    Jensen, P.4    Kushner, S.R.5
  • 65
    • 33845365770 scopus 로고    scopus 로고
    • Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry
    • Wu Z, et al. 2006. Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry. Nat. Struct. Mol. Biol. 13:1084-1091.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1084-1091
    • Wu, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.