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Volumn 198, Issue 16, 2016, Pages 2192-2203

Functional interaction between the cytoplasmic ABC protein LptB and the inner membrane LptC protein, components of the lipopolysaccharide transport machinery in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; BACTERIUM LIPOPOLYSACCHARIDE; CYTOPLASM PROTEIN; LPTB PROTEIN; LPTC PROTEIN; MEMBRANE PROTEIN; MUTANT PROTEIN; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; LIPOPOLYSACCHARIDE; LPTB PROTEIN, E COLI; LPTC PROTEIN, E COLI;

EID: 84982798409     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00329-16     Document Type: Article
Times cited : (16)

References (44)
  • 2
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67:593-656. http://dx.doi.org/10.1128/MMBR.67.4.593-656.2003.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 3
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccha-ride in the outer membrane of Escherichia coli
    • Wu T, McCandlish AC, Gronenberg LS, Chng SS, Silhavy TJ, Kahne D. 2006. Identification of a protein complex that assembles lipopolysaccha-ride in the outer membrane of Escherichia coli. Proc Natl Acad Sci U S A 103:11754-11759. http://dx.doi.org/10.1073/pnas.0604744103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.S.4    Silhavy, T.J.5    Kahne, D.6
  • 4
    • 33845950113 scopus 로고    scopus 로고
    • Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli
    • Sperandeo P, Cescutti R, Villa R, Di Benedetto C, Candia D, Dehò G, Polissi A. 2007. Characterization of lptA and lptB, two essential genes implicated in lipopolysaccharide transport to the outer membrane of Escherichia coli. J Bacteriol 189:244-253. http://dx.doi.org/10.1128/JB.01126-06.
    • (2007) J Bacteriol , vol.189 , pp. 244-253
    • Sperandeo, P.1    Cescutti, R.2    Villa, R.3    Di Benedetto, C.4    Candia, D.5    Dehò, G.6    Polissi, A.7
  • 5
    • 46049106143 scopus 로고    scopus 로고
    • Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Sperandeo P, Lau FK, Carpentieri A, De Castro C, Molinaro A, Dehò G, Silhavy TJ, Polissi A. 2008. Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli. J Bacteriol 190:4460 - 4469. http://dx.doi.org/10.1128/JB.00270-08.
    • (2008) J Bacteriol , vol.190 , pp. 4460 - 4469
    • Sperandeo, P.1    Lau, F.K.2    Carpentieri, A.3    De Castro, C.4    Molinaro, A.5    Dehò, G.6    Silhavy, T.J.7    Polissi, A.8
  • 6
    • 44449176988 scopus 로고    scopus 로고
    • Identification of two inner membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • Ruiz N, Gronenberg LS, Kahne D, Silhavy TJ. 2008. Identification of two inner membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli. Proc Natl Acad Sci U S A 105: 5537-5542. http://dx.doi.org/10.1073/pnas.0801196105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5537-5542
    • Ruiz, N.1    Gronenberg, L.S.2    Kahne, D.3    Silhavy, T.J.4
  • 7
    • 77953084208 scopus 로고    scopus 로고
    • Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex
    • Chng SS, Gronenberg LS, Kahne D. 2010. Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex. Biochemistry 49:4565-4567. http://dx.doi.org/10.1021/bi100493e.
    • (2010) Biochemistry , vol.49 , pp. 4565-4567
    • Chng, S.S.1    Gronenberg, L.S.2    Kahne, D.3
  • 8
    • 67649367532 scopus 로고    scopus 로고
    • Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides
    • Narita S, Tokuda H. 2009. Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides. FEBS Lett 583:2160-2164. http://dx.doi.org/10.1016/j.febslet.2009.05.051.
    • (2009) FEBS Lett , vol.583 , pp. 2160-2164
    • Narita, S.1    Tokuda, H.2
  • 9
    • 84870243063 scopus 로고    scopus 로고
    • Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli
    • Okuda S, Freinkman E, Kahne D. 2012. Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli. Science 338:1214-1217. http://dx.doi.org/10.1126/science.1228984.
    • (2012) Science , vol.338 , pp. 1214-1217
    • Okuda, S.1    Freinkman, E.2    Kahne, D.3
  • 10
    • 84897544524 scopus 로고    scopus 로고
    • Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport
    • Sherman DJ, Lazarus MB, Murphy L, Liu C, Walker S, Ruiz N, Kahne D. 2014. Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport. Proc Natl Acad Sci USA 111:4982-4987. http://dx.doi.org/10.1073/pnas.1323516111.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 4982-4987
    • Sherman, D.J.1    Lazarus, M.B.2    Murphy, L.3    Liu, C.4    Walker, S.5    Ruiz, N.6    Kahne, D.7
  • 11
    • 79952289193 scopus 로고    scopus 로고
    • The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel
    • Freinkman E, Chng SS, Kahne D. 2011. The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel. Proc Natl Acad Sci U S A 108:2486-2491. http://dx.doi.org/10.1073/pnas.1015617108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2486-2491
    • Freinkman, E.1    Chng, S.S.2    Kahne, D.3
  • 12
    • 84903716134 scopus 로고    scopus 로고
    • Structural basis for lipopolysaccharide insertion in the bacterial outer membrane
    • Qiao S, Luo Q, Zhao Y, Zhang XC, Huang Y. 2014. Structural basis for lipopolysaccharide insertion in the bacterial outer membrane. Nature 511: 108-111. http://dx.doi.org/10.1038/nature13484.
    • (2014) Nature , vol.511 , pp. 108-111
    • Qiao, S.1    Luo, Q.2    Zhao, Y.3    Zhang, X.C.4    Huang, Y.5
  • 13
    • 77950438894 scopus 로고    scopus 로고
    • Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane
    • Chng SS, Ruiz N, Chimalakonda G, Silhavy TJ, Kahne D. 2010. Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane. Proc Natl Acad Sci USA 107:5363-5368. http://dx.doi.org/10.1073/pnas.0912872107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5363-5368
    • Chng, S.S.1    Ruiz, N.2    Chimalakonda, G.3    Silhavy, T.J.4    Kahne, D.5
  • 14
    • 79952300098 scopus 로고    scopus 로고
    • Lipoprotein LptE is required for the assembly of LptD by the beta-barrel assembly machine in the outer membrane of Escherichia coli
    • Chimalakonda G, Ruiz N, Chng SS, Garner RA, Kahne D, Silhavy TJ. 2011. Lipoprotein LptE is required for the assembly of LptD by the beta-barrel assembly machine in the outer membrane of Escherichia coli. Proc Natl Acad Sci U S A 108:2492-2497. http://dx.doi.org/10.1073/pnas.1019089108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2492-2497
    • Chimalakonda, G.1    Ruiz, N.2    Chng, S.S.3    Garner, R.A.4    Kahne, D.5    Silhavy, T.J.6
  • 15
    • 79951599665 scopus 로고    scopus 로고
    • New insights into the Lpt machinery for lipopolysaccharide transport to the cell surface: LptA-LptC interaction and LptA stability as sensors of a properly assembled transenvelope complex
    • Sperandeo P, Villa R, Martorana AM, Samalikova M, Grandori R, Dehò G, Polissi A. 2011. New insights into the Lpt machinery for lipopolysaccharide transport to the cell surface: LptA-LptC interaction and LptA stability as sensors of a properly assembled transenvelope complex. J Bacteriol 193:1042-1053. http://dx.doi.org/10.1128/JB.01037-10.
    • (2011) J Bacteriol , vol.193 , pp. 1042-1053
    • Sperandeo, P.1    Villa, R.2    Martorana, A.M.3    Samalikova, M.4    Grandori, R.5    Dehò, G.6    Polissi, A.7
  • 16
    • 84862548484 scopus 로고    scopus 로고
    • Regulated assembly of the transenvelope protein complex required for lipopolysaccharide export
    • Freinkman E, Okuda S, Ruiz N, Kahne D. 2012. Regulated assembly of the transenvelope protein complex required for lipopolysaccharide export. Biochemistry 51:4800 - 4806. http://dx.doi.org/10.1021/bi300592c.
    • (2012) Biochemistry , vol.51 , pp. 4800 - 4806
    • Freinkman, E.1    Okuda, S.2    Ruiz, N.3    Kahne, D.4
  • 17
    • 77958502198 scopus 로고    scopus 로고
    • Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli
    • Tran AX, Dong C, Whitfield C. 2010. Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli. J Biol Chem 285:33529-33539. http://dx.doi.org/10.1074/jbc.M110.144709.
    • (2010) J Biol Chem , vol.285 , pp. 33529-33539
    • Tran, A.X.1    Dong, C.2    Whitfield, C.3
  • 18
    • 51749125875 scopus 로고    scopus 로고
    • Novel structure of the conserved Gram-negative lipopolysaccharide transport protein A and mutagenesis analysis
    • Suits MD, Sperandeo P, Dehò G, Polissi A, Jia Z. 2008. Novel structure of the conserved Gram-negative lipopolysaccharide transport protein A and mutagenesis analysis. J Mol Biol 380:476 - 488. http://dx.doi.org/10.1016/j.jmb.2008.04.045.
    • (2008) J Mol Biol , vol.380 , pp. 476 - 488
    • Suits, M.D.1    Sperandeo, P.2    Dehò, G.3    Polissi, A.4    Jia, Z.5
  • 21
    • 84907504111 scopus 로고    scopus 로고
    • Structural and functional studies of conserved nucleotide-binding protein LptB in lipopolysaccharide transport
    • Wang Z, Xiang Q, Zhu X, Dong H, He C, Wang H, Zhang Y, Wang W, Dong C. 2014. Structural and functional studies of conserved nucleotide-binding protein LptB in lipopolysaccharide transport. Biochem Biophys Res Commun 452:443-449. http://dx.doi.org/10.1016/j.bbrc.2014.08.094.
    • (2014) Biochem Biophys Res Commun , vol.452 , pp. 443-449
    • Wang, Z.1    Xiang, Q.2    Zhu, X.3    Dong, H.4    He, C.5    Wang, H.6    Zhang, Y.7    Wang, W.8    Dong, C.9
  • 22
    • 84873564764 scopus 로고    scopus 로고
    • The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains
    • Villa R, Martorana AM, Okuda S, Gourlay LJ, Nardini M, Sperandeo P, Dehò G, Bolognesi M, Kahne D, Polissi A. 2013. The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains. J Bacteriol 195:1100 - 1108. http://dx.doi.org/10.1128/JB.02057-12.
    • (2013) J Bacteriol , vol.195 , pp. 1100 - 1108
    • Villa, R.1    Martorana, A.M.2    Okuda, S.3    Gourlay, L.J.4    Nardini, M.5    Sperandeo, P.6    Dehò, G.7    Bolognesi, M.8    Kahne, D.9    Polissi, A.10
  • 23
    • 84884305905 scopus 로고    scopus 로고
    • Protease homolog BepA (YfgC) promotes assembly and degradation of beta-barrel membrane proteins in Escherichia coli
    • Narita S, Masui C, Suzuki T, Dohmae N, Akiyama Y. 2013. Protease homolog BepA (YfgC) promotes assembly and degradation of beta-barrel membrane proteins in Escherichia coli. Proc Natl Acad Sci U S A 110: E3612-E3621. http://dx.doi.org/10.1073/pnas.1312012110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E3612-E3621
    • Narita, S.1    Masui, C.2    Suzuki, T.3    Dohmae, N.4    Akiyama, Y.5
  • 24
    • 4544374421 scopus 로고    scopus 로고
    • Scanning the Escherichia coli chromosome by random transposon mutagenesis and multiple phenotypic screening
    • Serina S, Nozza F, Nicastro G, Faggioni F, Mottl H, Dehò G, Polissi A. 2004. Scanning the Escherichia coli chromosome by random transposon mutagenesis and multiple phenotypic screening. Res Microbiol 155:692-701. http://dx.doi.org/10.1016/j.resmic.2004.05.006.
    • (2004) Res Microbiol , vol.155 , pp. 692-701
    • Serina, S.1    Nozza, F.2    Nicastro, G.3    Faggioni, F.4    Mottl, H.5    Dehò, G.6    Polissi, A.7
  • 26
    • 0027209438 scopus 로고
    • Three-step PCR mutagenesis for linker scanning
    • Li XM, Shapiro LJ. 1993. Three-step PCR mutagenesis for linker scanning. Nucleic Acids Res 21:3745-3748. http://dx.doi.org/10.1093/nar/21.16.3745.
    • (1993) Nucleic Acids Res , vol.21 , pp. 3745-3748
    • Li, X.M.1    Shapiro, L.J.2
  • 27
  • 28
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey TL, Elkan C. 1994. Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc Int Conf Intell Syst Mol Biol 2:28-36.
    • (1994) Proc Int Conf Intell Syst Mol Biol , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 30
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. 1988. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 16:10881-10890. http://dx.doi.org/10.1093/nar/16.22.10881.
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 31
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S, Henikoff JG. 1992. Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci U S A 89:10915-10919. http://dx.doi.org/10.1073/pnas.89.22.10915.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 33
    • 84925156346 scopus 로고    scopus 로고
    • The I-TASSER suite: protein structure and function prediction
    • Yang J, Yan R, Roy A, Xu D, Poisson J, Zhang Y. 2015. The I-TASSER suite: protein structure and function prediction. Nat Methods 12:7-8.
    • (2015) Nat Methods , vol.12 , pp. 7-8
    • Yang, J.1    Yan, R.2    Roy, A.3    Xu, D.4    Poisson, J.5    Zhang, Y.6
  • 34
    • 84918819193 scopus 로고    scopus 로고
    • Prediction and analysis of intrinsically disordered proteins
    • Punta M, Simon I, Dosztanyi Z. 2015. Prediction and analysis of intrinsically disordered proteins. Methods Mol Biol 1261:35-59. http://dx.doi.org/10.1007/978-1-4939-2230-7_3.
    • (2015) Methods Mol Biol , vol.1261 , pp. 35-59
    • Punta, M.1    Simon, I.2    Dosztanyi, Z.3
  • 35
    • 79957852570 scopus 로고    scopus 로고
    • Complex transcriptional organization regulates an Escherichia coli locus implicated in lipopolysaccharide biogenesis
    • Martorana AM, Sperandeo P, Polissi A, Dehò G. 2011. Complex transcriptional organization regulates an Escherichia coli locus implicated in lipopolysaccharide biogenesis. Res Microbiol 162:470 - 482. http://dx.doi.org/10.1016/j.resmic.2011.03.007.
    • (2011) Res Microbiol , vol.162 , pp. 470 - 482
    • Martorana, A.M.1    Sperandeo, P.2    Polissi, A.3    Dehò, G.4
  • 36
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson AL, Dassa E, Orelle C, Chen J. 2008. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol Mol Biol Rev 72:317-364. http://dx.doi.org/10.1128/MMBR.00031-07.
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 37
    • 84961964762 scopus 로고    scopus 로고
    • Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model
    • Okuda S, Sherman DJ, Silhavy TJ, Ruiz N, Kahne D. 2016. Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model. Nat Rev Microbiol 14:337-345. http://dx.doi.org/10.1038/nrmicro.2016.25.
    • (2016) Nat Rev Microbiol , vol.14 , pp. 337-345
    • Okuda, S.1    Sherman, D.J.2    Silhavy, T.J.3    Ruiz, N.4    Kahne, D.5
  • 38
    • 84878854997 scopus 로고    scopus 로고
    • Ralstonia solanacearum RSc0411 (lptC) is a determinant for full virulence and has a strain-specific novel function in the T3SS activity
    • Yang WC, Lin YM, Cheng YS, Cheng CP. 2013. Ralstonia solanacearum RSc0411 (lptC) is a determinant for full virulence and has a strain-specific novel function in the T3SS activity. Microbiology 159:1136-1148. http://dx.doi.org/10.1099/mic.0.064915-0.
    • (2013) Microbiology , vol.159 , pp. 1136-1148
    • Yang, W.C.1    Lin, Y.M.2    Cheng, Y.S.3    Cheng, C.P.4
  • 39
    • 84857467931 scopus 로고    scopus 로고
    • Adaptation and preadaptation of Salmonella enterica to bile
    • Hernández SB, Cota I, Ducret A, Aussel L, Casadesus J. 2012. Adaptation and preadaptation of Salmonella enterica to bile. PLoS Genet 8:e1002459. http://dx.doi.org/10.1371/journal.pgen.1002459.
    • (2012) PLoS Genet , vol.8 , pp. e1002459
    • Hernández, S.B.1    Cota, I.2    Ducret, A.3    Aussel, L.4    Casadesus, J.5
  • 40
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. 1983. Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166:557-580. http://dx.doi.org/10.1016/S0022-2836(83)80284-8.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 41
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant SG, Jessee J, Bloom FR, Hanahan D. 1990. Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc Natl Acad SciUSA 87:4645-4649. http://dx.doi.org/10.1073/pnas.87.12.4645.
    • (1990) Proc Natl Acad SciUSA , vol.87 , pp. 4645-4649
    • Grant, S.G.1    Jessee, J.2    Bloom, F.R.3    Hanahan, D.4
  • 42
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and mu
    • Casadaban MJ. 1976. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and mu. J Mol Biol 104:541-555. http://dx.doi.org/10.1016/0022-2836(76)90119-4.
    • (1976) J Mol Biol , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 43
    • 0001246049 scopus 로고
    • Derivatives and genotypes of some mutant derivatives of Escherichia coli K-12, p 1191-1219
    • Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (ed), ASM Press, Washington, DC
    • Bachmann BJ. 1987. Derivatives and genotypes of some mutant derivatives of Escherichia coli K-12, p 1191-1219. In Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (ed), Escherichia coli and Salmonella Typhimurium cellular and molecular biology, vol 2. ASM Press, Washington, DC.
    • (1987) Escherichia coli and Salmonella Typhimurium cellular and molecular biology , vol.2
    • Bachmann, B.J.1
  • 44
    • 33745974919 scopus 로고    scopus 로고
    • Nonessential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus
    • Sperandeo P, Pozzi C, Dehò G, Polissi A. 2006. Nonessential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus. Res Microbiol 157:547-558. http://dx.doi.org/10.1016/j.resmic.2005.11.014.
    • (2006) Res Microbiol , vol.157 , pp. 547-558
    • Sperandeo, P.1    Pozzi, C.2    Dehò, G.3    Polissi, A.4


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