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Volumn 196, Issue 23, 2014, Pages 4111-4119

Charge requirements of lipid II flippase activity in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; LIPID BINDING PROTEIN; LIPID II FLIPPASE; MEMBRANE ENZYME; MEMBRANE PROTEIN; MURJ PROTEIN; UNCLASSIFIED DRUG; YTGP PROTEIN; ESCHERICHIA COLI PROTEIN; MURAMYL-NAC-(PENTAPEPTIDE)PYROPHOSPHORYL-UNDECAPRENOL; MURJ PROTEIN, E COLI; PHOSPHOLIPID TRANSFER PROTEIN; URIDINE DIPHOSPHATE N ACETYLMURAMIC ACID;

EID: 84910011192     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.02172-14     Document Type: Article
Times cited : (23)

References (41)
  • 1
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas A, Banzhaf M, Gross CA, Vollmer W. 2012. From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat. Rev. Microbiol. 10:123-136. http://dx.doi.org/10.1038/nrmicro2677.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 2
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • Vollmer W, Bertsche U. 2008. Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim. Biophys. Acta 1778: 1714-1734. http://dx.doi.org/10.1016/j.bbamem.2007.06.007.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1714-1734
    • Vollmer, W.1    Bertsche, U.2
  • 5
    • 39149123173 scopus 로고    scopus 로고
    • The biosynthesis of peptidoglycan lipid-linked intermediates
    • Bouhss A, Trunkfield AE, Bugg TDH, Mengin-Lecreulx D. 2008. The biosynthesis of peptidoglycan lipid-linked intermediates. FEMS Microbiol. Rev. 32:208-233. http://dx.doi.org/10.1111/j.1574-6976.2007.00089.x.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 208-233
    • Bouhss, A.1    Trunkfield, A.E.2    Bugg, T.D.H.3    Mengin-Lecreulx, D.4
  • 7
    • 84861892432 scopus 로고    scopus 로고
    • Structural perspective of peptidoglycan biosynthesis and assembly
    • Lovering AL, Safadi SS, Strynadka NCJ. 2012. Structural perspective of peptidoglycan biosynthesis and assembly. Annu. Rev. Biochem. 81:451-478. http://dx.doi.org/10.1146/annurev-biochem-061809-112742.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 451-478
    • Lovering, A.L.1    Safadi, S.S.2    Strynadka, N.C.J.3
  • 8
    • 73449119238 scopus 로고    scopus 로고
    • Flipping lipids: why an' what's the reason for? ACS Chem
    • Sanyal S, Menon AK. 2009. Flipping lipids: why an' what's the reason for? ACS Chem. Biol. 4:895-909. http://dx.doi.org/10.1021/cb900163d.
    • (2009) Biol. , vol.4 , pp. 895-909
    • Sanyal, S.1    Menon, A.K.2
  • 9
    • 84904097466 scopus 로고    scopus 로고
    • MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis
    • Sham L-T, Butler EK, Lebar MD, Kahne D, Bernhardt TG, Ruiz N. 2014. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis. Science 345:220-222. http://dx.doi.org/10.1126/science.1254522.
    • (2014) Science , vol.345 , pp. 220-222
    • Sham, L.-T.1    Butler, E.K.2    Lebar, M.D.3    Kahne, D.4    Bernhardt, T.G.5    Ruiz, N.6
  • 10
    • 55749104427 scopus 로고    scopus 로고
    • Involvement of an essential gene, mviN, in murein synthesis in Escherichia coli
    • Inoue A, Murata Y, Takahashi H, Tsuji N, Fujisaki S, Kato J-I. 2008. Involvement of an essential gene, mviN, in murein synthesis in Escherichia coli. J. Bacteriol. 190:7298-7301. http://dx.doi.org/10.1128/JB.00551-08.
    • (2008) J. Bacteriol. , vol.190 , pp. 7298-7301
    • Inoue, A.1    Murata, Y.2    Takahashi, H.3    Tsuji, N.4    Fujisaki, S.5    Kato, J.-I.6
  • 11
    • 55749095406 scopus 로고    scopus 로고
    • Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli
    • Ruiz N. 2008. Bioinformatics identification of MurJ (MviN) as the peptidoglycan lipid II flippase in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 105:15553-15557. http://dx.doi.org/10.1073/pnas.0808352105.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 15553-15557
    • Ruiz, N.1
  • 12
    • 84899816263 scopus 로고    scopus 로고
    • A Burkholderia cenocepacia MurJ (MviN) homolog is essential for cell wall peptidoglycan synthesis and bacterial viability
    • Mohamed YF, Valvano MA. 2014. A Burkholderia cenocepacia MurJ (MviN) homolog is essential for cell wall peptidoglycan synthesis and bacterial viability. Glycobiology 24:564-576. http://dx.doi.org/10.1093/glycob/cwu025.
    • (2014) Glycobiology , vol.24 , pp. 564-576
    • Mohamed, Y.F.1    Valvano, M.A.2
  • 13
    • 0037337313 scopus 로고    scopus 로고
    • The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) exporter superfamily
    • Hvorup RN, Winnen B, Chang AB, Jiang Y, Zhou X-F, Saier MH. 2003. The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) exporter superfamily. Eur. J. Biochem. 270:799-813. http://dx.doi.org/10.1046/j.1432-1033.2003.03418.x.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 799-813
    • Hvorup, R.N.1    Winnen, B.2    Chang, A.B.3    Jiang, Y.4    Zhou, X.-F.5    Saier, M.H.6
  • 14
    • 84885459056 scopus 로고    scopus 로고
    • Structurefunction analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli
    • Butler EK, Davis RM, Bari V, Nicholson PA, Ruiz N. 2013. Structurefunction analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli. J. Bacteriol. 195:4639-4649. http://dx.doi.org/10.1128/JB.00731-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 4639-4649
    • Butler, E.K.1    Davis, R.M.2    Bari, V.3    Nicholson, P.A.4    Ruiz, N.5
  • 15
    • 64649085938 scopus 로고    scopus 로고
    • Multidrug efflux transporters in the MATE family
    • Kuroda T, Tsuchiya T. 2009. Multidrug efflux transporters in the MATE family. Biochim. Biophys. Acta 1794:763-768. http://dx.doi.org/10.1016/j.bbapap.2008.11.012.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 763-768
    • Kuroda, T.1    Tsuchiya, T.2
  • 16
    • 77958596325 scopus 로고    scopus 로고
    • Structure of a cation-bound multidrug and toxic compound extrusion transporter
    • He X, Szewczyk P, Karyakin A, Evin M, Hong W-X, Zhang Q, Chang G. 2010. Structure of a cation-bound multidrug and toxic compound extrusion transporter. Nature 467:991-994. http://dx.doi.org/10.1038/nature09408.
    • (2010) Nature , vol.467 , pp. 991-994
    • He, X.1    Szewczyk, P.2    Karyakin, A.3    Evin, M.4    Hong, W.-X.5    Zhang, Q.6    Chang, G.7
  • 17
    • 84887491471 scopus 로고    scopus 로고
    • Structural insights into H+-coupled multidrug extrusion by a MATE transporter
    • Lu M, Radchenko M, Symersky J, Nie R, Guo Y. 2013. Structural insights into H+-coupled multidrug extrusion by a MATE transporter. Nat. Struct. Mol. Biol. 20:1310-1317. http://dx.doi.org/10.1038/nsmb.2687.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1310-1317
    • Lu, M.1    Radchenko, M.2    Symersky, J.3    Nie, R.4    Guo, Y.5
  • 20
    • 84875910878 scopus 로고    scopus 로고
    • Wzx flippase-mediated membrane translocation of sugar polymer precursors in bacteria
    • Islam ST, Lam JS. 2013. Wzx flippase-mediated membrane translocation of sugar polymer precursors in bacteria. Environ. Microbiol. 15:1001-1015. http://dx.doi.org/10.1111/j.1462-2920.2012.02890.x.
    • (2013) Environ. Microbiol. , vol.15 , pp. 1001-1015
    • Islam, S.T.1    Lam, J.S.2
  • 22
    • 67749139787 scopus 로고    scopus 로고
    • Streptococcus pyogenes YtgP (Spy_0390) complements Escherichia coli strains depleted of the putative peptidoglycan flippase, MurJ
    • Ruiz N. 2009. Streptococcus pyogenes YtgP (Spy_0390) complements Escherichia coli strains depleted of the putative peptidoglycan flippase, MurJ. Antimicrob. Agents Chemother. 53:3604-3605. http://dx.doi.org/10.1128/AAC.00578-09.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 3604-3605
    • Ruiz, N.1
  • 23
    • 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
  • 24
    • 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
  • 26
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research
    • Kitagawa M, Ara T, Arifuzzaman M, Ioka-Nakamichi T, Inamoto E, Toyonaga H, Mori H. 2005. Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res. 12:291-299. http://dx.doi.org/10.1093/dnares/dsi012.
    • (2005) DNA Res. , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 27
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y. 2010. I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5:725-738. http://dx.doi.org/10.1038/nprot.2010.5.
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 28
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov IN, Bourne PE. 1998. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11:739-747. http://dx.doi.org/10.1093/protein/11.9.739.
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 29
    • 84865157678 scopus 로고    scopus 로고
    • A cationic lumen in the Wzx flippase mediates anionic O-antigen subunit translocation in Pseudomonas aeruginosa PAO1
    • Islam ST, Fieldhouse RJ, Anderson EM, Taylor VL, Keates RAB, Ford RC, Lam JS. 2012. A cationic lumen in the Wzx flippase mediates anionic O-antigen subunit translocation in Pseudomonas aeruginosa PAO1. Mol. Microbiol. 84:1165-1176. http://dx.doi.org/10.1111/j.1365-2958.2012.08084.x.
    • (2012) Mol. Microbiol. , vol.84 , pp. 1165-1176
    • Islam, S.T.1    Fieldhouse, R.J.2    Anderson, E.M.3    Taylor, V.L.4    Keates, R.A.B.5    Ford, R.C.6    Lam, J.S.7
  • 30
    • 0032540320 scopus 로고    scopus 로고
    • The proton motive force, acting on acidic residues, promotes translocation of amino-terminal domains of membrane proteins when the hydrophobicity of the translocation signal is low
    • Delgado-Partin VM, Dalbey RE. 1998. The proton motive force, acting on acidic residues, promotes translocation of amino-terminal domains of membrane proteins when the hydrophobicity of the translocation signal is low. J. Biol. Chem. 273:9927-9934. http://dx.doi.org/10.1074/jbc.273.16.9927.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9927-9934
    • Delgado-Partin, V.M.1    Dalbey, R.E.2
  • 31
    • 0030953689 scopus 로고    scopus 로고
    • Negatively charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in the Escherichia coli inner membrane
    • Kiefer D, Hu X, Dalbey R, Kuhn A. 1997. Negatively charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in the Escherichia coli inner membrane. EMBO J. 16:2197-2204. http://dx.doi.org/10.1093/emboj/16.9.2197.
    • (1997) EMBO J. , vol.16 , pp. 2197-2204
    • Kiefer, D.1    Hu, X.2    Dalbey, R.3    Kuhn, A.4
  • 32
    • 0033584852 scopus 로고    scopus 로고
    • A single negatively charged residue affects the orientation of a membrane protein in the inner membrane of Escherichia coli only when it is located adjacent to a transmembrane domain
    • Rutz C, Rosenthal W, Schülein R. 1999. A single negatively charged residue affects the orientation of a membrane protein in the inner membrane of Escherichia coli only when it is located adjacent to a transmembrane domain. J. Biol. Chem. 274:33757-33763. http://dx.doi.org/10.1074/jbc.274.47.33757.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33757-33763
    • Rutz, C.1    Rosenthal, W.2    Schülein, R.3
  • 33
    • 84875195995 scopus 로고    scopus 로고
    • Charge composition features of model single-span membrane proteins that determine selection of YidC and SecYEG translocase pathways in Escherichia coli
    • Zhu L, Wasey A, White SH, Dalbey RE. 2013. Charge composition features of model single-span membrane proteins that determine selection of YidC and SecYEG translocase pathways in Escherichia coli. J. Biol. Chem. 288:7704-7716. http://dx.doi.org/10.1074/jbc.M112.429431.
    • (2013) J. Biol. Chem. , vol.288 , pp. 7704-7716
    • Zhu, L.1    Wasey, A.2    White, S.H.3    Dalbey, R.E.4
  • 34
    • 39149110299 scopus 로고    scopus 로고
    • Peptidoglycan structure and architecture
    • Vollmer W, Blanot D, De Pedro MA. 2008. Peptidoglycan structure and architecture. FEMS Microbiol. Rev. 32:149-167. http://dx.doi.org/10.1111/j.1574-6976.2007.00094.x.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 149-167
    • Vollmer, W.1    Blanot, D.2    De Pedro, M.A.3
  • 36
    • 79955654072 scopus 로고    scopus 로고
    • Arginine in membranes: the connection between molecular dynamics simulations and translocon-mediated insertion experiments
    • Schow E, Freites JA, Cheng P, Bernsel A, von Heijne G, White S, Tobias D. 2011. Arginine in membranes: the connection between molecular dynamics simulations and translocon-mediated insertion experiments. J. Membrane Biol. 239:35-48. http://dx.doi.org/10.1007/s00232-010-9330-x.
    • (2011) J. Membrane Biol. , vol.239 , pp. 35-48
    • Schow, E.1    Freites, J.A.2    Cheng, P.3    Bernsel, A.4    von Heijne, G.5    White, S.6    Tobias, D.7
  • 37
    • 84860151584 scopus 로고    scopus 로고
    • Crystal structure of Staphylococcus aureus transglycosylase in complex with a lipid II analog and elucidation of peptidoglycan synthesis mechanism
    • Huang C-Y, Shih H-W, Lin L-Y, Tien Y-W, Cheng T-JR, Cheng W-C, Wong C-H, Ma C. 2012. Crystal structure of Staphylococcus aureus transglycosylase in complex with a lipid II analog and elucidation of peptidoglycan synthesis mechanism. Proc. Natl. Acad. Sci. U. S. A. 109:6496-6501. http://dx.doi.org/10.1073/pnas.1203900109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 6496-6501
    • Huang, C.-Y.1    Shih, H.-W.2    Lin, L.-Y.3    Tien, Y.-W.4    Cheng, T.-J.R.5    Cheng, W.-C.6    Wong, C.-H.7    Ma, C.8
  • 39
    • 57649134967 scopus 로고    scopus 로고
    • Importance of the conserved residues in the peptidoglycan glycosyltransferase module of the class A penicillin-binding protein 1b of Escherichia coli
    • Terrak M, Sauvage E, Derouaux A, Dehareng D, Bouhss A, Breukink E, Jeanjean S, Nguyen-Distèche M. 2008. Importance of the conserved residues in the peptidoglycan glycosyltransferase module of the class A penicillin-binding protein 1b of Escherichia coli. J. Biol. Chem. 283: 28464-28470. http://dx.doi.org/10.1074/jbc.M803223200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 28464-28470
    • Terrak, M.1    Sauvage, E.2    Derouaux, A.3    Dehareng, D.4    Bouhss, A.5    Breukink, E.6    Jeanjean, S.7    Nguyen-Distèche, M.8
  • 40
    • 34248400401 scopus 로고    scopus 로고
    • Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis
    • Yuan Y, Barrett D, Zhang Y, Kahne D, Sliz P, Walker S. 2007. Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis. Proc. Natl. Acad. Sci. U. S. A. 104:5348-5353. http://dx.doi.org/10.1073/pnas.0701160104.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 5348-5353
    • Yuan, Y.1    Barrett, D.2    Zhang, Y.3    Kahne, D.4    Sliz, P.5    Walker, S.6
  • 41
    • 84887168855 scopus 로고    scopus 로고
    • Proton-dependent gating and proton uptake by Wzx support O-antigen-subunit antiport across the bacterial inner membrane
    • e00678-13
    • Islam ST, Eckford PDW, Jones ML, Nugent T, Bear CE, Vogel C, Lam JS. 2013. Proton-dependent gating and proton uptake by Wzx support O-antigen-subunit antiport across the bacterial inner membrane. mBio 4:e00678-13. http://dx.doi.org/10.1128/mBio.00678-13.
    • (2013) mBio , vol.4
    • Islam, S.T.1    Eckford, P.D.W.2    Jones, M.L.3    Nugent, T.4    Bear, C.E.5    Vogel, C.6    Lam, J.S.7


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