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Volumn 11, Issue 1, 2015, Pages 61-70

Structure and function of neisseria gonorrhoeae MtrF illuminates a class of antimetabolite efflux pumps

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN MTRF; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; MTRR PROTEIN, NEISSERIA GONORRHOEAE; REPRESSOR PROTEIN; SULFONAMIDE;

EID: 84927692255     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2015.03.003     Document Type: Article
Times cited : (40)

References (47)
  • 3
    • 0032949426 scopus 로고    scopus 로고
    • The multidrug efflux protein NorM is a prototype of a new family of transporters
    • Brown M.H., Paulsen I.T., Skurray R.A. The multidrug efflux protein NorM is a prototype of a new family of transporters. Mol. Microbiol. 1999, 31:394-395.
    • (1999) Mol. Microbiol. , vol.31 , pp. 394-395
    • Brown, M.H.1    Paulsen, I.T.2    Skurray, R.A.3
  • 5
    • 34247599895 scopus 로고    scopus 로고
    • Escherichia coli abg genes enable uptake and cleavage of the folate catabolite p-aminobenzoyl-glutamate
    • Carter E.L., Jager L., Gardner L., Hall C.C., Willis S., Green J.M. Escherichia coli abg genes enable uptake and cleavage of the folate catabolite p-aminobenzoyl-glutamate. J.Bacteriol. 2007, 189:3329-3334.
    • (2007) J.Bacteriol. , vol.189 , pp. 3329-3334
    • Carter, E.L.1    Jager, L.2    Gardner, L.3    Hall, C.C.4    Willis, S.5    Green, J.M.6
  • 6
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley D.O., Rapp M., Granseth E., Melén K., Drew D., von Heijne G. Global topology analysis of the Escherichia coli inner membrane proteome. Science 2005, 308:1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melén, K.4    Drew, D.5    von Heijne, G.6
  • 7
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko K.A., Wanner B.L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 2000, 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 8
    • 0030788246 scopus 로고    scopus 로고
    • Involvement of the gonococcal MtrE protein in the resistance of Neisseria gonorrhoeae to toxic hydrophobic agents
    • Delahay R.M., Robertson B.D., Balthazar J.T., Shafer W.M., Ison C.A. Involvement of the gonococcal MtrE protein in the resistance of Neisseria gonorrhoeae to toxic hydrophobic agents. Microbiology 1997, 143:2127-2133.
    • (1997) Microbiology , vol.143 , pp. 2127-2133
    • Delahay, R.M.1    Robertson, B.D.2    Balthazar, J.T.3    Shafer, W.M.4    Ison, C.A.5
  • 10
  • 11
    • 18944382290 scopus 로고    scopus 로고
    • Regulation of mtrF expression in Neisseria gonorrhoeae and its role in high-level antimicrobial resistance
    • Folster J.P., Shafer W.M. Regulation of mtrF expression in Neisseria gonorrhoeae and its role in high-level antimicrobial resistance. J.Bacteriol. 2005, 187:3713-3720.
    • (2005) J.Bacteriol. , vol.187 , pp. 3713-3720
    • Folster, J.P.1    Shafer, W.M.2
  • 12
    • 0029078189 scopus 로고
    • Transcriptional control of the mtr efflux system of Neisseria gonorrhoeae
    • Hagman K.E., Shafer W.M. Transcriptional control of the mtr efflux system of Neisseria gonorrhoeae. J.Bacteriol. 1995, 177:4162-4165.
    • (1995) J.Bacteriol. , vol.177 , pp. 4162-4165
    • Hagman, K.E.1    Shafer, W.M.2
  • 13
    • 0028906903 scopus 로고
    • Resistance of Neisseria gonorrhoeae to antimicrobial hydrophobic agents is modulated by the mtrRCDE efflux system
    • Hagman K.E., Pan W., Spratt B.G., Balthazar J.T., Judd R.C., Shafer W.M. Resistance of Neisseria gonorrhoeae to antimicrobial hydrophobic agents is modulated by the mtrRCDE efflux system. Microbiology 1995, 141:611-622.
    • (1995) Microbiology , vol.141 , pp. 611-622
    • Hagman, K.E.1    Pan, W.2    Spratt, B.G.3    Balthazar, J.T.4    Judd, R.C.5    Shafer, W.M.6
  • 14
    • 0030788726 scopus 로고    scopus 로고
    • The MtrD protein of Neisseria gonorrhoeae is a member of the resistance/nodulation/division protein family constituting part of an efflux system
    • Hagman K.E., Lucas C.E., Balthazar J.T., Snyder L., Nilles M., Judd R.C., Shafer W.M. The MtrD protein of Neisseria gonorrhoeae is a member of the resistance/nodulation/division protein family constituting part of an efflux system. Microbiology 1997, 143:2117-2125.
    • (1997) Microbiology , vol.143 , pp. 2117-2125
    • Hagman, K.E.1    Lucas, C.E.2    Balthazar, J.T.3    Snyder, L.4    Nilles, M.5    Judd, R.C.6    Shafer, W.M.7
  • 15
    • 0031725643 scopus 로고    scopus 로고
    • Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli
    • Hussein M.J., Green J.M., Nichols B.P. Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli. J.Bacteriol. 1998, 180:6260-6268.
    • (1998) J.Bacteriol. , vol.180 , pp. 6260-6268
    • Hussein, M.J.1    Green, J.M.2    Nichols, B.P.3
  • 17
    • 84876726390 scopus 로고    scopus 로고
    • Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pump
    • Janganan T.K., Bavro V.N., Zhang L., Borges-Walmsley M.I., Walmsley A.R. Tripartite efflux pumps: energy is required for dissociation, but not assembly or opening of the outer membrane channel of the pump. Mol. Microbiol. 2013, 88:590-602.
    • (2013) Mol. Microbiol. , vol.88 , pp. 590-602
    • Janganan, T.K.1    Bavro, V.N.2    Zhang, L.3    Borges-Walmsley, M.I.4    Walmsley, A.R.5
  • 18
    • 0021104706 scopus 로고
    • Nucleotide sequence of Escherichia coli pabA and its evolutionary relationship to trp(G)D
    • Kaplan J.B., Nichols B.P. Nucleotide sequence of Escherichia coli pabA and its evolutionary relationship to trp(G)D. J.Mol. Biol. 1983, 168:451-468.
    • (1983) J.Mol. Biol. , vol.168 , pp. 451-468
    • Kaplan, J.B.1    Nichols, B.P.2
  • 19
    • 14044254160 scopus 로고    scopus 로고
    • A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants
    • Klaus S.M.J., Wegkamp A., Sybesma W., Hugenholtz J., Gregory J.F., Hanson A.D. A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants. J.Biol. Chem. 2005, 280:5274-5280.
    • (2005) J.Biol. Chem. , vol.280 , pp. 5274-5280
    • Klaus, S.M.J.1    Wegkamp, A.2    Sybesma, W.3    Hugenholtz, J.4    Gregory, J.F.5    Hanson, A.D.6
  • 20
    • 79251563176 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump
    • Kulathila R., Kulathila R., Indic M., van den Berg B. Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump. PLoS ONE 2011, 6:e15610.
    • (2011) PLoS ONE , vol.6 , pp. e15610
    • Kulathila, R.1    Kulathila, R.2    Indic, M.3    van den Berg, B.4
  • 21
    • 0032782869 scopus 로고    scopus 로고
    • The farAB-encoded efflux pump mediates resistance of gonococci to long-chained antibacterial fatty acids
    • Lee E.H., Shafer W.M. The farAB-encoded efflux pump mediates resistance of gonococci to long-chained antibacterial fatty acids. Mol. Microbiol. 1999, 33:839-845.
    • (1999) Mol. Microbiol. , vol.33 , pp. 839-845
    • Lee, E.H.1    Shafer, W.M.2
  • 22
    • 84891826713 scopus 로고    scopus 로고
    • Crystal structures of CusC review conformational changes accompanying folding and transmembrane channel formation
    • Lei H.T., Bolla J.R., Bishop N.R., Su C.C., Yu E.W. Crystal structures of CusC review conformational changes accompanying folding and transmembrane channel formation. J.Mol. Biol. 2014, 426:403-411.
    • (2014) J.Mol. Biol. , vol.426 , pp. 403-411
    • Lei, H.T.1    Bolla, J.R.2    Bishop, N.R.3    Su, C.C.4    Yu, E.W.5
  • 24
    • 0029129966 scopus 로고
    • Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa
    • Li X.Z., Nikaido H., Poole K. Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 1995, 39:1948-1953.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1948-1953
    • Li, X.Z.1    Nikaido, H.2    Poole, K.3
  • 25
    • 50949102768 scopus 로고    scopus 로고
    • Functional cloning and characterization of the multidrug efflux pumps NorM from Neisseria gonorrhoeae and YdhE from Escherichia coli
    • Long F., Rouquette-Loughlin C., Shafer W.M., Yu E.W. Functional cloning and characterization of the multidrug efflux pumps NorM from Neisseria gonorrhoeae and YdhE from Escherichia coli. Antimicrob. Agents Chemother. 2008, 52:3052-3060.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 3052-3060
    • Long, F.1    Rouquette-Loughlin, C.2    Shafer, W.M.3    Yu, E.W.4
  • 26
    • 77957141422 scopus 로고    scopus 로고
    • Crystal structures of the CusA heavy-metal efflux pump suggest methionine-mediated metal transport mechanism
    • Long F., Su C.-C., Zimmermann M.T., Boyken S.E., Rajashankar K.R., Jernigan R.L., Yu E.W. Crystal structures of the CusA heavy-metal efflux pump suggest methionine-mediated metal transport mechanism. Nature 2010, 467:484-488.
    • (2010) Nature , vol.467 , pp. 484-488
    • Long, F.1    Su, C.-C.2    Zimmermann, M.T.3    Boyken, S.E.4    Rajashankar, K.R.5    Jernigan, R.L.6    Yu, E.W.7
  • 28
    • 0029113544 scopus 로고
    • Importance of lipooligosaccharide structure in determining gonococcal resistance to hydrophobic antimicrobial agents resulting from the mtr efflux system
    • Lucas C.E., Hagman K.E., Levin J.C., Stein D.C., Shafer W.M. Importance of lipooligosaccharide structure in determining gonococcal resistance to hydrophobic antimicrobial agents resulting from the mtr efflux system. Mol. Microbiol. 1995, 16:1001-1009.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1001-1009
    • Lucas, C.E.1    Hagman, K.E.2    Levin, J.C.3    Stein, D.C.4    Shafer, W.M.5
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor M. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, M.2
  • 31
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: a graphical user interface formacromolecular phasing with SHELX programs
    • Pape T., Schneider T.R. HKL2MAP: a graphical user interface formacromolecular phasing with SHELX programs. J.Appl. Crystallogr. 2004, 37:843-844.
    • (2004) J.Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 33
    • 0034090541 scopus 로고    scopus 로고
    • AcrD of Escherichia coli is an aminoglycoside efflux pump
    • Rosenberg E.Y., Ma D., Nikaido H. AcrD of Escherichia coli is an aminoglycoside efflux pump. J.Bacteriol. 2000, 182:1754-1756.
    • (2000) J.Bacteriol. , vol.182 , pp. 1754-1756
    • Rosenberg, E.Y.1    Ma, D.2    Nikaido, H.3
  • 34
    • 0037309093 scopus 로고    scopus 로고
    • The NorM efflux pump of Neisseria gonorrhoeae and Neisseria meningitidis recognizes antimicrobial cationic compounds
    • Rouquette-Loughlin C., Dunham S.A., Kuhn M., Balthazar J.T., Shafer W.M. The NorM efflux pump of Neisseria gonorrhoeae and Neisseria meningitidis recognizes antimicrobial cationic compounds. J.Bacteriol. 2003, 185:1101-1106.
    • (2003) J.Bacteriol. , vol.185 , pp. 1101-1106
    • Rouquette-Loughlin, C.1    Dunham, S.A.2    Kuhn, M.3    Balthazar, J.T.4    Shafer, W.M.5
  • 37
    • 0032539553 scopus 로고    scopus 로고
    • Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family
    • Shafer W.M., Qu X., Waring A.J., Lehrer R.I. Modulation of Neisseria gonorrhoeae susceptibility to vertebrate antibacterial peptides due to a member of the resistance/nodulation/division efflux pump family. Proc. Natl. Acad. Sci. USA 1998, 95:1829-1833.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1829-1833
    • Shafer, W.M.1    Qu, X.2    Waring, A.J.3    Lehrer, R.I.4
  • 38
    • 0035083379 scopus 로고    scopus 로고
    • Genetic organization and regulation of antimicrobial efflux systems possessed by Neisseria gonorrhoeae and Neisseria meningitidis
    • Shafer W.M., Veal W.L., Lee E.H., Zarantonelli L., Balthazar J.T., Rouquette C. Genetic organization and regulation of antimicrobial efflux systems possessed by Neisseria gonorrhoeae and Neisseria meningitidis. J.Mol. Microbiol. Biotechnol. 2001, 3:219-224.
    • (2001) J.Mol. Microbiol. Biotechnol. , vol.3 , pp. 219-224
    • Shafer, W.M.1    Veal, W.L.2    Lee, E.H.3    Zarantonelli, L.4    Balthazar, J.T.5    Rouquette, C.6
  • 39
    • 0035210945 scopus 로고    scopus 로고
    • Maximum-likelihood density modification using pattern recognition of structural motifs
    • Terwilliger T.C. Maximum-likelihood density modification using pattern recognition of structural motifs. Acta Crystallogr. D Biol. Crystallogr. 2001, 57:1755-1762.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1755-1762
    • Terwilliger, T.C.1
  • 40
    • 3542998054 scopus 로고    scopus 로고
    • AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex
    • Tikhonova E.B., Zgurskaya H.I. AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex. J.Biol. Chem. 2004, 279:32116-32124.
    • (2004) J.Biol. Chem. , vol.279 , pp. 32116-32124
    • Tikhonova, E.B.1    Zgurskaya, H.I.2
  • 41
    • 0033170990 scopus 로고    scopus 로고
    • The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins
    • Tseng T.T., Gratwick K.S., Kollman J., Park D., Nies D.H., Goffeau A., Saier M.H. The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. J.Mol. Microbiol. Biotechnol. 1999, 1:107-125.
    • (1999) J.Mol. Microbiol. Biotechnol. , vol.1 , pp. 107-125
    • Tseng, T.T.1    Gratwick, K.S.2    Kollman, J.3    Park, D.4    Nies, D.H.5    Goffeau, A.6    Saier, M.H.7
  • 42
    • 84903598016 scopus 로고    scopus 로고
    • Antimicrobial resistance in Neisseria gonorrhoeae in the 21st century: past, evolution, and future
    • Unemo M., Shafer W.M. Antimicrobial resistance in Neisseria gonorrhoeae in the 21st century: past, evolution, and future. Clin. Microbiol. Rev. 2014, 27:587-613.
    • (2014) Clin. Microbiol. Rev. , vol.27 , pp. 587-613
    • Unemo, M.1    Shafer, W.M.2
  • 43
    • 0037254049 scopus 로고    scopus 로고
    • Identification of a cell envelope protein (MtrF) involved in hydrophobic antimicrobial resistance in Neisseria gonorrhoeae
    • Veal W.L., Shafer W.M. Identification of a cell envelope protein (MtrF) involved in hydrophobic antimicrobial resistance in Neisseria gonorrhoeae. J.Antimicrob. Chemother. 2003, 51:27-37.
    • (2003) J.Antimicrob. Chemother. , vol.51 , pp. 27-37
    • Veal, W.L.1    Shafer, W.M.2
  • 44
    • 0036785342 scopus 로고    scopus 로고
    • Overexpression of the MtrC-MtrD-MtrE efflux pump due to an mtrR mutation is required for chromosomally mediated penicillin resistance in Neisseria gonorrhoeae
    • Veal W.L., Nicholas R.A., Shafer W.M. Overexpression of the MtrC-MtrD-MtrE efflux pump due to an mtrR mutation is required for chromosomally mediated penicillin resistance in Neisseria gonorrhoeae. J.Bacteriol. 2002, 184:5619-5624.
    • (2002) J.Bacteriol. , vol.184 , pp. 5619-5624
    • Veal, W.L.1    Nicholas, R.A.2    Shafer, W.M.3
  • 45
    • 52649131941 scopus 로고    scopus 로고
    • Clinically relevant mutations that cause derepression of the Neisseria gonorrhoeae MtrC-MtrD-MtrE Efflux pump system confer different levels of antimicrobial resistance and invivo fitness
    • Warner D.M., Shafer W.M., Jerse A.E. Clinically relevant mutations that cause derepression of the Neisseria gonorrhoeae MtrC-MtrD-MtrE Efflux pump system confer different levels of antimicrobial resistance and invivo fitness. Mol. Microbiol. 2008, 70:462-478.
    • (2008) Mol. Microbiol. , vol.70 , pp. 462-478
    • Warner, D.M.1    Shafer, W.M.2    Jerse, A.E.3
  • 46
    • 0020074927 scopus 로고
    • Use of glycerol-cryoprotected Lactobacillus casei for microbiological assay of folic acid
    • Wilson S.D., Horne D.W. Use of glycerol-cryoprotected Lactobacillus casei for microbiological assay of folic acid. Clin. Chem. 1982, 28:1198-1200.
    • (1982) Clin. Chem. , vol.28 , pp. 1198-1200
    • Wilson, S.D.1    Horne, D.W.2
  • 47
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool D., Boudker O., Jin Y., Gouaux E. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 2004, 431:811-818.
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4


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