메뉴 건너뛰기




Volumn 428, Issue 3, 2016, Pages 644-657

Molecular basis of polyspecificity of the Small Multidrug Resistance Efflux Pump AbeS from Acinetobacter baumannii

Author keywords

Antibiotic resistance; EmrE; Membrane transport; Reconstitution; Substrate promiscuity

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; ACRIFLAVINE; AMINO ACID; ANTIPORTER; BENZALKONIUM; ETHIDIUM; LIPOSOME; MEMBRANE PROTEIN; MULTIDRUG RESISTANCE PROTEIN; MULTIDRUG RESISTANCE PROTEIN EMRE; TETRAPHENYLPHOSPHONIUM; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; EMRE PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN;

EID: 84958911587     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.12.006     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 68949110351 scopus 로고    scopus 로고
    • Efflux-mediated drug resistance in bacteria: An update
    • X.-Z. Li, and H. Nikaido Efflux-mediated drug resistance in bacteria: An update Drugs 69 2009 1555 1623
    • (2009) Drugs , vol.69 , pp. 1555-1623
    • Li, X.-Z.1    Nikaido, H.2
  • 2
    • 64749086579 scopus 로고
    • Regulation and physiological function of multidrug efflux pumps in Escherichia coli and Salmonella
    • K. Nishino, E. Nikaido, and A. Yamaguchi Regulation and physiological function of multidrug efflux pumps in Escherichia coli and Salmonella Biochim. Biophys. Acta 2009 1794 834 843
    • (1794) Biochim. Biophys. Acta , vol.2009 , pp. 834-843
    • Nishino, K.1    Nikaido, E.2    Yamaguchi, A.3
  • 3
    • 84926035587 scopus 로고    scopus 로고
    • The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria
    • X.-Z. Li, P. Plésiat, and H. Nikaido The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria Clin. Microbiol. Rev. 28 2015 337 418
    • (2015) Clin. Microbiol. Rev. , vol.28 , pp. 337-418
    • Li, X.-Z.1    Plésiat, P.2    Nikaido, H.3
  • 4
    • 70349086535 scopus 로고    scopus 로고
    • CraA, a major facilitator superfamily efflux pump associated with chloramphenicol resistance in Acinetobacter baumannii
    • I. Roca, S. Marti, P. Espinal, P. Martínez, I. Gibert, and J. Vila CraA, a major facilitator superfamily efflux pump associated with chloramphenicol resistance in Acinetobacter baumannii Antimicrob. Agents Chemother. 53 2009 4013 4014
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 4013-4014
    • Roca, I.1    Marti, S.2    Espinal, P.3    Martínez, P.4    Gibert, I.5    Vila, J.6
  • 5
    • 52449130017 scopus 로고    scopus 로고
    • Clinical impact of the over-expression of efflux pump in nonfermentative Gram-negative bacilli, development of efflux pump inhibitors
    • J. Vila, and J.L. Martínez Clinical impact of the over-expression of efflux pump in nonfermentative Gram-negative bacilli, development of efflux pump inhibitors Curr. Drug Targets 9 2008 797 807
    • (2008) Curr. Drug Targets , vol.9 , pp. 797-807
    • Vila, J.1    Martínez, J.L.2
  • 7
    • 22144471145 scopus 로고    scopus 로고
    • Bacterial resistance to antibiotics: Active efflux and reduced uptake
    • A. Kumar, and H.P. Schweizer Bacterial resistance to antibiotics: Active efflux and reduced uptake Adv. Drug Deliv. Rev. 57 2005 1486 1513
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 1486-1513
    • Kumar, A.1    Schweizer, H.P.2
  • 8
    • 33747154459 scopus 로고    scopus 로고
    • Multidrug-resistance efflux pumps - Not just for resistance
    • L.J.V. Piddock Multidrug-resistance efflux pumps - Not just for resistance Nat. Rev. Microbiol. 4 2006 629 636
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 629-636
    • Piddock, L.J.V.1
  • 9
    • 84924150331 scopus 로고    scopus 로고
    • Homologs of the Acinetobacter baumannii AceI transporter represent a new family of bacterial multidrug efflux systems
    • K.A. Hassan, Q. Liu, P.J.F. Henderson, and I.T. Paulsen Homologs of the Acinetobacter baumannii AceI transporter represent a new family of bacterial multidrug efflux systems MBio 2015 10.1128/mBio.01982-14
    • (2015) MBio
    • Hassan, K.A.1    Liu, Q.2    Henderson, P.J.F.3    Paulsen, I.T.4
  • 10
    • 64649106418 scopus 로고
    • EmrE, a model for studying evolution and mechanism of ion-coupled transporters
    • S. Schuldiner EmrE, a model for studying evolution and mechanism of ion-coupled transporters Biochim. Biophys. Acta 2009 1794 748 762
    • (1794) Biochim. Biophys. Acta , vol.2009 , pp. 748-762
    • Schuldiner, S.1
  • 11
    • 84903206136 scopus 로고    scopus 로고
    • +-coupled antiporters
    • +-coupled antiporters J. Mol. Biol. 426 2014 2539 2546
    • (2014) J. Mol. Biol. , vol.426 , pp. 2539-2546
    • Schuldiner, S.1
  • 14
    • 25444519556 scopus 로고    scopus 로고
    • Exploring the binding domain of EmrE, the smallest multidrug transporter
    • M. Sharoni, S. Steiner-Mordoch, and S. Schuldiner Exploring the binding domain of EmrE, the smallest multidrug transporter J. Biol. Chem. 280 2005 32849 32855
    • (2005) J. Biol. Chem. , vol.280 , pp. 32849-32855
    • Sharoni, M.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 15
    • 0037507278 scopus 로고    scopus 로고
    • An amino acid cluster around the essential Glu-14 is part of the substrate- and proton-binding domain of EmrE, a multidrug transporter from Escherichia coli
    • N. Gutman, S. Steiner-Mordoch, and S. Schuldiner An amino acid cluster around the essential Glu-14 is part of the substrate- and proton-binding domain of EmrE, a multidrug transporter from Escherichia coli J. Biol. Chem. 278 2003 16082 16087
    • (2003) J. Biol. Chem. , vol.278 , pp. 16082-16087
    • Gutman, N.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 16
    • 33751167032 scopus 로고    scopus 로고
    • MdfA from Escherichia coli, a model protein for studying secondary multidrug transport
    • N. Sigal, D. Cohen-Karni, S. Siemion, and E. Bibi MdfA from Escherichia coli, a model protein for studying secondary multidrug transport J. Mol. Microbiol. Biotechnol. 11 2006 308 317
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 308-317
    • Sigal, N.1    Cohen-Karni, D.2    Siemion, S.3    Bibi, E.4
  • 17
    • 64649100965 scopus 로고
    • Drug transport mechanism of the AcrB efflux pump
    • K.M. Pos Drug transport mechanism of the AcrB efflux pump Biochim. Biophys. Acta 2009 1794 782 793
    • (1794) Biochim. Biophys. Acta , vol.2009 , pp. 782-793
    • Pos, K.M.1
  • 18
    • 67049115572 scopus 로고    scopus 로고
    • A coordinated network of transporters with overlapping specificities provides a robust survival strategy
    • N. Tal, and S. Schuldiner A coordinated network of transporters with overlapping specificities provides a robust survival strategy Proc. Natl. Acad. Sci. U. S. A. 106 2009 9051 9056
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9051-9056
    • Tal, N.1    Schuldiner, S.2
  • 19
    • 84355166442 scopus 로고    scopus 로고
    • Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket
    • R. Nakashima, K. Sakurai, S. Yamasaki, K. Nishino, and A. Yamaguchi Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket Nature 480 2011 565 569
    • (2011) Nature , vol.480 , pp. 565-569
    • Nakashima, R.1    Sakurai, K.2    Yamasaki, S.3    Nishino, K.4    Yamaguchi, A.5
  • 20
    • 84905399186 scopus 로고    scopus 로고
    • Switch-loop flexibility affects transport of large drugs by the promiscuous AcrB multidrug efflux transporter
    • H.J. Cha, R.T. Müller, and K.M. Pos Switch-loop flexibility affects transport of large drugs by the promiscuous AcrB multidrug efflux transporter Antimicrob. Agents Chemother. 58 2014 4767 4772
    • (2014) Antimicrob. Agents Chemother. , vol.58 , pp. 4767-4772
    • Cha, H.J.1    Müller, R.T.2    Pos, K.M.3
  • 21
    • 73849095384 scopus 로고    scopus 로고
    • Screening and quantification of the expression of antibiotic resistance genes in Acinetobacter baumannii with a microarray
    • S. Coyne, G. Guigon, P. Courvalin, and B. Périchon Screening and quantification of the expression of antibiotic resistance genes in Acinetobacter baumannii with a microarray Antimicrob. Agents Chemother. 54 2010 333 340
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 333-340
    • Coyne, S.1    Guigon, G.2    Courvalin, P.3    Périchon, B.4
  • 22
    • 57349139420 scopus 로고    scopus 로고
    • Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii
    • M.D. Adams, K. Goglin, N. Molyneaux, K.M. Hujer, H. Lavender, J.J. Jamison, and et al. Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii J. Bacteriol. 190 2008 8053 8064
    • (2008) J. Bacteriol. , vol.190 , pp. 8053-8064
    • Adams, M.D.1    Goglin, K.2    Molyneaux, N.3    Hujer, K.M.4    Lavender, H.5    Jamison, J.J.6
  • 23
    • 71249142662 scopus 로고    scopus 로고
    • Role of AbeS, a novel efflux pump of the SMR family of transporters, in resistance to antimicrobial agents in Acinetobacter baumannii
    • V.B. Srinivasan, G. Rajamohan, and W. a Gebreyes Role of AbeS, a novel efflux pump of the SMR family of transporters, in resistance to antimicrobial agents in Acinetobacter baumannii Antimicrob. Agents Chemother. 53 2009 5312 5316
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 5312-5316
    • Srinivasan, V.B.1    Rajamohan, G.2    Gebreyes, W.A.3
  • 25
    • 84945928515 scopus 로고    scopus 로고
    • Large scale determination of previously unsolved protein structures using evolutionary information
    • S. Ovchinnikov, L. Kinch, H. Park, Y. Liao, J. Pei, D.E. Kim, and et al. Large scale determination of previously unsolved protein structures using evolutionary information Elife 4 2015 e09248
    • (2015) Elife , vol.4
    • Ovchinnikov, S.1    Kinch, L.2    Park, H.3    Liao, Y.4    Pei, J.5    Kim, D.E.6
  • 27
    • 0034677201 scopus 로고    scopus 로고
    • A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
    • T.R. Muth, and S. Schuldiner A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE EMBO J. 19 2000 234 240
    • (2000) EMBO J. , vol.19 , pp. 234-240
    • Muth, T.R.1    Schuldiner, S.2
  • 28
    • 77952021098 scopus 로고    scopus 로고
    • Topologically random insertion of EmrE supports a pathway for evolution of inverted repeats in ion-coupled transporters
    • I. Nasie, S. Steiner-Mordoch, A. Gold, and S. Schuldiner Topologically random insertion of EmrE supports a pathway for evolution of inverted repeats in ion-coupled transporters J. Biol. Chem. 285 2010 15234 15244
    • (2010) J. Biol. Chem. , vol.285 , pp. 15234-15244
    • Nasie, I.1    Steiner-Mordoch, S.2    Gold, A.3    Schuldiner, S.4
  • 29
    • 0034051663 scopus 로고    scopus 로고
    • An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli
    • H. Yerushalmi, and S. Schuldiner An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli J. Biol. Chem. 275 2000 5264 5269
    • (2000) J. Biol. Chem. , vol.275 , pp. 5264-5269
    • Yerushalmi, H.1    Schuldiner, S.2
  • 30
    • 33745821170 scopus 로고    scopus 로고
    • Identification of tyrosine residues critical for the function of an ion-coupled multidrug transporter
    • D. Rotem, S. Steiner-Mordoch, and S. Schuldiner Identification of tyrosine residues critical for the function of an ion-coupled multidrug transporter J. Biol. Chem. 281 2006 18715 18722
    • (2006) J. Biol. Chem. , vol.281 , pp. 18715-18722
    • Rotem, D.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 31
    • 10344220028 scopus 로고    scopus 로고
    • EmrE, a multidrug transporter from Escherichia coli, transports monovalent and divalent substrates with the same stoichiometry
    • D. Rotem, and S. Schuldiner EmrE, a multidrug transporter from Escherichia coli, transports monovalent and divalent substrates with the same stoichiometry J. Biol. Chem. 279 2004 48787 48793
    • (2004) J. Biol. Chem. , vol.279 , pp. 48787-48793
    • Rotem, D.1    Schuldiner, S.2
  • 33
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • T. Baba, T. Ara, M. Hasegawa, Y. Takai, Y. Okumura, M. Baba, and et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection Mol. Syst. Biol. 2 2006 2006.0008
    • (2006) Mol. Syst. Biol. , vol.2 , pp. 20060008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 34
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • K.A. Datsenko, and B.L. Wanner One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products Proc. Natl. Acad. Sci. U. S. A. 97 2000 6640 6645
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 35
    • 0023189083 scopus 로고
    • Multicopy expression vectors carrying the lac repressor gene for regulated high-level expression of genes in Escherichia coli
    • M.J. Stark Multicopy expression vectors carrying the lac repressor gene for regulated high-level expression of genes in Escherichia coli Gene 51 1987 255 267
    • (1987) Gene , vol.51 , pp. 255-267
    • Stark, M.J.1
  • 36
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • S. Tabor, and C.C. Richardson A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes Proc. Natl. Acad. Sci. U. S. A. 82 1985 1074 1078
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 37
    • 79953845449 scopus 로고    scopus 로고
    • A versatile and efficient high-throughput cloning tool for structural biology
    • E.R. Geertsma, and R. Dutzler A versatile and efficient high-throughput cloning tool for structural biology Biochemistry 50 2011 3272 3278
    • (2011) Biochemistry , vol.50 , pp. 3272-3278
    • Geertsma, E.R.1    Dutzler, R.2
  • 38
    • 84934438515 scopus 로고    scopus 로고
    • Fast and easy method for construction of plasmid vectors using modified quick-change mutagenesis
    • J.W. Bok, and N.P. Keller Fast and easy method for construction of plasmid vectors using modified quick-change mutagenesis Methods Mol. Biol. 944 2012 163 174
    • (2012) Methods Mol. Biol. , vol.944 , pp. 163-174
    • Bok, J.W.1    Keller, N.P.2
  • 40
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • B. Miroux, and J.E. Walker Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels J. Mol. Biol. 260 1996 289 298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.