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Volumn 8, Issue SUPPL., 2003, Pages

Mechanism of antibiotic efflux in gram-negative bacteria

Author keywords

Gram Negative Bacteria; Mechanism; Microbiology; Multidrug Efflux Transporters; Review

Indexed keywords

GLYCOPROTEIN P; ANTIINFECTIVE AGENT; MULTIDRUG RESISTANCE PROTEIN;

EID: 4344652234     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1134     Document Type: Review
Times cited : (15)

References (84)
  • 1
    • 0030273002 scopus 로고    scopus 로고
    • Tetracycline resistance determinants: Mechanisms of action, regulation of expression, genetic mobility, and distribution
    • M. C. Roberts. Tetracycline resistance determinants: mechanisms of action, regulation of expression, genetic mobility, and distribution. FEMS Microbiol Rev 19, 1-24 (1996)
    • (1996) FEMS Microbiol Rev , vol.19 , pp. 1-24
    • Roberts, M.C.1
  • 3
    • 0032173598 scopus 로고    scopus 로고
    • Multiple antibiotic resistance and efflux
    • H. Nikaido. Multiple antibiotic resistance and efflux. Curr Opin Microbiol 1, 516-23 (1998)
    • (1998) Curr Opin Microbiol , vol.1 , pp. 516-523
    • Nikaido, H.1
  • 4
    • 0034791408 scopus 로고    scopus 로고
    • Multidrug resistance in Gram-negative bacteria
    • K. Poole. Multidrug resistance in Gram-negative bacteria. Curr Opin Microbiol 4, 500-8 (2001)
    • (2001) Curr Opin Microbiol , vol.4 , pp. 500-508
    • Poole, K.1
  • 5
    • 0033912430 scopus 로고    scopus 로고
    • Multidrug resistance mechanisms: Drug efflux across two membranes
    • H. I. Zgurskaya & H. Nikaido. Multidrug resistance mechanisms: drug efflux across two membranes. Molecular Microbiology 37, 219-25 (2000)
    • (2000) Molecular Microbiology , vol.37 , pp. 219-225
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 6
    • 0034799367 scopus 로고    scopus 로고
    • Efflux-mediated drug resistance in Gram-positive bacteria
    • P. N. Markham & A. A. Neyfakh. Efflux-mediated drug resistance in Gram-positive bacteria. Curr Opin Microbiol 4, 509-14 (2001)
    • (2001) Curr Opin Microbiol , vol.4 , pp. 509-514
    • Markham, P.N.1    Neyfakh, A.A.2
  • 8
    • 0033170990 scopus 로고    scopus 로고
    • The RND permease superfamily: An ancient, ubiquitous and diverse family that includes human disease and development proteins
    • T. T. Tseng, K. S. Gratwick, J. Kollman, D. Park, D. H. Nies, A. Goffeau & M. H. Saier, Jr. The RND permease superfamily: an ancient, ubiquitous and diverse family that includes human disease and development proteins. J Mol Microbiol Biotechnol 1, 107-25 (1999)
    • (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 Jr., M.H.7
  • 9
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria
    • T. Dinh, I. T. Paulsen & M. H. Saier, Jr. A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria. J Bacteriol 176, 3825-31 (1994)
    • (1994) J Bacteriol , vol.176 , pp. 3825-3831
    • Dinh, T.1    Paulsen, I.T.2    Saier Jr., M.H.3
  • 10
    • 0031278034 scopus 로고    scopus 로고
    • A family of gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from gram-negative bacteria
    • I. T. Paulsen, J. H. Park, P. S. Choi & M. H. Saier, Jr. A family of gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from gram-negative bacteria. FEMS Microbiol Lett 156, 1-8 (1997)
    • (1997) FEMS Microbiol Lett , vol.156 , pp. 1-8
    • Paulsen, I.T.1    Park, J.H.2    Choi, P.S.3    Saier Jr., M.H.4
  • 12
    • 0034115142 scopus 로고    scopus 로고
    • Interplay between efflux pumps may provide either additive or multiplicative effects on drug resistance
    • A. Lee, W. Mao, M. S. Warren, A. Mistry, K. Hoshino, R. Okumura, H. Ishida & O. Lomovskaya. Interplay between efflux pumps may provide either additive or multiplicative effects on drug resistance. J Bacteriol 182, 3142-50 (2000)
    • (2000) J Bacteriol , vol.182 , pp. 3142-3150
    • Lee, A.1    Mao, W.2    Warren, M.S.3    Mistry, A.4    Hoshino, K.5    Okumura, R.6    Ishida, H.7    Lomovskaya, O.8
  • 13
    • 0030934759 scopus 로고    scopus 로고
    • Active efflux of bile salts by Escherichia coli
    • D. G. Thanassi, L. W. Cheng & H. Nikaido. Active efflux of bile salts by Escherichia coli. J Bacteriol 179, 2512-8 (1997)
    • (1997) J Bacteriol , vol.179 , pp. 2512-2518
    • Thanassi, D.G.1    Cheng, L.W.2    Nikaido, H.3
  • 14
    • 0033515018 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa killing of Caenorhabditis elegans used to identify P. aeruginosa virulence factors
    • M. W. Tan, L. G. Rahme, J. A. Sternberg, R. G. Tompkins & F. M. Ausubel. Pseudomonas aeruginosa killing of Caenorhabditis elegans used to identify P. aeruginosa virulence factors. Proc Natl Acad Sci U S A 96, 2408-13 (1999)
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2408-2413
    • Tan, M.W.1    Rahme, L.G.2    Sternberg, J.A.3    Tompkins, R.G.4    Ausubel, F.M.5
  • 16
    • 0031661594 scopus 로고    scopus 로고
    • Influence of the MexAB-OprM multidrug efflux system on quorum sensing in Pseudomonas aeruginosa
    • K. Evans, L. Passador, R. Srikumar, E. Tsang, J. Nezezon & K. Poole. Influence of the MexAB-OprM multidrug efflux system on quorum sensing in Pseudomonas aeruginosa. J Bacteriol 180, 5443-7 (1998)
    • (1998) J Bacteriol , vol.180 , pp. 5443-5447
    • Evans, K.1    Passador, L.2    Srikumar, R.3    Tsang, E.4    Nezezon, J.5    Poole, K.6
  • 17
    • 0036267595 scopus 로고    scopus 로고
    • Control of the AcrAB multidrug efflux pump by quorum-sensing regulator SdiA
    • S. Rahmati, S. Yang, A. L. Davidson & E. L. Zechiedrich. Control of the AcrAB multidrug efflux pump by quorum-sensing regulator SdiA. Mol Microbiol 43, 677-85 (2002)
    • (2002) Mol Microbiol , vol.43 , pp. 677-685
    • Rahmati, S.1    Yang, S.2    Davidson, A.L.3    Zechiedrich, E.L.4
  • 18
    • 0035079739 scopus 로고    scopus 로고
    • Inhibition of efflux pumps as a novel approach to combat drug resistance in bacteria
    • O. Lomovskaya & W. Watkins. Inhibition of efflux pumps as a novel approach to combat drug resistance in bacteria. J Mol Microbiol Biotechnol 3, 225-36 (2001)
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 225-236
    • Lomovskaya, O.1    Watkins, W.2
  • 21
    • 0035353081 scopus 로고    scopus 로고
    • Multidrug efflux in Pseudomonas aeruginosa: Components, mechanisms and clinical significance
    • K. Poole & R. Srikumar. Multidrug efflux in Pseudomonas aeruginosa: components, mechanisms and clinical significance. Curr Top Med Chem 1, 59-71 (2001)
    • (2001) Curr Top Med Chem , vol.1 , pp. 59-71
    • Poole, K.1    Srikumar, R.2
  • 22
    • 0031720812 scopus 로고    scopus 로고
    • Multidrug efflux pump AcrAB of Salmonella typhimurium excretes only those beta-lactam antibiotics containing lipophilic side chains
    • H. Nikaido, M. Basina, V. Nguyen & E. Y. Rosenberg. Multidrug efflux pump AcrAB of Salmonella typhimurium excretes only those beta-lactam antibiotics containing lipophilic side chains. Journal of Bacteriology 180, 4686-92 (1998)
    • (1998) Journal of Bacteriology , vol.180 , pp. 4686-4692
    • Nikaido, H.1    Basina, M.2    Nguyen, V.3    Rosenberg, E.Y.4
  • 23
    • 0033534178 scopus 로고    scopus 로고
    • The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids
    • A. Margolles, M. Putman, H. W. van Veen & W. N. Konings. The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids. Biochemistry 38, 16298-306 (1999)
    • (1999) Biochemistry , vol.38 , pp. 16298-16306
    • Margolles, A.1    Putman, M.2    Van Veen, H.W.3    Konings, W.N.4
  • 25
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: A physiological role for the mdr2 gene
    • S. Ruetz & P. Gros. Phosphatidylcholine translocase: a physiological role for the mdr2 gene. Cell 77, 1071-81 (1994)
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Ruetz, S.1    Gros, P.2
  • 26
    • 0029781640 scopus 로고    scopus 로고
    • Multidrug resistance in Lactococcus lactis: Evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane
    • H. Bolhuis, H. W. van Veen, D. Molenaar, B. Poolman, A. J. Driessen & W. N. Konings. Multidrug resistance in Lactococcus lactis: evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane. Embo J 15, 4239-45 (1996)
    • (1996) Embo J , vol.15 , pp. 4239-4245
    • Bolhuis, H.1    Van Veen, H.W.2    Molenaar, D.3    Poolman, B.4    Driessen, A.J.5    Konings, W.N.6
  • 28
    • 0030784559 scopus 로고    scopus 로고
    • Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membrane by P-glycoprotein
    • A. B. Shapiro & V. Ling. Extraction of Hoechst 33342 from the cytoplasmic leaflet of the plasma membrane by P-glycoprotein. European Journal of Biochemistry 259, 122-129 (1997)
    • (1997) European Journal of Biochemistry , vol.259 , pp. 122-129
    • Shapiro, A.B.1    Ling, V.2
  • 29
    • 0033524927 scopus 로고    scopus 로고
    • Bioenergetics of the staphylococcal multidrug export protein QacA. Identification of distinct binding sites for monovalent and divalent cations
    • B. A. Mitchell, I. T. Paulsen, M. H. Brown & R. A. Skurray. Bioenergetics of the staphylococcal multidrug export protein QacA. Identification of distinct binding sites for monovalent and divalent cations. Journal of Biological Chemistry 274, 3541-8 (1999)
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 3541-3548
    • Mitchell, B.A.1    Paulsen, I.T.2    Brown, M.H.3    Skurray, R.A.4
  • 30
    • 0345035518 scopus 로고    scopus 로고
    • The secondary multidrug transporter LmrP contains multiple drug interaction sites
    • M. Putman, L. A. Koole, H. W. van Veen & W. N. Konings. The secondary multidrug transporter LmrP contains multiple drug interaction sites. Biochemistry 38, 13900-5 (1999)
    • (1999) Biochemistry , vol.38 , pp. 13900-13905
    • Putman, M.1    Koole, L.A.2    Van Veen, H.W.3    Konings, W.N.4
  • 31
    • 0035940473 scopus 로고    scopus 로고
    • Evidence for simultaneous binding of dissimilar substrates by the Escherichia coli multidrug transporter MdfA
    • O. Lewinson & E. Bibi. Evidence for simultaneous binding of dissimilar substrates by the Escherichia coli multidrug transporter MdfA. Biochemistry 40, 12612-8 (2001)
    • (2001) Biochemistry , vol.40 , pp. 12612-12618
    • Lewinson, O.1    Bibi, E.2
  • 32
    • 0034995904 scopus 로고    scopus 로고
    • Multidrug transporters in prokaryotic and eukaryotic cells: Physiological functions and transport mechanisms
    • C. G. Blackmore, P. A. McNaughton & H. W. van Veen. Multidrug transporters in prokaryotic and eukaryotic cells: physiological functions and transport mechanisms. Mol Membr Biol 18, 97-103 (2001)
    • (2001) Mol Membr Biol , vol.18 , pp. 97-103
    • Blackmore, C.G.1    McNaughton, P.A.2    Van Veen, H.W.3
  • 33
    • 0035853848 scopus 로고    scopus 로고
    • Major photoaffinity drug binding sites in multidrug resistance protein 1 (MRP1) are within transmembrane domains 10-11 and 16-17
    • R. Daoud, M. Julien, P. Gros & E. Georges. Major photoaffinity drug binding sites in multidrug resistance protein 1 (MRP1) are within transmembrane domains 10-11 and 16-17. J Biol Chem 276, 12324-30 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 12324-12330
    • Daoud, R.1    Julien, M.2    Gros, P.3    Georges, E.4
  • 34
    • 0032321870 scopus 로고    scopus 로고
    • Photoaffinity labels for characterizing drug interaction sites of P-glycoprotein
    • A. R. Safa. Photoaffinity labels for characterizing drug interaction sites of P-glycoprotein. Meth Enzymol 292, 289-307 (1998)
    • (1998) Meth Enzymol , vol.292 , pp. 289-307
    • Safa, A.R.1
  • 35
    • 0026580336 scopus 로고
    • Is the multidrug transporter a flippase?
    • C. F. Higgins & M. M. Gottesman. Is the multidrug transporter a flippase? Trends Biochem Sci 17, 18-21 (1992)
    • (1992) Trends Biochem Sci , vol.17 , pp. 18-21
    • Higgins, C.F.1    Gottesman, M.M.2
  • 36
    • 0036040137 scopus 로고    scopus 로고
    • How to distinguish between the vacuum cleaner and flippase mechanisms of the ImrA multi-drug transporter in Lactococcus lactis
    • J. H. Hofmeyr, J. M. Rohwer, J. L. Snoep, H. V. Westerhoff & W. N. Konings. How to distinguish between the vacuum cleaner and flippase mechanisms of the ImrA multi-drug transporter in Lactococcus lactis. Mol Biol Rep 29, 107-12 (2002)
    • (2002) Mol Biol Rep , vol.29 , pp. 107-112
    • Hofmeyr, J.H.1    Rohwer, J.M.2    Snoep, J.L.3    Westerhoff, H.V.4    Konings, W.N.5
  • 37
    • 0034212332 scopus 로고    scopus 로고
    • The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism
    • H. W. van Veen, A. Margolles, M. Muller, C. F. Higgins & W. N. Konings. The homodimeric ATP-binding cassette transporter LmrA mediates multidrug transport by an alternating two-site (two-cylinder engine) mechanism. EMBO Journal 19, 2503-14 (2000)
    • (2000) EMBO Journal , vol.19 , pp. 2503-2514
    • Van Veen, H.W.1    Margolles, A.2    Muller, M.3    Higgins, C.F.4    Konings, W.N.5
  • 38
    • 0029129966 scopus 로고
    • Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa
    • X. Z. Li, H. Nikaido & K. Poole. Role of mexA-mexB-oprM in antibiotic efflux in Pseudomonas aeruginosa. Antimicrob Agents Chemother 39, 1948-53 (1995)
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 1948-1953
    • Li, X.Z.1    Nikaido, H.2    Poole, K.3
  • 39
    • 0036889445 scopus 로고    scopus 로고
    • Chimeric Analysis of the Multicomponent Multidrug Efflux Transporters from Gram-Negative Bacteria
    • E. B. Tikhonova, Q. Wang & H. I. Zgurskaya. Chimeric Analysis of the Multicomponent Multidrug Efflux Transporters from Gram-Negative Bacteria. J Bacteriol 184, 6499-6507 (2002)
    • (2002) J Bacteriol , vol.184 , pp. 6499-6507
    • Tikhonova, E.B.1    Wang, Q.2    Zgurskaya, H.I.3
  • 40
    • 0036889033 scopus 로고    scopus 로고
    • Substrate Specificity of the RND-Type Multidrug Efflux Pumps AcrB and AcrD of Escherichia coli Is Determined Predominately by Two Large Periplasmic Loops
    • C. A. Elkins & H. Nikaido. Substrate Specificity of the RND-Type Multidrug Efflux Pumps AcrB and AcrD of Escherichia coli Is Determined Predominately by Two Large Periplasmic Loops. J Bacteriol 184, 6490-6498 (2002)
    • (2002) J Bacteriol , vol.184 , pp. 6490-6498
    • Elkins, C.A.1    Nikaido, H.2
  • 41
    • 0036437057 scopus 로고    scopus 로고
    • On the mechanism of substrate specificity by resistance nodulation division (RND)-type multidrug resistance pumps: The large periplasmic loops of MexD from Pseudomonas aeruginosa are involved in substrate recognition
    • W. Mao, M. S. Warren, D. S. Black, T. Satou, T. Murata, T. Nishino, N. Gotoh & O. Lomovskaya. On the mechanism of substrate specificity by resistance nodulation division (RND)-type multidrug resistance pumps: the large periplasmic loops of MexD from Pseudomonas aeruginosa are involved in substrate recognition. Mol Microbiol 46, 889-901 (2002)
    • (2002) Mol Microbiol , vol.46 , pp. 889-901
    • Mao, W.1    Warren, M.S.2    Black, D.S.3    Satou, T.4    Murata, T.5    Nishino, T.6    Gotoh, N.7    Lomovskaya, O.8
  • 42
    • 0034090541 scopus 로고    scopus 로고
    • AcrD of Escherichia coli is an aminoglycoside efflux pump
    • E. Y. Rosenberg, D. Ma & H. Nikaido. AcrD of Escherichia coli is an aminoglycoside efflux pump. J Bacteriol 182, 1754-6 (2000)
    • (2000) J Bacteriol , vol.182 , pp. 1754-1756
    • Rosenberg, E.Y.1    Ma, D.2    Nikaido, H.3
  • 43
    • 0345466364 scopus 로고    scopus 로고
    • Involvement of an active efflux system in the natural resistance of Pseudomonas aeruginosa to aminoglycosides
    • J. R. Aires, T. Kohler, H. Nikaido & P. Plesiat. Involvement of an active efflux system in the natural resistance of Pseudomonas aeruginosa to aminoglycosides. Antimicrob Agents Chemother 43, 2624-8 (1999)
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 2624-2628
    • Aires, J.R.1    Kohler, T.2    Nikaido, H.3    Plesiat, P.4
  • 44
    • 0344927562 scopus 로고    scopus 로고
    • Conjugate export pumps of the multidrug resistance protein (MRP) family: Localization, substrate specificity, and MRP2-mediated drug resistance
    • J. Konig, A. T. Nies, Y. Cui, I. Leier & D. Keppler. Conjugate export pumps of the multidrug resistance protein (MRP) family: localization, substrate specificity, and MRP2-mediated drug resistance. Biochim Biophys Acta 1461, 377-94 (1999)
    • (1999) Biochim Biophys Acta , vol.1461 , pp. 377-394
    • Konig, J.1    Nies, A.T.2    Cui, Y.3    Leier, I.4    Keppler, D.5
  • 46
    • 0035905808 scopus 로고    scopus 로고
    • Crystal structure of the transcription activator BmrR bound to DNA and a drug
    • E. E. Heldwein & R. G. Brennan. Crystal structure of the transcription activator BmrR bound to DNA and a drug. Nature 409, 378-82 (2001)
    • (2001) Nature , vol.409 , pp. 378-382
    • Heldwein, E.E.1    Brennan, R.G.2
  • 48
    • 0036040835 scopus 로고    scopus 로고
    • Structural mechanisms of multidrug recognition and regulation by bacterial multidrug transcription factors
    • M. A. Schumacher & R. G. Brennan. Structural mechanisms of multidrug recognition and regulation by bacterial multidrug transcription factors. Mol Microbiol 45, 885-93 (2002)
    • (2002) Mol Microbiol , vol.45 , pp. 885-893
    • Schumacher, M.A.1    Brennan, R.G.2
  • 49
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • S. Murakami, R. Nakashima, E. Yamashita & A. Yamaguchi. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419, 587-93 (2002)
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 50
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • G. Chang & C. B. Roth. Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 293, 1793-800 (2001)
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 51
    • 0036066806 scopus 로고    scopus 로고
    • The baeSR two-component regulatory system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobiocin and deoxycholate
    • N. Baranova & H. Nikaido. The baeSR two-component regulatory system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobiocin and deoxycholate. J Bacteriol 184, 4168-76 (2002)
    • (2002) J Bacteriol , vol.184 , pp. 4168-4176
    • Baranova, N.1    Nikaido, H.2
  • 52
    • 4344564806 scopus 로고    scopus 로고
    • The transmembrane domains of the ABC multidrug transporter LmrA form a cytoplasmic exposed, aqueous chamber within the membrane
    • G. J. Poelarends & W. N. Konings. The transmembrane domains of the ABC multidrug transporter LmrA form a cytoplasmic exposed, aqueous chamber within the membrane. J Biol Chem 14, 14 (2002)
    • (2002) J Biol Chem , vol.14 , pp. 14
    • Poelarends, G.J.1    Konings, W.N.2
  • 53
    • 0033543578 scopus 로고    scopus 로고
    • Energetics and topology of CzcA, a cation/proton antiporter of the resistance-nodulation-cell division protein family
    • M. Goldberg, T. Pribyl, S. Juhnke & D. H. Nies. Energetics and topology of CzcA, a cation/proton antiporter of the resistance-nodulation-cell division protein family. J Biol Chem 274, 26065-70 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 26065-26070
    • Goldberg, M.1    Pribyl, T.2    Juhnke, S.3    Nies, D.H.4
  • 55
    • 0037020216 scopus 로고    scopus 로고
    • Hedgehog-mediated patterning of the mammalian embryo requires transporter-like function of dispatched
    • Y. Ma, A. Erkner, R. Gong, S. Yao, J. Taipale, K. Basler & P. A. Beachy. Hedgehog-mediated patterning of the mammalian embryo requires transporter-like function of dispatched. Cell 111, 63-75 (2002)
    • (2002) Cell , vol.111 , pp. 63-75
    • Ma, Y.1    Erkner, A.2    Gong, R.3    Yao, S.4    Taipale, J.5    Basler, K.6    Beachy, P.A.7
  • 56
    • 0035984788 scopus 로고    scopus 로고
    • Amino Acid Residues Essential for Function of the MexF Efflux Pump Protein of Pseudomonas aeruginosa
    • J. R. Aires, J. C. Pechere, C. Van Delden & T. Kohler. Amino Acid Residues Essential for Function of the MexF Efflux Pump Protein of Pseudomonas aeruginosa. Antimicrob Agents Chemother 46, 2169-73 (2002)
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 2169-2173
    • Aires, J.R.1    Pechere, J.C.2    Van Delden, C.3    Kohler, T.4
  • 57
    • 0025134451 scopus 로고
    • Genetic analysis of an MDR-like export system: The secretion of colicin V
    • L. Gilson, H. K. Mahanty & R. Kolter. Genetic analysis of an MDR-like export system: the secretion of colicin V. Embo J 9, 3875-94 (1990)
    • (1990) Embo J , vol.9 , pp. 3875-3894
    • Gilson, L.1    Mahanty, H.K.2    Kolter, R.3
  • 58
    • 0032538793 scopus 로고    scopus 로고
    • Substrate-induced assembly of a contiguous channel for protein export from E.coli: Reversible bridging of an inner-membrane translocase to an outer membrane exit pore
    • T. Thanabalu, E. Koronakis, C. Hughes & V. Koronakis. Substrate-induced assembly of a contiguous channel for protein export from E.coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore. Embo J 17, 6487-96 (1998)
    • (1998) Embo J , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 59
    • 0031962577 scopus 로고    scopus 로고
    • Expression of Pseudomonas aeruginosa multidrug efflux pumps MexA-MexB- OprM and MexC-MexD-OprJ in a multidrug-sensitive Escherichia coli strain
    • R. Srikumar, T. Kon, N. Gotoh & K. Poole. Expression of Pseudomonas aeruginosa multidrug efflux pumps MexA-MexB- OprM and MexC-MexD-OprJ in a multidrug-sensitive Escherichia coli strain. Antimicrob Agents Chemother 42, 65-71 (1998)
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 65-71
    • Srikumar, R.1    Kon, T.2    Gotoh, N.3    Poole, K.4
  • 60
  • 61
    • 0032146271 scopus 로고    scopus 로고
    • Functional replacement of OprJ by OprM in the MexCD-OprJ multidrug efflux system of Pseudomonas aeruginosa
    • N. Gotoh, H. Tsujimoto, A. Nomura, K. Okamoto, M. Tsuda & T. Nishino. Functional replacement of OprJ by OprM in the MexCD-OprJ multidrug efflux system of Pseudomonas aeruginosa. FEMS Microbiology Letters 165, 21-7 (1998)
    • (1998) FEMS Microbiology Letters , vol.165 , pp. 21-27
    • Gotoh, N.1    Tsujimoto, H.2    Nomura, A.3    Okamoto, K.4    Tsuda, M.5    Nishino, T.6
  • 62
    • 0035091452 scopus 로고    scopus 로고
    • Suppression of hypersensitivity of Escherichia coli acrB mutant to organic solvents by integrational activation of the acrEF operon with the IS1 or IS2 element
    • K. Kobayashi, N. Tsukagoshi & R. Aono. Suppression of hypersensitivity of Escherichia coli acrB mutant to organic solvents by integrational activation of the acrEF operon with the IS1 or IS2 element. J Bacteriol 183, 2646-53 (2001)
    • (2001) J Bacteriol , vol.183 , pp. 2646-2653
    • Kobayashi, K.1    Tsukagoshi, N.2    Aono, R.3
  • 64
    • 0033940002 scopus 로고    scopus 로고
    • Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli
    • H. I. Zgurskaya & H. Nikaido. Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli. Journal of Bacteriology 182, 4264-7 (2000)
    • (2000) Journal of Bacteriology , vol.182 , pp. 4264-4267
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 65
    • 0030858697 scopus 로고    scopus 로고
    • Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion protein family, interacts with CvaB and TolC
    • J. Hwang, X. Zhong & P. C. Tai. Interactions of dedicated export membrane proteins of the colicin V secretion system: CvaA, a member of the membrane fusion protein family, interacts with CvaB and TolC. J Bacteriol 179, 6264-70 (1997)
    • (1997) J Bacteriol , vol.179 , pp. 6264-6270
    • Hwang, J.1    Zhong, X.2    Tai, P.C.3
  • 66
    • 0034973115 scopus 로고    scopus 로고
    • The TolC protein of Escherichia coli serves as a cell-surface receptor for the newly characterized TLS bacteriophage
    • G. J. German & R. Misra. The TolC protein of Escherichia coli serves as a cell-surface receptor for the newly characterized TLS bacteriophage. J Mol Biol 308, 579-85 (2001)
    • (2001) J Mol Biol , vol.308 , pp. 579-585
    • German, G.J.1    Misra, R.2
  • 67
    • 0036589207 scopus 로고    scopus 로고
    • Mechanisms of colicin binding and transport through outer membrane porins
    • Z. Cao & P. E. Klebba. Mechanisms of colicin binding and transport through outer membrane porins. Biochimie 84, 399-412 (2002)
    • (2002) Biochimie , vol.84 , pp. 399-412
    • Cao, Z.1    Klebba, P.E.2
  • 68
    • 0033623839 scopus 로고    scopus 로고
    • TolC, a macromolecular periplasmic 'chunnel'
    • K. Postle & H. Vakharia. TolC, a macromolecular periplasmic 'chunnel'. Nat Struct Biol 7, 527-30 (2000)
    • (2000) Nat Struct Biol , vol.7 , pp. 527-530
    • Postle, K.1    Vakharia, H.2
  • 69
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • V. Koronakis, A. Sharff, E. Koronakis, B. Luisi & C. Hughes. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405, 914-9 (2000)
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 70
    • 0027586320 scopus 로고
    • To1C of Escherichia coli functions as an outer membrane channel
    • R. Benz, E. Maier & I. Gentschev. To1C of Escherichia coli functions as an outer membrane channel. Zentralbl Bakteriol 278, 187-96 (1993)
    • (1993) Zentralbl Bakteriol , vol.278 , pp. 187-196
    • Benz, R.1    Maier, E.2    Gentschev, I.3
  • 71
    • 0036147130 scopus 로고    scopus 로고
    • Electrophysiological Behavior of the TolC Channel-Tunnel in Planar Lipid Bilayers
    • C. Andersen, C. Hughes & V. Koronakis. Electrophysiological Behavior of the TolC Channel-Tunnel in Planar Lipid Bilayers. J Membr Biol 185, 83-92 (2002)
    • (2002) J Membr Biol , vol.185 , pp. 83-92
    • Andersen, C.1    Hughes, C.2    Koronakis, V.3
  • 73
    • 0036015627 scopus 로고    scopus 로고
    • An aspartate ring at the TolC tunnel entrance determines ion selectivity and presents a target for blocking by large cations
    • C. Andersen, E. Koronakis, C. Hughes & V. Koronakis. An aspartate ring at the TolC tunnel entrance determines ion selectivity and presents a target for blocking by large cations. Mol Microbiol 44, 1131-9 (2002)
    • (2002) Mol Microbiol , vol.44 , pp. 1131-1139
    • Andersen, C.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 74
    • 0030696854 scopus 로고    scopus 로고
    • In vivo and in vitro studies on interactions between the components of the hemolysin (HlyA) secretion machinery of Escherichia coli
    • S. Schlor, A. Schmidt, E. Maier, R. Benz, W. Goebel & I. Gentschev. In vivo and in vitro studies on interactions between the components of the hemolysin (HlyA) secretion machinery of Escherichia coli. Mol Gen Genet 256, 306-19 (1997)
    • (1997) Mol Gen Genet , vol.256 , pp. 306-319
    • Schlor, S.1    Schmidt, A.2    Maier, E.3    Benz, R.4    Goebel, W.5    Gentschev, I.6
  • 75
    • 0035174213 scopus 로고    scopus 로고
    • Carboxy-terminal region involved in activity of Escherichia coli TolC
    • H. Yamanaka, H. Izawa & K. Okamoto. Carboxy-terminal region involved in activity of Escherichia coli TolC. J Bacteriol 183, 6961-4 (2001)
    • (2001) J Bacteriol , vol.183 , pp. 6961-6964
    • Yamanaka, H.1    Izawa, H.2    Okamoto, K.3
  • 76
    • 0035185376 scopus 로고    scopus 로고
    • Mutational analysis of the OprM outer membrane component of the MexA- MexB-OprM multidrug efflux system of Pseudomonas aeruginosa
    • X. Z. Li & K. Poole. Mutational analysis of the OprM outer membrane component of the MexA- MexB-OprM multidrug efflux system of Pseudomonas aeruginosa. J Bacteriol 183, 12-27 (2001)
    • (2001) J Bacteriol , vol.183 , pp. 12-27
    • Li, X.Z.1    Poole, K.2
  • 77
    • 0035174835 scopus 로고    scopus 로고
    • Isolation and characterization of Escherichia coli tolC mutants defective in secreting enzymatically active alpha-hemolysin
    • H. Vakharia, G. J. German & R. Misra. Isolation and characterization of Escherichia coli tolC mutants defective in secreting enzymatically active alpha-hemolysin. J Bacteriol 183, 6908-16 (2001)
    • (2001) J Bacteriol , vol.183 , pp. 6908-6916
    • Vakharia, H.1    German, G.J.2    Misra, R.3
  • 78
    • 0033534373 scopus 로고    scopus 로고
    • AcrA is a highly asymmetric protein capable of spanning the periplasm
    • H. I. Zgurskaya & H. Nikaido. AcrA is a highly asymmetric protein capable of spanning the periplasm. J. Mol. Biol. 285, 409-420 (1999)
    • (1999) J. Mol. Biol. , vol.285 , pp. 409-420
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 79
    • 0035782880 scopus 로고    scopus 로고
    • Lipid-layer crystallization and preliminary three-dimensional structural analysis of AcrA, the periplasmic component of a bacterial multidrug efflux pump
    • A. J. Avila-Sakar, S. Misaghi, E. M. Wilson-Kubalek, K. H. Downing, H. Zgurskaya, H. Nikaido & E. Nogales. Lipid-layer crystallization and preliminary three-dimensional structural analysis of AcrA, the periplasmic component of a bacterial multidrug efflux pump. J Struct Biol 136, 81-8 (2001)
    • (2001) J Struct Biol , vol.136 , pp. 81-88
    • Avila-Sakar, A.J.1    Misaghi, S.2    Wilson-Kubalek, E.M.3    Downing, K.H.4    Zgurskaya, H.5    Nikaido, H.6    Nogales, E.7
  • 80
    • 0033515434 scopus 로고    scopus 로고
    • Alignment and structure prediction of divergent protein families: Periplasmic and outer membrane proteins of bacterial efflux pumps
    • J. M. Johnson & G. M. Church. Alignment and structure prediction of divergent protein families: periplasmic and outer membrane proteins of bacterial efflux pumps. J Mol Biol 287, 695-715 (1999)
    • (1999) J Mol Biol , vol.287 , pp. 695-715
    • Johnson, J.M.1    Church, G.M.2
  • 81
    • 0034681390 scopus 로고    scopus 로고
    • Function of the membrane fusion protein, MexA, of the MexA, B-OprM efflux pump in Pseudomonas aeruginosa without an anchoring membrane
    • H. Yoneyama, H. Maseda, H. Kamiguchi & T. Nakae. Function of the membrane fusion protein, MexA, of the MexA, B-OprM efflux pump in Pseudomonas aeruginosa without an anchoring membrane. J Biol Chem 275, 4628-34 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 4628-4634
    • Yoneyama, H.1    Maseda, H.2    Kamiguchi, H.3    Nakae, T.4
  • 82
    • 0028151060 scopus 로고
    • Identification and characterization of two functional domains of the hemolysin translocator protein HlyD
    • R. Schulein, I. Gentschev, S. Schlor, R. Gross & W. Goebel. Identification and characterization of two functional domains of the hemolysin translocator protein HlyD. Mol Gen Genet 245, 203-11 (1994)
    • (1994) Mol Gen Genet , vol.245 , pp. 203-211
    • Schulein, R.1    Gentschev, I.2    Schlor, S.3    Gross, R.4    Goebel, W.5
  • 83
    • 0026766441 scopus 로고
    • A topological model for the haemolysin translocator protein HlyD
    • R. Schulein, I. Gentschev, H. J. Mollenkopf & W. Goebel. A topological model for the haemolysin translocator protein HlyD. Mol Gen Genet 234, 155-63 (1992)
    • (1992) Mol Gen Genet , vol.234 , pp. 155-163
    • Schulein, R.1    Gentschev, I.2    Mollenkopf, H.J.3    Goebel, W.4
  • 84
    • 0035955547 scopus 로고    scopus 로고
    • Substrate-triggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli
    • L. Balakrishnan, C. Hughes & V. Koronakis. Substrate-triggered recruitment of the TolC channel-tunnel during type I export of hemolysin by Escherichia coli. J Mol Biol 313, 501-10 (2001)
    • (2001) J Mol Biol , vol.313 , pp. 501-510
    • Balakrishnan, L.1    Hughes, C.2    Koronakis, V.3


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