메뉴 건너뛰기




Volumn 63, Issue 3, 2007, Pages 895-910

Reconstitution of the Escherichia coli macrolide transporter: The periplasmic membrane fusion protein MacA stimulates the ATPase activity of MacB

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; MACA PROTEIN; MACB PROTEIN; MACROLIDE; MEMBRANE FUSION PROTEIN; OUTER MEMBRANE PROTEIN; PHOSPHOLIPID; TOLC PROTEIN; UNCLASSIFIED DRUG;

EID: 33846263341     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05549.x     Document Type: Article
Times cited : (93)

References (50)
  • 1
    • 14644397893 scopus 로고    scopus 로고
    • Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli
    • Aires, J.R., and Nikaido, H. (2005) Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli. J Bacteriol 187: 1923-1929.
    • (2005) J Bacteriol , vol.187 , pp. 1923-1929
    • Aires, J.R.1    Nikaido, H.2
  • 2
    • 2942731519 scopus 로고    scopus 로고
    • Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa
    • Akama, H., Matsuura, T., Kashiwagi, S., Yoneyama, H., Narita, S., Tsukihara, T., et al. (2004) Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa. J Biol Chem 279: 25939-25942.
    • (2004) J Biol Chem , vol.279 , pp. 25939-25942
    • Akama, H.1    Matsuura, T.2    Kashiwagi, S.3    Yoneyama, H.4    Narita, S.5    Tsukihara, T.6
  • 3
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phospholipids
    • Ames, B.N. (1966) Assay of inorganic phosphate, total phosphate and phospholipids. Methods Enzymol VIII: 115-118.
    • (1966) Methods Enzymol , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 4
    • 0035425018 scopus 로고    scopus 로고
    • Protein export and drug efflux through bacterial channel-tunnels
    • Andersen, C., Hughes, C., and Koronakis, V. (2001) Protein export and drug efflux through bacterial channel-tunnels. Curr Opin Cell Biol 13: 412-416.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 412-416
    • Andersen, C.1    Hughes, C.2    Koronakis, V.3
  • 5
    • 33645803827 scopus 로고    scopus 로고
    • Identification of Bacillus subtilis sigma-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacilli
    • Butcher, B.G., and Helmann, J.D. (2006) Identification of Bacillus subtilis sigma-dependent genes that provide intrinsic resistance to antimicrobial compounds produced by Bacilli. Mol Microbiol 60: 765-782.
    • (2006) Mol Microbiol , vol.60 , pp. 765-782
    • Butcher, B.G.1    Helmann, J.D.2
  • 6
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 7
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins
    • Davidson, A.L., Shuman, H.A., and Nikaido, H. (1992) Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins. Proc Natl Acad Sci USA 89: 2360-2364.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2360-2364
    • Davidson, A.L.1    Shuman, H.A.2    Nikaido, H.3
  • 8
    • 0032322690 scopus 로고    scopus 로고
    • Erwinia metalloprotease permease: Aspects of secretion pathway and secretion functions
    • Delepelaire, P. (1998) Erwinia metalloprotease permease: aspects of secretion pathway and secretion functions. Methods Enzymol 292: 67-81.
    • (1998) Methods Enzymol , vol.292 , pp. 67-81
    • Delepelaire, P.1
  • 9
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria
    • Dinh, T., Paulsen, I.T., and Saier, M.H., Jr (1994) A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria. J Bacteriol 176: 3825-3831.
    • (1994) J Bacteriol , vol.176 , pp. 3825-3831
    • Dinh, T.1    Paulsen, I.T.2    Saier Jr, M.H.3
  • 10
    • 0029804316 scopus 로고    scopus 로고
    • Efficient purification and reconstitution of P-glycoprotein for functional and structural studies
    • Dong, M., Penin, F., and Baggetto, L.G. (1996) Efficient purification and reconstitution of P-glycoprotein for functional and structural studies. J Biol Chem 271: 28875-28883.
    • (1996) J Biol Chem , vol.271 , pp. 28875-28883
    • Dong, M.1    Penin, F.2    Baggetto, L.G.3
  • 11
    • 9944247705 scopus 로고    scopus 로고
    • Three's company: Component structures bring a closer view of tripartite drug efflux pumps
    • Eswaran, J., Koronakis, E., Higgins, M.K., Hughes, C., and Koronakis, V. (2004) Three's company: component structures bring a closer view of tripartite drug efflux pumps. Curr Opin Struct Biol 14: 741-747.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 741-747
    • Eswaran, J.1    Koronakis, E.2    Higgins, M.K.3    Hughes, C.4    Koronakis, V.5
  • 12
    • 31844452412 scopus 로고    scopus 로고
    • Insight in eukaryotic ABC transporter function by mutation analysis
    • Frelet, A., and Klein, M. (2006) Insight in eukaryotic ABC transporter function by mutation analysis. FEBS Lett 580: 1064-1084.
    • (2006) FEBS Lett , vol.580 , pp. 1064-1084
    • Frelet, A.1    Klein, M.2
  • 13
    • 0025134451 scopus 로고
    • Genetic analysis of an MDR-like export system: The secretion of colicin V
    • Gilson, L., Mahanty, H.K., and Kolter, R. (1990) Genetic analysis of an MDR-like export system: the secretion of colicin V. EMBO J 9: 3875-3894.
    • (1990) EMBO J , vol.9 , pp. 3875-3894
    • Gilson, L.1    Mahanty, H.K.2    Kolter, R.3
  • 14
    • 0034014613 scopus 로고    scopus 로고
    • Membrane-fusion protein homologues in Gram-positive bacteria
    • Harley, K.T., Djordjevic, G.M., Tseng, T., and Saier, M.H., Jr (2000) Membrane-fusion protein homologues in Gram-positive bacteria. Mol Microbiol 36: 516-157.
    • (2000) Mol Microbiol , vol.36 , pp. 516-157
    • Harley, K.T.1    Djordjevic, G.M.2    Tseng, T.3    Saier Jr, M.H.4
  • 16
    • 0032698874 scopus 로고    scopus 로고
    • ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans
    • Holland, I.B., and Blight, M.A. (1999) ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J Mol Biol 293: 381-399.
    • (1999) J Mol Biol , vol.293 , pp. 381-399
    • Holland, I.B.1    Blight, M.A.2
  • 17
    • 10044231647 scopus 로고    scopus 로고
    • Interaction between the TolC and AcrA proteins of a multidrug efflux system of Escherichia coli
    • Husain, F., Humbard, M., and Misra, R. (2004) Interaction between the TolC and AcrA proteins of a multidrug efflux system of Escherichia coli. J Bacteriol 186: 8533-8536.
    • (2004) J Bacteriol , vol.186 , pp. 8533-8536
    • Husain, F.1    Humbard, M.2    Misra, R.3
  • 18
    • 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
    • Hwang, J., Zhong, X., and Tai, P.C. (1997) 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: 6264-6270.
    • (1997) J Bacteriol , vol.179 , pp. 6264-6270
    • Hwang, J.1    Zhong, X.2    Tai, P.C.3
  • 19
    • 0032483039 scopus 로고    scopus 로고
    • Unidirectional reconstitution and characterization of purified Na+/proline transporter of Escherichia coli
    • Jung, H., Tebbe, S., Schmid, R., and Jung, K. (1998) Unidirectional reconstitution and characterization of purified Na+/proline transporter of Escherichia coli. Biochemistry 37: 11083-11088.
    • (1998) Biochemistry , vol.37 , pp. 11083-11088
    • Jung, H.1    Tebbe, S.2    Schmid, R.3    Jung, K.4
  • 20
    • 0002650761 scopus 로고    scopus 로고
    • Cytoplasmic membrane
    • Neidhardt, F.C, ed, Washington, DC: American Society for Microbiology Press, pp
    • Kadner, R. (1996) Cytoplasmic membrane. In Escherichia coli and Salmonella: Cellular and Molecular Biology, Vol. 1. Neidhardt, F.C. (ed.). Washington, DC: American Society for Microbiology Press, pp. 58-87.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , vol.1 , pp. 58-87
    • Kadner, R.1
  • 21
    • 0034806355 scopus 로고    scopus 로고
    • Novel macrolide-specific ABC-type efflux transporter in Escherichia coli
    • Kobayashi, N., Nishino, K., and Yamaguchi, A. (2001) Novel macrolide-specific ABC-type efflux transporter in Escherichia coli. J Bacteriol 183: 5639-5644.
    • (2001) J Bacteriol , vol.183 , pp. 5639-5644
    • Kobayashi, N.1    Nishino, K.2    Yamaguchi, A.3
  • 22
    • 0037523158 scopus 로고    scopus 로고
    • Membrane topology of ABC-type macrolide antibiotic exporter MacB in Escherichia coli
    • Kobayashi, N., Nishino, K., Hirata, T., and Yamaguchi, A. (2003) Membrane topology of ABC-type macrolide antibiotic exporter MacB in Escherichia coli. FEBS Lett 546: 241-246.
    • (2003) FEBS Lett , vol.546 , pp. 241-246
    • Kobayashi, N.1    Nishino, K.2    Hirata, T.3    Yamaguchi, A.4
  • 23
    • 33646876880 scopus 로고    scopus 로고
    • Stimulation of the ATPase activity of the yeast mitochondrial ABC transporter Atm1p by thiol compounds
    • Kuhnke, G., Neumann, K., Muhlenhoff, U., and Lill, R. (2006) Stimulation of the ATPase activity of the yeast mitochondrial ABC transporter Atm1p by thiol compounds. Mol Membr Biol 23: 173-184.
    • (2006) Mol Membr Biol , vol.23 , pp. 173-184
    • Kuhnke, G.1    Neumann, K.2    Muhlenhoff, U.3    Lill, R.4
  • 24
    • 0029908021 scopus 로고    scopus 로고
    • Protein secretion in gram-negative bacteria: Assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding
    • Letoffe, S., Delepelaire, P., and Wandersman, C. (1996) Protein secretion in gram-negative bacteria: assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding. EMBO J 15: 5804-5811.
    • (1996) EMBO J , vol.15 , pp. 5804-5811
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 25
    • 0033534452 scopus 로고    scopus 로고
    • Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. Effect of different ligands and consequences for the mechanism of action
    • Liu, C.E., Liu, P.Q., Wolf, A., Lin, E., and Ames, G.F. (1999) Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. Effect of different ligands and consequences for the mechanism of action. J Biol Chem 274: 739-747.
    • (1999) J Biol Chem , vol.274 , pp. 739-747
    • Liu, C.E.1    Liu, P.Q.2    Wolf, A.3    Lin, E.4    Ames, G.F.5
  • 26
    • 0032562793 scopus 로고    scopus 로고
    • Direct formation of mixed micelles in the solubilization of phospholipid liposomes by Triton X-100
    • Lopez, O., de la Maza, A., Coderch, L., Lopez-Iglesias, C., Wehrli, E., and Parra, J.L. (1998) Direct formation of mixed micelles in the solubilization of phospholipid liposomes by Triton X-100. FEBS Lett 426: 314-318.
    • (1998) FEBS Lett , vol.426 , pp. 314-318
    • Lopez, O.1    de la Maza, A.2    Coderch, L.3    Lopez-Iglesias, C.4    Wehrli, E.5    Parra, J.L.6
  • 27
    • 0032705124 scopus 로고    scopus 로고
    • The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E. coli-based protein production
    • Matsuo, E., Sampei, G., Mizobuchi, K., and Ito, K. (1999) The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E. coli-based protein production. FEBS Lett 461: 6-8.
    • (1999) FEBS Lett , vol.461 , pp. 6-8
    • Matsuo, E.1    Sampei, G.2    Mizobuchi, K.3    Ito, K.4
  • 28
    • 33644833626 scopus 로고    scopus 로고
    • Conformational flexibility in the multidrug efflux system protein AcrA
    • Mikolosko, J., Bobyk, K., Zgurskaya, H.I., and Ghosh, P. (2006) Conformational flexibility in the multidrug efflux system protein AcrA. Structure 14: 577-587.
    • (2006) Structure , vol.14 , pp. 577-587
    • Mikolosko, J.1    Bobyk, K.2    Zgurskaya, H.I.3    Ghosh, P.4
  • 29
    • 0023432172 scopus 로고
    • Role of micF in the tolC-mediated regulation of OmpF, a major outer membrane protein of Escherichia coli K-12
    • Misra, R., and Reeves, P.R. (1987) Role of micF in the tolC-mediated regulation of OmpF, a major outer membrane protein of Escherichia coli K-12. J Bacteriol 169: 4722-4730.
    • (1987) J Bacteriol , vol.169 , pp. 4722-4730
    • Misra, R.1    Reeves, P.R.2
  • 30
    • 0035185526 scopus 로고    scopus 로고
    • A MATE family multidrug efflux transporter pumps out fluoroquinolones in Bacteroides thetaiotaomicron
    • Miyamae, S., Ueda, O., Yoshimura, F., Hwang, J., Tanaka, Y., and Nikaido, H. (2001) A MATE family multidrug efflux transporter pumps out fluoroquinolones in Bacteroides thetaiotaomicron. Antimicrob Agents Chemother 45: 3341-3346.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 3341-3346
    • Miyamae, S.1    Ueda, O.2    Yoshimura, F.3    Hwang, J.4    Tanaka, Y.5    Nikaido, H.6
  • 31
    • 16644374081 scopus 로고    scopus 로고
    • P-glycoprotein retains function when reconstituted into a sphingolipid- and cholesterol-rich environment
    • Modok, S., Heyward, C., and Callaghan, R. (2004) P-glycoprotein retains function when reconstituted into a sphingolipid- and cholesterol-rich environment. J Lipid Res 45: 1910-1918.
    • (2004) J Lipid Res , vol.45 , pp. 1910-1918
    • Modok, S.1    Heyward, C.2    Callaghan, R.3
  • 32
    • 2342664171 scopus 로고    scopus 로고
    • Assembly of the MexAB-OprM multidrug efflux system of Pseudomonas aeruginosa: Identification and characterization of mutations in mexA compromising MexA multimerization and interaction with MexB
    • Nehme, D., Li, X.Z., Elliot, R., and Poole, K. (2004) Assembly of the MexAB-OprM multidrug efflux system of Pseudomonas aeruginosa: identification and characterization of mutations in mexA compromising MexA multimerization and interaction with MexB. J Bacteriol 186: 2973-2983.
    • (2004) J Bacteriol , vol.186 , pp. 2973-2983
    • Nehme, D.1    Li, X.Z.2    Elliot, R.3    Poole, K.4
  • 33
    • 0028337332 scopus 로고
    • Maltose transport system of Escherichia coli: An ABC-type transporter
    • Nikaido, H. (1994) Maltose transport system of Escherichia coli: an ABC-type transporter. FEBS Lett 346: 55-58.
    • (1994) FEBS Lett , vol.346 , pp. 55-58
    • Nikaido, H.1
  • 34
    • 0032323640 scopus 로고    scopus 로고
    • Overview of bacterial ABC transporters
    • Nikaido, H., and Hall, J.A. (1998) Overview of bacterial ABC transporters. Methods Enzymol 292: 3-20.
    • (1998) Methods Enzymol , vol.292 , pp. 3-20
    • Nikaido, H.1    Hall, J.A.2
  • 35
    • 0035084352 scopus 로고    scopus 로고
    • AcrAB and related multidrug efflux pumps of Escherichia coli
    • Nikaido, H., and Zgurskaya, H.I. (2001) AcrAB and related multidrug efflux pumps of Escherichia coli. J Mol Microbiol Biotechnol 3: 215-218.
    • (2001) J Mol Microbiol Biotechnol , vol.3 , pp. 215-218
    • Nikaido, H.1    Zgurskaya, H.I.2
  • 36
    • 33645062695 scopus 로고    scopus 로고
    • Virulence and drug resistance roles of multidrug efflux systems of Salmonella enterica serovar Typhimurium
    • Nishino, K., Latifi, T., and Groisman, E.A. (2006) Virulence and drug resistance roles of multidrug efflux systems of Salmonella enterica serovar Typhimurium. Mol Microbiol 59: 126-141.
    • (2006) Mol Microbiol , vol.59 , pp. 126-141
    • Nishino, K.1    Latifi, T.2    Groisman, E.A.3
  • 37
    • 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
    • Paulsen, I.T., Park, J.H., Choi, P.S., and Saier, M.H., Jr (1997) 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) 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
  • 38
    • 0037055994 scopus 로고    scopus 로고
    • Multidrug transporters and antibiotic resistance in Lactococcus lactis
    • Poelarends, G.J., Mazurkiewicz, P., and Konings, W.N. (2002) Multidrug transporters and antibiotic resistance in Lactococcus lactis. Biochim Biophys Acta 1555: 1-7.
    • (2002) Biochim Biophys Acta , vol.1555 , pp. 1-7
    • Poelarends, G.J.1    Mazurkiewicz, P.2    Konings, W.N.3
  • 39
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • Ramachandra, M., Ambudkar, S.V., Chen, D., Hrycyna, C.A., Dey, S., Gottesman, M.M., and Pastan, I. (1998) Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state. Biochemistry 37: 5010-5019.
    • (1998) Biochemistry , vol.37 , pp. 5010-5019
    • Ramachandra, M.1    Ambudkar, S.V.2    Chen, D.3    Hrycyna, C.A.4    Dey, S.5    Gottesman, M.M.6    Pastan, I.7
  • 40
    • 0014171268 scopus 로고
    • Ion-exchange thin-layer chromatography. XVI. Techniques for preparation and analysis of oligonucleotides
    • Randerath, E., and Randerath, K. (1967) Ion-exchange thin-layer chromatography. XVI. Techniques for preparation and analysis of oligonucleotides. J Chromatogr 31: 485-499.
    • (1967) J Chromatogr , vol.31 , pp. 485-499
    • Randerath, E.1    Randerath, K.2
  • 41
    • 0033973103 scopus 로고    scopus 로고
    • The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil
    • Reich-Slotky, R., Panagiotidis, C., Reyes, M., and Shuman, H.A. (2000) The detergent-soluble maltose transporter is activated by maltose binding protein and verapamil. J Bacteriol 182: 993-1000.
    • (2000) J Bacteriol , vol.182 , pp. 993-1000
    • Reich-Slotky, R.1    Panagiotidis, C.2    Reyes, M.3    Shuman, H.A.4
  • 42
    • 0027937143 scopus 로고
    • ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells
    • Shapiro, A.B., and Ling, V. (1994) ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells. J Biol Chem 269: 3745-3754.
    • (1994) J Biol Chem , vol.269 , pp. 3745-3754
    • Shapiro, A.B.1    Ling, V.2
  • 43
    • 0026785288 scopus 로고
    • Pore-forming activity of OmpA protein of Escherichia coli
    • Sugawara, E., and Nikaido, H. (1992) Pore-forming activity of OmpA protein of Escherichia coli. J Biol Chem 267: 2507-2511.
    • (1992) J Biol Chem , vol.267 , pp. 2507-2511
    • Sugawara, E.1    Nikaido, H.2
  • 44
    • 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
    • Thanabalu, T., Koronakis, E., Hughes, C., and Koronakis, V. (1998) 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: 6487-6496.
    • (1998) EMBO J , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 45
    • 3542998054 scopus 로고    scopus 로고
    • AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex
    • Tikhonova, E.B., and Zgurskaya, H.I. (2004) AcrA, AcrB, and TolC of Escherichia coli form a stable intermembrane multidrug efflux complex. J Biol Chem 279: 32116-32124.
    • (2004) J Biol Chem , vol.279 , pp. 32116-32124
    • Tikhonova, E.B.1    Zgurskaya, H.I.2
  • 46
    • 3242890387 scopus 로고    scopus 로고
    • Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system
    • Touze, T., Eswaran, J., Bokma, E., Koronakis, E., Hughes, C., and Koronakis, V. (2004) Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system. Mol Microbiol 53: 697-706.
    • (2004) Mol Microbiol , vol.53 , pp. 697-706
    • Touze, T.1    Eswaran, J.2    Bokma, E.3    Koronakis, E.4    Hughes, C.5    Koronakis, V.6
  • 47
    • 0033594886 scopus 로고    scopus 로고
    • Bypassing the periplasm: Reconstitution of the AcrAB multidrug efflux pump of Escherichia coli
    • Zgurskaya, H.I., and Nikaido, H. (1999a) Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli. Proc Natl Acad Sci USA 96: 7190-7195.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7190-7195
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 48
    • 0033534373 scopus 로고    scopus 로고
    • AcrA is a highly asymmetric protein capable of spanning the periplasm
    • Zgurskaya, H.I., and Nikaido, H. (1999b) AcrA is a highly asymmetric protein capable of spanning the periplasm. J Mol Biol 285: 409-420.
    • (1999) J Mol Biol , vol.285 , pp. 409-420
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 49
    • 0033912430 scopus 로고    scopus 로고
    • Multidrug resistance mechanisms: Drug efflux across two membranes
    • Zgurskaya, H.I., and Nikaido, H. (2000a) Multidrug resistance mechanisms: drug efflux across two membranes. Mol Microbiol 37: 219-225.
    • (2000) Mol Microbiol , vol.37 , pp. 219-225
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 50
    • 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
    • Zgurskaya, H.I., and Nikaido, H. (2000b) Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli. J Bacteriol 182: 4264-4267.
    • (2000) J Bacteriol , vol.182 , pp. 4264-4267
    • Zgurskaya, H.I.1    Nikaido, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.