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Volumn 380, Issue 2, 2009, Pages 338-342

The multidrug resistance efflux complex, EmrAB from Escherichia coli forms a dimer in vitro

Author keywords

EmrAB TolC; Membrane transport; Multidrug resistance; Oligomer; Single particle electron microscopy; Tripartite efflux system

Indexed keywords

CARRIER PROTEIN; DIMER; EMRA; EMRB; HYBRID PROTEIN; MEMBRANE FUSION PROTEIN; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN; TOLC PROTEIN; UNCLASSIFIED DRUG;

EID: 60349111859     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.01.081     Document Type: Article
Times cited : (57)

References (33)
  • 3
    • 0034792632 scopus 로고    scopus 로고
    • The role of the TolC family in protein transport and multidrug efflux
    • Sharff A., Fanutti C., Shyi J., Calladine C., and Luisi B. The role of the TolC family in protein transport and multidrug efflux. Eur. J. Biochem. 268 (2001) 5011-5026
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5011-5026
    • Sharff, A.1    Fanutti, C.2    Shyi, J.3    Calladine, C.4    Luisi, B.5
  • 5
    • 0042430540 scopus 로고    scopus 로고
    • Multidrug exporting secondary transporters
    • Murakami S., and Yamaguchi A. Multidrug exporting secondary transporters. Curr. Opin. Struct. Biol. 13 2003 (2003) 443-452
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , Issue.2003 , pp. 443-452
    • Murakami, S.1    Yamaguchi, A.2
  • 6
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S., Nakashima R., Yamashita E., and Yamaguchi A. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419 (2002) 587-593
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 7
    • 3542998054 scopus 로고    scopus 로고
    • AcrA, AcrB, TolC of Escherichia coli form a stable intermembrane multidrug efflux complex
    • Tikhonova E.B., and Zgurskaya H.I. AcrA, AcrB, TolC of Escherichia coli form a stable intermembrane multidrug efflux complex. J. Biol. Chem. 279 (2004) 32116-32124
    • (2004) J. Biol. Chem. , vol.279 , pp. 32116-32124
    • Tikhonova, E.B.1    Zgurskaya, H.I.2
  • 8
    • 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. 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 (1998) 6487-6496
    • (1998) EMBO J. , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 9
    • 27844467773 scopus 로고    scopus 로고
    • A molecular understanding of the catalytic cycle of the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva J., Jenewan S., Oswald C., Jumpertz T., Holland I.B., and Schmitt L. A molecular understanding of the catalytic cycle of the nucleotide-binding domain of the ABC transporter HlyB. Biochem. Soc. Trans. 33 (2005) 990-995
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 990-995
    • Zaitseva, J.1    Jenewan, S.2    Oswald, C.3    Jumpertz, T.4    Holland, I.B.5    Schmitt, L.6
  • 10
    • 0026686805 scopus 로고
    • Emr, an Escherichia coli locus for multidrug resistance
    • Lomovskaya O., and Lewis K. Emr, an Escherichia coli locus for multidrug resistance. Proc. Natl. Acad. Sci. USA 89 (1992) 8938-8942
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8938-8942
    • Lomovskaya, O.1    Lewis, K.2
  • 11
    • 0034699320 scopus 로고    scopus 로고
    • Translocases: a bacterial tunnel for drugs and proteins
    • Lewis K. Translocases: a bacterial tunnel for drugs and proteins. Curr. Biol. 10 (2000) R678-R681
    • (2000) Curr. Biol. , vol.10
    • Lewis, K.1
  • 12
    • 0038670226 scopus 로고    scopus 로고
    • Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump
    • Yu E.W., McDermott G., Zgurskaya H.I., Nikaido H., and Koshland Jr. D.E. Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump. Science 300 (2003) 976-980
    • (2003) Science , vol.300 , pp. 976-980
    • Yu, E.W.1    McDermott, G.2    Zgurskaya, H.I.3    Nikaido, H.4    Koshland Jr., D.E.5
  • 13
    • 2942731519 scopus 로고    scopus 로고
    • Crystal structure of the membrane fusion proteins, MexA, of the multidrug transpoter in Pseudomonas aeruginosa
    • Akama H., Matsuura T., Kashiwagi S., Yoneymara H., Narita S., Tsukihara T., Nakagawa A., and Nakae T. Crystal structure of the membrane fusion proteins, MexA, of the multidrug transpoter in Pseudomonas aeruginosa. J. Biol. Chem. 279 2004 (2004) 25939-25942
    • (2004) J. Biol. Chem. , vol.279 , Issue.2004 , pp. 25939-25942
    • Akama, H.1    Matsuura, T.2    Kashiwagi, S.3    Yoneymara, H.4    Narita, S.5    Tsukihara, T.6    Nakagawa, A.7    Nakae, T.8
  • 15
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis V., Sharff A., Koronakis E., Luisi B., and Hughes C. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405 (2000) 914-919
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 16
    • 33644833626 scopus 로고    scopus 로고
    • Conformational flexibility in the multidrug efflux system protein AcrA
    • Mikolosko J., Bobyk K., Zgurskaya H.I., and Ghosh P. Conformational flexibility in the multidrug efflux system protein AcrA. Structure 14 (2006) 577-587
    • (2006) Structure , vol.14 , pp. 577-587
    • Mikolosko, J.1    Bobyk, K.2    Zgurskaya, H.I.3    Ghosh, P.4
  • 17
    • 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. Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system. Mol. Microbiol. 53 (2004) 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
  • 18
    • 25144504245 scopus 로고    scopus 로고
    • A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study
    • Yu E.W., Aires J.R., McDermott G., and Nikaido H. A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study. J. Bacteriol. 187 (2005) 6804-6815
    • (2005) J. Bacteriol. , vol.187 , pp. 6804-6815
    • Yu, E.W.1    Aires, J.R.2    McDermott, G.3    Nikaido, H.4
  • 19
    • 33847616996 scopus 로고    scopus 로고
    • Substrate competition studies using whole-cell accumulation assays with the major tripartite multidrug efflux pumps of Escherichia coli
    • Elkins C.A., and Mullis L.B. Substrate competition studies using whole-cell accumulation assays with the major tripartite multidrug efflux pumps of Escherichia coli. Antimicrob. Agents Chemother. 51 (2007) 923-929
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 923-929
    • Elkins, C.A.1    Mullis, L.B.2
  • 20
    • 31344433137 scopus 로고    scopus 로고
    • Mammalian steroid hormones are substrates for the major RND- and MFS-type tripartite efflux pumps of Escherichia coli
    • Elkins C.A., and Mullis L.B. Mammalian steroid hormones are substrates for the major RND- and MFS-type tripartite efflux pumps of Escherichia coli. J. Bacteriol. 188 (2006) 1191-1195
    • (2006) J. Bacteriol. , vol.188 , pp. 1191-1195
    • Elkins, C.A.1    Mullis, L.B.2
  • 21
  • 22
    • 34248359106 scopus 로고    scopus 로고
    • A periplasmic coilecoil interface underlying TolC recruitment and the assembly of bacterial drug efflux pumps
    • Lobedanz S., Bokma E., Symmons M.F., Koronakis E., Hughes C., and Koronakis V. A periplasmic coilecoil interface underlying TolC recruitment and the assembly of bacterial drug efflux pumps. Proc. Natl. Acad. Sci. USA 14 (2007) 4612-4617
    • (2007) Proc. Natl. Acad. Sci. USA , vol.14 , pp. 4612-4617
    • Lobedanz, S.1    Bokma, E.2    Symmons, M.F.3    Koronakis, E.4    Hughes, C.5    Koronakis, V.6
  • 24
    • 33646271643 scopus 로고    scopus 로고
    • The hydantoin transport protein from Microbacterium liquefaciens
    • Suzuki S., and Henderson P.J.F. The hydantoin transport protein from Microbacterium liquefaciens. J. Bacteriol. 188 (2006) 3329-3336
    • (2006) J. Bacteriol. , vol.188 , pp. 3329-3336
    • Suzuki, S.1    Henderson, P.J.F.2
  • 25
    • 1542779653 scopus 로고    scopus 로고
    • Expression and purification of the amphipathic form of rabbit cytochrome b5 in Escherichia coli
    • Selinsky B.S. (Ed), Humana Press, New Jersey
    • Waskell L. Expression and purification of the amphipathic form of rabbit cytochrome b5 in Escherichia coli. In: Selinsky B.S. (Ed). Membrane Protein Protocols: Expression, Purification, and Characterization (2003), Humana Press, New Jersey 3-9
    • (2003) Membrane Protein Protocols: Expression, Purification, and Characterization , pp. 3-9
    • Waskell, L.1
  • 26
    • 0033594886 scopus 로고    scopus 로고
    • Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli
    • Zgurskaya H.I., and Nikaido H. Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli. Proc. Natl. Acad. Sci. USA 96 (1999) 7190-7195
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7190-7195
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 27
    • 4444282465 scopus 로고    scopus 로고
    • The reconstitution and activity of the small multidrug transporter EmrE is modulated by non-bilayer lipid composition
    • Curnow P., Lorch M., Charalambous K., and Booth P.J. The reconstitution and activity of the small multidrug transporter EmrE is modulated by non-bilayer lipid composition. J. Mol. Biol. 343 (2004) 213-222
    • (2004) J. Mol. Biol. , vol.343 , pp. 213-222
    • Curnow, P.1    Lorch, M.2    Charalambous, K.3    Booth, P.J.4
  • 28
    • 3142538754 scopus 로고    scopus 로고
    • Seeing GroEL at 6 Å resolution by single particle electron cryomicroscopy
    • Ludtke S.J., Chen D.H., Song J.L., Chuang D.T., and Chiu W. Seeing GroEL at 6 Å resolution by single particle electron cryomicroscopy. Structure 12 (2004) 1129-1136
    • (2004) Structure , vol.12 , pp. 1129-1136
    • Ludtke, S.J.1    Chen, D.H.2    Song, J.L.3    Chuang, D.T.4    Chiu, W.5
  • 29
    • 0029916485 scopus 로고    scopus 로고
    • A new generation of the IMAGIC image processing system
    • van Heel M., Harauz G., and Orlova E.V. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116 (1996) 17-24
    • (1996) J. Struct. Biol. , vol.116 , pp. 17-24
    • van Heel, M.1    Harauz, G.2    Orlova, E.V.3
  • 30
    • 0033989509 scopus 로고    scopus 로고
    • 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis
    • Nield J., Orlova E.V., Morris E.P., Gowen B., van Heel M., and Barber J. 3D map of the plant photosystem II supercomplex obtained by cryoelectron microscopy and single particle analysis. Nat. Struct. Biol. 7 (2000) 44-47
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 44-47
    • Nield, J.1    Orlova, E.V.2    Morris, E.P.3    Gowen, B.4    van Heel, M.5    Barber, J.6
  • 32
    • 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
    • Avila-Sakar A.J., Misaghi S., Wilson-Kubalek E.M., Downing K.H., Zgurskaya H., Nikaido H., and Nogales E. Lipid-layer crystallization and preliminary three-dimensional structural analysis of AcrA, the periplasmic component of a bacterial multidrug efflux pump. J. Struct. Biol. 136 (2001) 81-88
    • (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
  • 33
    • 0041659129 scopus 로고    scopus 로고
    • Linkage of the efflux-pump expression level with substrate extrusion rate in the MexAB-OprM efflux pump of Pseudomonas aeruginosa
    • Narita S., Eda S., Yoshihara E., and Nakae T. Linkage of the efflux-pump expression level with substrate extrusion rate in the MexAB-OprM efflux pump of Pseudomonas aeruginosa. Biochem. Biophys. Res. Commun. 308 (2003) 922-926
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 922-926
    • Narita, S.1    Eda, S.2    Yoshihara, E.3    Nakae, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.