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Volumn 44, Issue 19, 2005, Pages 7369-7377

Substrate-induced tryptophan fluorescence changes in EmrE, the smallest ion-coupled multidrug transporter

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CONCENTRATION (PROCESS); ESCHERICHIA COLI; FLUORESCENCE; MUTAGENESIS; PROTEINS; QUENCHING; SOLUBILITY; SUBSTRATES;

EID: 18544374282     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050356t     Document Type: Article
Times cited : (52)

References (43)
  • 4
    • 0034677201 scopus 로고    scopus 로고
    • A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE
    • Muth, T. R., and Schuldiner, S. (2000) A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE, EMBO J. 19, 234-240.
    • (2000) EMBO J. , vol.19 , pp. 234-240
    • Muth, T.R.1    Schuldiner, S.2
  • 5
    • 0035930531 scopus 로고    scopus 로고
    • Functional analysis of novel multidrug transporters from human pathogens
    • Ninio, S., Rotem, D., and Schuldiner, S. (2001) Functional analysis of novel multidrug transporters from human pathogens, J. Biol. Chem. 276, 48250-48256.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48250-48256
    • Ninio, S.1    Rotem, D.2    Schuldiner, S.3
  • 7
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Elbaz, Y., Steiner-Mordoch, S., Danieli, T., and Schuldiner, S. (2004) In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state, Proc. Natl. Acad. Sci. U.S.A. 101, 1519-1524.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1519-1524
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 8
    • 0035930510 scopus 로고    scopus 로고
    • In vitro monomer swapping in EmrE, a multidrug transporter from Escherichia coli, reveals that the oligomer is the functional unit
    • Rotem, D., Sal-man, N., and Schuldiner, S. (2001) In vitro monomer swapping in EmrE, a multidrug transporter from Escherichia coli, reveals that the oligomer is the functional unit, J. Biol. Chem. 276, 48243-48249.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48243-48249
    • Rotem, D.1    Sal-man, N.2    Schuldiner, S.3
  • 9
    • 0346874401 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer
    • Ubarretxena-Belandia, I., Baldwin, J. M., Schuldiner, S., and Tate, C. G. (2003) Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer, EMBO J. 22, 6175-6181.
    • (2003) EMBO J. , vol.22 , pp. 6175-6181
    • Ubarretxena-Belandia, I.1    Baldwin, J.M.2    Schuldiner, S.3    Tate, C.G.4
  • 10
    • 3042561938 scopus 로고    scopus 로고
    • The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state
    • Butler, P., Ubarretxena-Belandia, I., Warne, T., and Tate, C. (2004) The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state, J. Mol. Biol. 340, 797-808.
    • (2004) J. Mol. Biol. , vol.340 , pp. 797-808
    • Butler, P.1    Ubarretxena-Belandia, I.2    Warne, T.3    Tate, C.4
  • 11
    • 0038146916 scopus 로고    scopus 로고
    • Characterization of an archaeal multidrug transporter with a unique amino acid composition
    • Ninio, S., and Schuldiner, S. (2003) Characterization of an archaeal multidrug transporter with a unique amino acid composition, J. Biol. Chem. 278, 12000-12005.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12000-12005
    • Ninio, S.1    Schuldiner, S.2
  • 12
    • 0034051663 scopus 로고    scopus 로고
    • An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli
    • Yerushalmi, H., and Schuldiner, S. (2000) An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli, J. Biol. Chem. 275, 5264-5269.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5264-5269
    • Yerushalmi, H.1    Schuldiner, S.2
  • 13
    • 0034733974 scopus 로고    scopus 로고
    • A common binding site for substrates and protons in EmrE, an ion-coupled multidrug transporter
    • Yerushalmi, H., and Schuldiner, S. (2000) A common binding site for substrates and protons in EmrE, an ion-coupled multidrug transporter, FEBS Lett. 476, 93-97.
    • (2000) FEBS Lett. , vol.476 , pp. 93-97
    • Yerushalmi, H.1    Schuldiner, S.2
  • 14
    • 0034610304 scopus 로고    scopus 로고
    • A model for coupling of H(+) and substrate fluxes based on "time-sharing" of a common binding site
    • Yerushalmi, H., and Schuldiner, S. (2000) A model for coupling of H(+) and substrate fluxes based on "time-sharing" of a common binding site, Biochemistry 39, 14711-14719.
    • (2000) Biochemistry , vol.39 , pp. 14711-14719
    • Yerushalmi, H.1    Schuldiner, S.2
  • 15
    • 0035918237 scopus 로고    scopus 로고
    • A single carboxyl mutant of the multidrug transporter EmrE is fully functional
    • Yerushalmi, H., Mordoch, S. S., and Schuldiner, S. (2001) A single carboxyl mutant of the multidrug transporter EmrE is fully functional, J. Biol. Chem. 276, 12744-12748.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12744-12748
    • Yerushalmi, H.1    Mordoch, S.S.2    Schuldiner, S.3
  • 16
    • 1642297145 scopus 로고    scopus 로고
    • Direct evidence for substrate induced proton release in detergent solubilized EmrE, a multidrug transporter
    • Soskine, M., Adam, Y., and Schuldiner, S. (2004) Direct evidence for substrate induced proton release in detergent solubilized EmrE, a multidrug transporter, J. Biol. Chem. 279, 9951-9955.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9951-9955
    • Soskine, M.1    Adam, Y.2    Schuldiner, S.3
  • 18
    • 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
    • Gutman, N., Steiner-Mordoch, S., and Schuldiner, S. (2003) 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, 16082-16087.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16082-16087
    • Gutman, N.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 19
    • 0036015623 scopus 로고    scopus 로고
    • Mystery of multidrug transporters: The answer can be simple
    • Neyfakh, A. A. (2002) Mystery of multidrug transporters: the answer can be simple, Mol. Microbiol. 44, 1123-1130.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1123-1130
    • Neyfakh, A.A.1
  • 20
    • 0037174841 scopus 로고    scopus 로고
    • Structural biology of bacterial multidrug resistance gene regulators
    • Godsey, M. H., Zheleznova Heldwein, E. E., and Brennan, R. G. (2002) Structural biology of bacterial multidrug resistance gene regulators, J. Biol. Chem. 277, 40169-40172.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40169-40172
    • Godsey, M.H.1    Zheleznova Heldwein, E.E.2    Brennan, R.G.3
  • 22
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami, S., Nakashima, R., Yamashita, E., and Yamaguchi, A. (2002) Crystal structure of bacterial multidrug efflux transporter AcrB, Nature 419, 587-593.
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 23
    • 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, D. E., Jr. (2003) Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump, Science 300, 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
  • 24
    • 0033525105 scopus 로고    scopus 로고
    • Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter
    • Zheleznova, E. E., Markham, P. N., Neyfakh, A. A., and Brennan, R. G. (1999) Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter, Cell 96, 353-362.
    • (1999) Cell , vol.96 , pp. 353-362
    • Zheleznova, E.E.1    Markham, P.N.2    Neyfakh, A.A.3    Brennan, R.G.4
  • 25
    • 0030043489 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D. A. (1996) Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp, Science 271, 163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 27
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and Richardson, C. (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes, Proc. Natl. Acad. Sci. U.S.A. 82, 1074-1078.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.2
  • 29
    • 0024520745 scopus 로고
    • Site directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. F., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.F.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 30
    • 0002802808 scopus 로고
    • Mutants of Escherichia coli requiring methionine or vitamin B12
    • Davies, B., and Mingioli, E. (1950) Mutants of Escherichia coli requiring methionine or vitamin B12, J. Bacteriol. 60, 17-28.
    • (1950) J. Bacteriol. , vol.60 , pp. 17-28
    • Davies, B.1    Mingioli, E.2
  • 31
    • 0029999396 scopus 로고    scopus 로고
    • Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle
    • Arkin, I. T., Russ, W. P., Lebendiker, M., and Schuldiner, S. (1996) Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle, Biochemistry 35, 7233-7238.
    • (1996) Biochemistry , vol.35 , pp. 7233-7238
    • Arkin, I.T.1    Russ, W.P.2    Lebendiker, M.3    Schuldiner, S.4
  • 32
    • 1642299702 scopus 로고    scopus 로고
    • The membrane topology of EmrE - A small multidrug transporter from Escherichia coli
    • Ninio, S., Elbaz, Y., and Schuldiner, S. (2004) The membrane topology of EmrE - a small multidrug transporter from Escherichia coli, FEBS Lett. 562, 193-196.
    • (2004) FEBS Lett. , vol.562 , pp. 193-196
    • Ninio, S.1    Elbaz, Y.2    Schuldiner, S.3
  • 33
    • 0027970086 scopus 로고
    • Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump
    • Grinius, L., and Goldberg, E. (1994) Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump, J. Biol. Chem. 269, 29998-30004.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29998-30004
    • Grinius, L.1    Goldberg, E.2
  • 34
    • 0029856981 scopus 로고    scopus 로고
    • Negative dominance studies demonstrate the oligomeric structure of emre, a multidrug antiporter from Escherichia coli
    • Yerushalmi, H., Lebendiker, M., and Schuldiner, S. (1996) Negative dominance studies demonstrate the oligomeric structure of emre, a multidrug antiporter from Escherichia coli, J. Biol. Chem. 271, 31044-31048.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31044-31048
    • Yerushalmi, H.1    Lebendiker, M.2    Schuldiner, S.3
  • 36
    • 0242363172 scopus 로고    scopus 로고
    • Exploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli
    • Vazquez-Ibar, J. L., Guan, L., Svrakic, M., and Kaback, H. R. (2003) Exploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli, Proc. Natl. Acad. Sci., U.S.A. 100, 12706-12711.
    • (2003) Proc. Natl. Acad. Sci., U.S.A. , vol.100 , pp. 12706-12711
    • Vazquez-Ibar, J.L.1    Guan, L.2    Svrakic, M.3    Kaback, H.R.4
  • 37
    • 0036591656 scopus 로고    scopus 로고
    • Cation-pi interactions in ligand recognition and catalysis
    • Zacharias, N., and Dougherty, D. A. (2002) Cation-pi interactions in ligand recognition and catalysis, Trends Pharmacol. Sci. 23, 281-287.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 281-287
    • Zacharias, N.1    Dougherty, D.A.2
  • 38
    • 0032406838 scopus 로고    scopus 로고
    • Statistical analysis of predicted transmembrane alpha-helices
    • Arkin, I. T., and Brunger, A. T. (1998) Statistical analysis of predicted transmembrane alpha-helices. Biochim. Biophys. Acta 1429, 113-128.
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 113-128
    • Arkin, I.T.1    Brunger, A.T.2
  • 39
    • 0025216064 scopus 로고
    • Design of a membrane transport protein for fluorescence spectroscopy
    • Menezes, M., Roepe, P., and Kaback, H. (1990) Design of a membrane transport protein for fluorescence spectroscopy, Proc. Natl. Acad. Sci. U.S.A. 87, 1638-1642.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 1638-1642
    • Menezes, M.1    Roepe, P.2    Kaback, H.3
  • 40
    • 0032509522 scopus 로고    scopus 로고
    • Structural studies of the melibiose permease of Escherichia coli by fluorescence resonance energy transfer. II. Identification of the tryptophan residues acting as energy donors
    • Cordat, E., Mus-Veteau, I., and Leblanc, G. (1998) Structural studies of the melibiose permease of Escherichia coli by fluorescence resonance energy transfer. II. Identification of the tryptophan residues acting as energy donors, J. Biol. Chem. 273, 33198-33202.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33198-33202
    • Cordat, E.1    Mus-Veteau, I.2    Leblanc, G.3
  • 41
    • 0028783805 scopus 로고
    • Fluorescence of native single-Trp mutants in the lactose permease from Escherichia coli: Structural properties and evidence for a substrate-induced conformational change
    • Weitzman, C., Consler, T. G., and Kaback, H. R. (1995) Fluorescence of native single-Trp mutants in the lactose permease from Escherichia coli: Structural properties and evidence for a substrate-induced conformational change, Protein Sci. 4, 2310-2318.
    • (1995) Protein Sci. , vol.4 , pp. 2310-2318
    • Weitzman, C.1    Consler, T.G.2    Kaback, H.R.3
  • 42
    • 0029831348 scopus 로고    scopus 로고
    • Melibiose permease of Escherichia coli: Structural organization of cosubstrate binding sites as deduced from tryptophan fluorescence analyses
    • Mus-Veteau, I., and Leblanc, G. (1996) Melibiose permease of Escherichia coli: structural organization of cosubstrate binding sites as deduced from tryptophan fluorescence analyses. Biochemistry 35, 12053-12060.
    • (1996) Biochemistry , vol.35 , pp. 12053-12060
    • Mus-Veteau, I.1    Leblanc, G.2
  • 43
    • 2942511249 scopus 로고    scopus 로고
    • Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli
    • Ma, C., and Chang, G. (2004) Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 101, 2852-2857.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2852-2857
    • Ma, C.1    Chang, G.2


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