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Volumn 96, Issue 3, 1999, Pages 353-362

Structural basis of multidrug recognition by BMRR, a transcription activator of a multidrug transporter

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN P; REGULATOR PROTEIN; REGULATOR PROTEIN BMRR; TETRAPHENYLPHOSPHONIUM; UNCLASSIFIED DRUG;

EID: 0033525105     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80548-6     Document Type: Article
Times cited : (171)

References (50)
  • 1
    • 0028104421 scopus 로고
    • A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates
    • Ahmed, M., Borsch, C.M., Taylor, S.S., Vazques-Laslop, N., and Neyfakh, A.A. (1994). A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates. J. Biol. Chem. 269, 28506-28513.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28506-28513
    • Ahmed, M.1    Borsch, C.M.2    Taylor, S.S.3    Vazques-Laslop, N.4    Neyfakh, A.A.5
  • 2
    • 0028918916 scopus 로고
    • DNA-bend modulation in a repressor-to-activator switching mechanism
    • Ansari, A.Z., Bradner, J.E., and O'Halloran, T.V. (1995). DNA-bend modulation in a repressor-to-activator switching mechanism. Nature 374, 371-375.
    • (1995) Nature , vol.374 , pp. 371-375
    • Ansari, A.Z.1    Bradner, J.E.2    O'Halloran, T.V.3
  • 4
    • 0030767713 scopus 로고    scopus 로고
    • Free R value: Cross-validation in crystallography
    • Brünger, A.T. (1997). Free R value: cross-validation in crystallography. Methods Enzymol. 277B, 366-396.
    • (1997) Methods Enzymol. , vol.277 B , pp. 366-396
    • Brünger, A.T.1
  • 5
    • 0032496377 scopus 로고    scopus 로고
    • Crystal structure of apo-cellular retinoic acid-binding protein type II (R111M) suggests a mechanism of ligand entry
    • Chen, X., Tordova, M., Gilliland, G.L, Wang, L, Li Y., Yan, H., and Ji, X. (1998). Crystal structure of apo-cellular retinoic acid-binding protein type II (R111M) suggests a mechanism of ligand entry. J. Mol. Biol. 278, 641-653.
    • (1998) J. Mol. Biol. , vol.278 , pp. 641-653
    • Chen, X.1    Tordova, M.2    Gilliland, G.L.3    Wang, L.4    Li, Y.5    Yan, H.6    Ji, X.7
  • 7
    • 0030044420 scopus 로고    scopus 로고
    • Solution structure of the ETS domain from murine Ets-1: A winged helix-turn-helix DNA binding motif
    • Donaldson, L.W., Petersen, J.M., Graves, B.J., and Mclntosh, L.P. (1996). Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motif. EMBO J. 15, 125-134.
    • (1996) EMBO J. , vol.15 , pp. 125-134
    • Donaldson, L.W.1    Petersen, J.M.2    Graves, B.J.3    Mclntosh, L.P.4
  • 11
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • Flower, D.R. (1996). The lipocalin protein family: structure and function. Biochem. J. 378, 1-14.
    • (1996) Biochem. J. , vol.378 , pp. 1-14
    • Flower, D.R.1
  • 12
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for the processing and analysis of diffraction data from macromolecules
    • Furey, W., and Swaminathan, S. (1997). PHASES-95: a program package for the processing and analysis of diffraction data from macromolecules. Methods Enzymol. 277B, 590-620.
    • (1997) Methods Enzymol. , vol.277 B , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 13
    • 0029790760 scopus 로고    scopus 로고
    • SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form
    • Gaudu, P., and Weiss, B. (1996). SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc. Natl. Acad. Sci. USA 93, 10094-10098.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 14
    • 0031020837 scopus 로고    scopus 로고
    • Multidrug-resistant transport proteins in yeast: Complete inventory and phylogenetic characterization of yeast open reading frames with the major facilitator superfamily
    • Goffeau, A., Park, J., Paulsen, I.T., Jonniaux, J.L., Dinh, T., Mordant, P., and Saier, M.H. Jr. (1997). Multidrug-resistant transport proteins in yeast: complete inventory and phylogenetic characterization of yeast open reading frames with the major facilitator superfamily. Yeast 13, 43-54.
    • (1997) Yeast , vol.13 , pp. 43-54
    • Goffeau, A.1    Park, J.2    Paulsen, I.T.3    Jonniaux, J.L.4    Dinh, T.5    Mordant, P.6    Saier Jr., M.H.7
  • 15
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman, M.M., and Pastan, I. (1993). Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu. Rev. Biochem. 62, 385-427.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 16
    • 0032541162 scopus 로고    scopus 로고
    • QacR is a represser protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA
    • Grkovic, S., Brown, M.H., Roberts, N.J., Paulsen, I.T., and Skurray, R.A. (1998). QacR is a represser protein that regulates expression of the Staphylococcus aureus multidrug efflux pump QacA. J. Biol. Chem. 273, 18665-18673.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18665-18673
    • Grkovic, S.1    Brown, M.H.2    Roberts, N.J.3    Paulsen, I.T.4    Skurray, R.A.5
  • 17
    • 0030912902 scopus 로고    scopus 로고
    • Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator
    • Hidalgo, E., Ding, H., and Demple, B. (1997). Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator. TIBS 22, 207-210.
    • (1997) TIBS , vol.22 , pp. 207-210
    • Hidalgo, E.1    Ding, H.2    Demple, B.3
  • 18
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L, and Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 19
    • 0027251026 scopus 로고
    • Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans
    • Holmes, D.J., Caso, J.L., and Thompson, C.J. (1993). Autogenous transcriptional activation of a thiostrepton-induced gene in Streptomyces lividans. EMBO J. 12, 3183-3191.
    • (1993) EMBO J. , vol.12 , pp. 3183-3191
    • Holmes, D.J.1    Caso, J.L.2    Thompson, C.J.3
  • 20
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and Nicholls, A. (1995). Classical electrostatics in biology and chemistry. Science 268, 1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 21
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.Z., Zou, J.-Y., Cowan, S.W., and Kieldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.Z.1    Zou, J.-Y.2    Cowan, S.W.3    Kieldgaard, M.4
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • Kussie, P.H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A.J., and Pavletich, N.P. (1996). Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274, 948-953.
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Levine, A.J.6    Pavletich, N.P.7
  • 24
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Thornton, J.M.3
  • 26
    • 0022273106 scopus 로고
    • NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation
    • LeMaster, D.M., and Richards, P.M. (1985). NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteriation. Biochemistry 24, 7263-7268.
    • (1985) Biochemistry , vol.24 , pp. 7263-7268
    • Lemaster, D.M.1    Richards, P.M.2
  • 27
    • 0028999706 scopus 로고
    • EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB
    • Lomovskaya, O., Lewis, K., and Matin, A. (1995). EmrR is a negative regulator of the Escherichia coli multidrug resistance pump EmrAB. J. Bacteriol. 777, 2328-2334.
    • (1995) J. Bacteriol. , vol.777 , pp. 2328-2334
    • Lomovskaya, O.1    Lewis, K.2    Matin, A.3
  • 28
    • 0030023489 scopus 로고    scopus 로고
    • The local represser AcrR plays a modulating role in the regulation of acrAB genes of Escherichia coli by global stress signals
    • Ma, D., Alberti, C., Lynch, H., Nikaido, H., and Hearst, J.E. (1996). The local represser AcrR plays a modulating role in the regulation of acrAB genes of Escherichia coli by global stress signals. Mol. Microbiol. 19, 101-112.
    • (1996) Mol. Microbiol. , vol.19 , pp. 101-112
    • Ma, D.1    Alberti, C.2    Lynch, H.3    Nikaido, H.4    Hearst, J.E.5
  • 29
    • 33646314512 scopus 로고    scopus 로고
    • The drugbinding activity of the multidrug-responding transcriptional regulator BmrR resides in its C-terminal domain
    • Markham, P.M., Ahmed, M., and Neyfakh, A.A. (1996). The drugbinding activity of the multidrug-responding transcriptional regulator BmrR resides in its C-terminal domain. J. Bacteriol. 778,473-475.
    • (1996) J. Bacteriol. , vol.778 , pp. 473-475
    • Markham, P.M.1    Ahmed, M.2    Neyfakh, A.A.3
  • 30
    • 0031561388 scopus 로고    scopus 로고
    • Broad ligand specificity of the transcriptional regulator of the Bacillus subtilis multidrug transporter Bmr
    • Markham, P.M., LoGuidice, J., and Neyfakh, A.A. (1997). Broad ligand specificity of the transcriptional regulator of the Bacillus subtilis multidrug transporter Bmr. Biochem. Biophys. Res. Commun. 239, 269-272.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 269-272
    • Markham, P.M.1    Loguidice, J.2    Neyfakh, A.A.3
  • 32
    • 0029048413 scopus 로고
    • Structure of Bam HI endonuclease bound to DNA: Partial folding and unfolding on DNA binding
    • Newman, M., Strzelecka, T., Dorner, L.F., Schildkraut, I., and Aggarwal, A.K. (1995). Structure of Bam HI endonuclease bound to DNA: partial folding and unfolding on DNA binding. Science 269, 656-663.
    • (1995) Science , vol.269 , pp. 656-663
    • Newman, M.1    Strzelecka, T.2    Dorner, L.F.3    Schildkraut, I.4    Aggarwal, A.K.5
  • 33
    • 0025864903 scopus 로고
    • Efflux-mediated multidrug resistance in Bacillus subtilis: Similarities and dissimilarities with the mammalian system
    • Neyfakh, A.A., Bidnenko, V.E., and Chen, L.B. (1991). Efflux-mediated multidrug resistance in Bacillus subtilis: similarities and dissimilarities with the mammalian system. Proc. Natl. Acad. Sci. USA 88, 4781-4785.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4781-4785
    • Neyfakh, A.A.1    Bidnenko, V.E.2    Chen, L.B.3
  • 34
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Permeability barriers and active efflux
    • Nikaido, H. (1994). Prevention of drug access to bacterial targets: permeability barriers and active efflux. Science 264, 382-388.
    • (1994) Science , vol.264 , pp. 382-388
    • Nikaido, H.1
  • 35
    • 0025991706 scopus 로고
    • DNA-induced increase in the alpha-helical content of C/EBP and GCN4
    • O'Neil, K.T., Shuman, J.D., Ampe, C., and DeGrado, W.F. (1991). DNA-induced increase in the alpha-helical content of C/EBP and GCN4. Biochemistry 30, 9030-9034.
    • (1991) Biochemistry , vol.30 , pp. 9030-9034
    • O'Neil, K.T.1    Shuman, J.D.2    Ampe, C.3    Degrado, W.F.4
  • 36
    • 0029845047 scopus 로고    scopus 로고
    • Proton-dependent multidrug efflux systems
    • Paulsen, I.T., Brown, M.H., and Skurray, R.A. (1996). Proton-dependent multidrug efflux systems. Microbiol. Rev. 60, 575-608.
    • (1996) Microbiol. Rev. , vol.60 , pp. 575-608
    • Paulsen, I.T.1    Brown, M.H.2    Skurray, R.A.3
  • 37
    • 0028874393 scopus 로고
    • Modulation of transcription factor Ets-1 DNA binding: DNA-induced unfolding of an alpha helix
    • Petersen, J.M., Skalicky, J.J., Donaldson, L.W., Mclntosh, L.P., Alber, T., and Graves, B.J. (1995). Modulation of transcription factor Ets-1 DNA binding: DNA-induced unfolding of an alpha helix. Science 269, 1866-1869.
    • (1995) Science , vol.269 , pp. 1866-1869
    • Petersen, J.M.1    Skalicky, J.J.2    Donaldson, L.W.3    Mclntosh, L.P.4    Alber, T.5    Graves, B.J.6
  • 38
    • 0027244075 scopus 로고
    • Rat intestinal fatty acid binding protein. A model system for analyzing the forces that can bind fatty acids to proteins
    • Sacchettini, J.C., and Gordon, J.I. (1993). Rat intestinal fatty acid binding protein. A model system for analyzing the forces that can bind fatty acids to proteins. J. Biol. Chem. 268, 18399-18402.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18399-18402
    • Sacchettini, J.C.1    Gordon, J.I.2
  • 40
    • 0028810684 scopus 로고
    • Mechanism of corepressor-mediated specific DNA binding by the purine represser
    • Schumacher, M.A., Choi, K.Y., Lu, F., Zalkin, H., and Brennan, R.G. (1995). Mechanism of corepressor-mediated specific DNA binding by the purine represser. Cell 83, 147-155.
    • (1995) Cell , vol.83 , pp. 147-155
    • Schumacher, M.A.1    Choi, K.Y.2    Lu, F.3    Zalkin, H.4    Brennan, R.G.5
  • 41
    • 0031455482 scopus 로고    scopus 로고
    • The P-glycoprotein efflux pump: How does it transport drugs?
    • Sharom, F.J. (1997). The P-glycoprotein efflux pump: how does it transport drugs? J. Membr. Biol. 760, 161-175.
    • (1997) J. Membr. Biol. , vol.760 , pp. 161-175
    • Sharom, F.J.1
  • 42
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R.S., and Record, M.T., Jr. (1994). Coupling of local folding to site-specific binding of proteins to DNA. Science 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 43
    • 0029976830 scopus 로고    scopus 로고
    • Formation of the hinge helix in the lac represser is induced upon binding to the lac operator
    • Spronk, C.A.E.M., Slijper, M., van Boom, J.H., Kaptein, R., and Boelens, R. (1996). Formation of the hinge helix in the lac represser is induced upon binding to the lac operator. Nat. Struct. Biol. 11, 916-919.
    • (1996) Nat. Struct. Biol. , vol.11 , pp. 916-919
    • Spronk, C.A.E.M.1    Slijper, M.2    Van Boom, J.H.3    Kaptein, R.4    Boelens, R.5
  • 44
    • 0026734859 scopus 로고
    • Untwist and shout: A heavy metal-responsive transcriptional regulator
    • Summers, A.O. (1992). Untwist and shout: a heavy metal-responsive transcriptional regulator. J. Bacteriol. 774, 3097-3101.
    • (1992) J. Bacteriol. , vol.774 , pp. 3097-3101
    • Summers, A.O.1
  • 45
    • 0030757720 scopus 로고    scopus 로고
    • TNT refinement package
    • Tronrud, D.E. (1997). TNT refinement package. Methods Enzymol. 277B, 306-319.
    • (1997) Methods Enzymol. , vol.277 B , pp. 306-319
    • Tronrud, D.E.1
  • 46
    • 84913050729 scopus 로고
    • An efficient general-purpose least squares refinement program for macromolecular structures
    • Tronrud, D.E., TenEyck, L.F., and Matthews, B.W. (1987). An efficient general-purpose least squares refinement program for macromolecular structures. Acta Crystallogr. A43, 489-501.
    • (1987) Acta Crystallogr. , vol.A43 , pp. 489-501
    • Tronrud, D.E.1    TenEyck, L.F.2    Matthews, B.W.3
  • 47
    • 0030756675 scopus 로고    scopus 로고
    • Induced alpha helix in the VP16 activation domain upon binding to a human TAF
    • Uesugi, M., Nyanguile, O., Lu, H., Levine, A.J., and Verdine, G.L. (1997). Induced alpha helix in the VP16 activation domain upon binding to a human TAF. Science 277, 1310-1313.
    • (1997) Science , vol.277 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Lu, H.3    Levine, A.J.4    Verdine, G.L.5
  • 48
    • 0029061164 scopus 로고
    • Mercury199 NMR of the metal receptor site in MerR and its protein-DNA complex
    • Utschig, L.M., Bryson, J.W., and O'Halloran, T.V. (1995). Mercury199 NMR of the metal receptor site in MerR and its protein-DNA complex. Science 268, 380-385.
    • (1995) Science , vol.268 , pp. 380-385
    • Utschig, L.M.1    Bryson, J.W.2    O'Halloran, T.V.3
  • 49
    • 0000134034 scopus 로고
    • Strategy for data collection from protein crystals using a multiwire counter area detector diffractometer
    • Xuong, N.H., Nielsen, C., Hamlin, R., and Anderson, D.J. (1985). Strategy for data collection from protein crystals using a multiwire counter area detector diffractometer. J. Appl. Crystallogr. 18, 342-350.
    • (1985) J. Appl. Crystallogr. , vol.18 , pp. 342-350
    • Xuong, N.H.1    Nielsen, C.2    Hamlin, R.3    Anderson, D.J.4
  • 50
    • 0030671047 scopus 로고    scopus 로고
    • Preliminary structural studies on the multi-ligand-binding domain of the transcription activator, BmrR, from Bacillus subtilis
    • Zheleznova, E.E., Markham, P.M., Neyfakh, A.A., and Brennan, R.G. (1997). Preliminary structural studies on the multi-ligand-binding domain of the transcription activator, BmrR, from Bacillus subtilis. Protein Sei. 6, 2465-2468.
    • (1997) Protein Sei. , vol.6 , pp. 2465-2468
    • Zheleznova, E.E.1    Markham, P.M.2    Neyfakh, A.A.3    Brennan, R.G.4


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