메뉴 건너뛰기




Volumn 48, Issue 41, 2009, Pages 9794-9800

Biochemical characterization of the multidrug regulator QacR distinguishes residues that are crucial to multidrug binding and induction of qacA transcription

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; BINDING POCKETS; BIOCHEMICAL CHARACTERIZATION; DE-REPRESSION; ETHIDIUM; HIGH AFFINITY; LIGAND BINDING; LIPOPHILIC COMPOUNDS; MULTIDRUG EFFLUX; POLAR RESIDUES; RHODAMINE 6G; S. AUREUS; STAPHYLOCOCCUS AUREUS; STRUCTURAL CHANGE; TRANSCRIPTIONALLY ACTIVE;

EID: 70350072949     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901102h     Document Type: Article
Times cited : (7)

References (47)
  • 1
    • 0029845047 scopus 로고    scopus 로고
    • Protondependent multidrug efflux systems
    • Paulsen, I. T., Brown, M. H., and Skurray, R. A. (1996) Protondependent 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
  • 2
    • 34147214716 scopus 로고    scopus 로고
    • Multiple molecular mechanisms for multidrug resistance transporters
    • DOI 10.1038/nature05630, PII NATURE05630
    • Higgins, C. F. (2007) Multiple molecular mechanisms for multidrug resistance transporters. Nature 446, 749-757. (Pubitemid 46582024)
    • (2007) Nature , vol.446 , Issue.7137 , pp. 749-757
    • Higgins, C.F.1
  • 3
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • DOI 10.1038/nature05076, PII NATURE05076
    • Murakami, S., Nakashima, R., Yamashita, E., Matsumoto, T., and Yamaguchi, A. (2006) Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443, 173-179. (Pubitemid 44387601)
    • (2006) Nature , vol.443 , Issue.7108 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 4
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J., and Locher, K. P. (2006) Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 6
    • 0035824388 scopus 로고    scopus 로고
    • Structural mechanisms of QacR induction and multidrug recognition
    • DOI 10.1126/science.1066020
    • Schumacher, M. A., Miller, M. C., Grkovic, S., Brown, M. H., Skurray, R. A., and Brennan, R. G. (2001) Structural mechanisms of QacR induction and multidrug recognition. Science 294, 2158-2163. (Pubitemid 33150671)
    • (2001) Science , vol.294 , Issue.5549 , pp. 2158-2163
    • Schumacher, M.A.1    Miller, M.C.2    Grkovic, S.3    Brown, M.H.4    Skurray, R.A.5    Brennan, R.G.6
  • 7
    • 4143103793 scopus 로고    scopus 로고
    • Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein
    • Schumacher, M. A., Miller, M. C., and Brennan, R. G. (2004) Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein. EMBO J. 23, 2923-2930.
    • (2004) EMBO J. , vol.23 , pp. 2923-2930
    • Schumacher, M.A.1    Miller, M.C.2    Brennan, R.G.3
  • 8
    • 1842740025 scopus 로고    scopus 로고
    • Crystal structures of QacR-diamidine complexes reveal additional multidrug-binding modes and a novel mechanism of drug charge neutralization
    • Murray, D. S., Schumacher, M. A., and Brennan, R. G. (2004) Crystal structures of QacR-diamidine complexes reveal additional multidrug-binding modes and a novel mechanism of drug charge neutralization. J. Biol. Chem. 279, 14365-14371.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14365-14371
    • Murray, D.S.1    Schumacher, M.A.2    Brennan, R.G.3
  • 9
    • 34447119668 scopus 로고    scopus 로고
    • Multidrugbinding transcription factor QacR binds the bivalent aromatic diamidines DB75 and DB359 in multiple positions
    • Brooks, B. E., Piro, K. M., and Brennan, R. G. (2007) Multidrugbinding transcription factor QacR binds the bivalent aromatic diamidines DB75 and DB359 in multiple positions. J. Am. Chem. Soc. 129, 8389-8395.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 8389-8395
    • Brooks, B.E.1    Piro, K.M.2    Brennan, R.G.3
  • 10
    • 55549108388 scopus 로고    scopus 로고
    • Structures of BmrR-drug complexes reveal a rigid multidrug binding pocket and transcription activation through tyrosine expulsion
    • Newberry, K. J., Huffman, J. L., Miller, M. C., Vazquez-Laslop, N., Neyfakh, A. A., and Brennan, R. G. (2008) Structures of BmrR-drug complexes reveal a rigid multidrug binding pocket and transcription activation through tyrosine expulsion. J. Biol. Chem. 283, 26795-26804.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26795-26804
    • Newberry, K.J.1    Huffman, J.L.2    Miller, M.C.3    Vazquez-Laslop, N.4    Neyfakh, A.A.5    Brennan, R.G.6
  • 11
    • 0035905808 scopus 로고    scopus 로고
    • Crystal structure of the transcription activator BmrR bound to DNA and a drug
    • DOI 10.1038/35053138
    • Heldwein, E. E., and Brennan, R. G. (2001) Crystal structure of the transcription activator BmrR bound to DNA and a drug. Nature 409, 378-382. (Pubitemid 32151247)
    • (2001) Nature , vol.409 , Issue.6818 , pp. 378-382
    • Zheleznova Heldwein, E.E.1    Brennan, R.G.2
  • 12
    • 0033525105 scopus 로고    scopus 로고
    • Structural basis of multidrug recognition by BmrR, a transcriptional 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 transcriptional 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
  • 13
    • 34248152648 scopus 로고    scopus 로고
    • Crystal structures of multidrug binding protein TtgR in complex with antibiotics and plant antimicrobials
    • Alguel, Y., Meng, C., Teran, W., Krell, T., Ramos, J. L., Gallegos, M. T., and Zhang, X. (2007) Crystal structures of multidrug binding protein TtgR in complex with antibiotics and plant antimicrobials. J. Mol. Biol. 369, 829-840.
    • (2007) J. Mol. Biol. , vol.369 , pp. 829-840
    • Alguel, Y.1    Meng, C.2    Teran, W.3    Krell, T.4    Ramos, J.L.5    Gallegos, M.T.6    Zhang, X.7
  • 14
    • 58749086713 scopus 로고    scopus 로고
    • Structure of the transcriptional regulator LmrR and its mechanism of multidrug recognition
    • Madoori, P. K., Agustiandari, H., Driessen, A. J., and Thunnissen, A. M. (2009) Structure of the transcriptional regulator LmrR and its mechanism of multidrug recognition. EMBO J. 28, 156-166.
    • (2009) EMBO J. , vol.28 , pp. 156-166
    • Madoori, P.K.1    Agustiandari, H.2    Driessen, A.J.3    Thunnissen, A.M.4
  • 17
    • 0025695158 scopus 로고
    • Efflux-mediated antiseptic resistance gene qacA from Staphylococcus aureus: Common ancestry with tetracycline- And sugar-transport proteins
    • Rouch, D. A., Cram, D. S., DiBerardino, D., Littlejohn, T. G., and Skurray, R. A. (1990) Efflux-mediated antiseptic resistance gene qacA from Staphylococcus aureus: Common ancestry with tetracycline- and sugar-transport proteins. Mol. Microbiol. 4, 2051-2062.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2051-2062
    • Rouch, D.A.1    Cram, D.S.2    DiBerardino, D.3    Littlejohn, T.G.4    Skurray, R.A.5
  • 18
    • 0035205399 scopus 로고    scopus 로고
    • The staphylococcal QacR multidrug regulator binds a correctly spaced operator as a pair of dimers
    • DOI 10.1128/JB.183.24.7102-7109.2001
    • Grkovic, S., Brown, M. H., Schumacher, M. A., Brennan, R. G., and Skurray, R. A. (2001) The staphylococcal QacR multidrug regulator binds a correctly spaced operator as a pair of dimers. J. Bacteriol. 183, 7102-7109. (Pubitemid 33121843)
    • (2001) Journal of Bacteriology , vol.183 , Issue.24 , pp. 7102-7109
    • Grkovic, S.1    Brown, M.H.2    Schumacher, M.A.3    Brennan, R.G.4    Skurray, R.A.5
  • 19
    • 0036500260 scopus 로고    scopus 로고
    • Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR
    • DOI 10.1093/emboj/21.5.1210
    • Schumacher, M. A., Miller, M. C., Grkovic, S., Brown, M. H., Skurray, R. A., and Brennan, R. G. (2002) Structural basis for cooperative DNA binding by two dimers of the multidrug binding protein QacR. EMBO J. 21, 1210-1218. (Pubitemid 34206194)
    • (2002) EMBO Journal , vol.21 , Issue.5 , pp. 1210-1218
    • Schumacher, M.A.1    Miller, M.C.2    Grkovic, S.3    Brown, M.H.4    Skurray, R.A.5    Brennan, R.G.6
  • 20
    • 48649104875 scopus 로고    scopus 로고
    • QacR-cation recognition is mediated by a redundancy of residues capable of charge neutralization
    • Peters, K. M., Schuman, J. T., Skurray, R. A., Brown, M. H., Brennan, R. G., and Schumacher, M. A. (2008) QacR-cation recognition is mediated by a redundancy of residues capable of charge neutralization. Biochemistry 47, 8122-8129.
    • (2008) Biochemistry , vol.47 , pp. 8122-8129
    • Peters, K.M.1    Schuman, J.T.2    Skurray, R.A.3    Brown, M.H.4    Brennan, R.G.5    Schumacher, M.A.6
  • 21
    • 0028097634 scopus 로고
    • Transmembrane aromatic amino acid distribution in P-glycoprotein: Afunctional role in broad substrate specificity
    • Pawagi, A. B., Wang, J., Silverman, M., Reithmeier, R. A. F., and Deber, C. M. (1994) Transmembrane aromatic amino acid distribution in P-glycoprotein:Afunctional role in broad substrate specificity. J. Mol. Biol. 235, 554-564.
    • (1994) J. Mol. Biol. , vol.235 , pp. 554-564
    • Pawagi, A.B.1    Wang, J.2    Silverman, M.3    Reithmeier, R.A.F.4    Deber, C.M.5
  • 22
    • 0027260959 scopus 로고
    • Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein
    • Loo, T. W., and Clarke, D. M. (1993) Functional consequences of phenylalanine mutations in the predicted transmembrane domain of P-glycoprotein. J. Biol. Chem. 268, 19965-19972.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19965-19972
    • Loo, T.W.1    Clarke, D.M.2
  • 23
    • 0033924206 scopus 로고    scopus 로고
    • Functional analysis of a tryptophan- Less P-glycoprotein:Atool for tryptophan insertion and fluorescence spectroscopy
    • Kwan, T., Loughrey, H., Brault, M., Gruenheid, S., Urbatsch, I. L., Senior, A. E., and Gros, P. (2000) Functional analysis of a tryptophan- less P-glycoprotein:Atool for tryptophan insertion and fluorescence spectroscopy. Mol. Pharmacol. 58, 37-47.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 37-47
    • Kwan, T.1    Loughrey, H.2    Brault, M.3    Gruenheid, S.4    Urbatsch, I.L.5    Senior, A.E.6    Gros, P.7
  • 24
    • 33745821170 scopus 로고    scopus 로고
    • Identification of tyrosine residues critical for the function of an ion-coupled multidrug transporter
    • Rotem, D., Steiner-Mordoch, S., and Schuldiner, S. (2006) Identification of tyrosine residues critical for the function of an ion-coupled multidrug transporter. J. Biol. Chem. 281, 18715-18722.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18715-18722
    • Rotem, D.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 26
    • 25444519556 scopus 로고    scopus 로고
    • Exploring the binding domain of EmrE, the smallest multidrug transporter
    • Sharoni, M., Steiner-Mordoch, S., and Schuldiner, S. (2005) Exploring the binding domain of EmrE, the smallest multidrug transporter. J. Biol. Chem. 280, 32849-32855.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32849-32855
    • Sharoni, M.1    Steiner-Mordoch, S.2    Schuldiner, S.3
  • 27
    • 18544374282 scopus 로고    scopus 로고
    • Substrate-induced tryptophan fluorescence changes in EmrE, the smallest ion-coupled multidrug transporter
    • DOI 10.1021/bi050356t
    • Elbaz, Y., Tayer, N., Steinfels, E., Steiner-Mordoch, S., and Schuldiner, S. (2005) Substrate-induced tryptophan fluorescence changes in EmrE, the smallest ion-coupled multidrug transporter. Biochemistry 44, 7369-7377. (Pubitemid 40656680)
    • (2005) Biochemistry , vol.44 , Issue.19 , pp. 7369-7377
    • Elbaz, Y.1    Tayer, N.2    Steinfels, E.3    Steiner-Mordoch, S.4    Schuldiner, S.5
  • 29
    • 33644861768 scopus 로고    scopus 로고
    • Role of transmembrane segment 10 in efflux mediated by the staphylococcal multidrug transport protein QacA
    • Xu, Z., O'Rourke, B. A., Skurray, R. A., and Brown, M. H. (2006) Role of transmembrane segment 10 in efflux mediated by the staphylococcal multidrug transport protein QacA. J. Biol. Chem. 281, 792-799.
    • (2006) J. Biol. Chem. , vol.281 , pp. 792-799
    • Xu, Z.1    O'Rourke, B.A.2    Skurray, R.A.3    Brown, M.H.4
  • 30
    • 41549133136 scopus 로고    scopus 로고
    • Analysis of tryptophan residues in the staphylococcal multidrug transporter QacA reveals long-distance functional associations of residues on opposite sides of the membrane
    • Hassan, K. A., Souhani, T., Skurray, R. A., and Brown, M. H. (2008) Analysis of tryptophan residues in the staphylococcal multidrug transporter QacA reveals long-distance functional associations of residues on opposite sides of the membrane. J. Bacteriol. 190, 2441-2449.
    • (2008) J. Bacteriol. , vol.190 , pp. 2441-2449
    • Hassan, K.A.1    Souhani, T.2    Skurray, R.A.3    Brown, M.H.4
  • 31
    • 6344235517 scopus 로고    scopus 로고
    • Structure of EthR in a ligand bound conformation reveals therapeutic perspectives against tuberculosis
    • DOI 10.1016/j.molcel.2004.09.020, PII S1097276504005751
    • Frénois, F., Engohang-Ndong, J., Locht, C., Baulard, A. R., and Villeret, V. (2004) Structure of EthR in a ligand bound conformation reveals therapeutic perspectives against tuberculosis. Mol. Cell 16, 301-307. (Pubitemid 39388844)
    • (2004) Molecular Cell , vol.16 , Issue.2 , pp. 301-307
    • Frenois, F.1    Engohang-Ndong, J.2    Locht, C.3    Baulard, A.R.4    Villeret, V.5
  • 32
    • 3242812945 scopus 로고    scopus 로고
    • Crystal structure of the TetR/ CamR family repressor Mycobacterium tuberculosis EthR implicated in ethionamide resistance
    • Dover, L. G., Corsino, P. E., Daniels, I. R., Cocklin, S. L., Tatituri, V., Besra, G. S., and Futterer, K. (2004) Crystal structure of the TetR/ CamR family repressor Mycobacterium tuberculosis EthR implicated in ethionamide resistance. J. Mol. Biol. 340, 1095-1105.
    • (2004) J. Mol. Biol. , vol.340 , pp. 1095-1105
    • Dover, L.G.1    Corsino, P.E.2    Daniels, I.R.3    Cocklin, S.L.4    Tatituri, V.5    Besra, G.S.6    Futterer, K.7
  • 33
    • 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
  • 34
    • 23944511098 scopus 로고    scopus 로고
    • Antibiotic resistance: Multidrug efflux proteins, a common transport mechanism?
    • Langton, K. P., Henderson, P. J., and Herbert, R. B. (2005) Antibiotic resistance: Multidrug efflux proteins, a common transport mechanism? Nat. Prod. Rep. 22, 439-451.
    • (2005) Nat. Prod. Rep. , vol.22 , pp. 439-451
    • Langton, K.P.1    Henderson, P.J.2    Herbert, R.B.3
  • 36
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson, R. J., and Locher, K. P. (2007) Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 581, 935-938.
    • (2007) FEBS Lett. , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 38
    • 0036710081 scopus 로고    scopus 로고
    • The multidrug efflux pump NorA is not required for salicylate-induced reduction in drug accumulation by Staphylococcus aureus
    • Price, C. T., Kaatz, G. W., and Gustafson, J. E. (2002) The multidrug efflux pump NorA is not required for salicylate-induced reduction in drug accumulation by Staphylococcus aureus. Int. J. Antimicrob. Agents 20, 206-213.
    • (2002) Int. J. Antimicrob. Agents , vol.20 , pp. 206-213
    • Price, C.T.1    Kaatz, G.W.2    Gustafson, J.E.3
  • 39
    • 0026891517 scopus 로고
    • Improved method for electroporation of Staphylococcus aureus
    • Schenk, S., and Laddaga, R. A. (1992) Improved method for electroporation of Staphylococcus aureus. FEMS Microbiol. Lett. 73, 133-138.
    • (1992) FEMS Microbiol. Lett. , vol.73 , pp. 133-138
    • Schenk, S.1    Laddaga, R.A.2
  • 40
    • 0020538080 scopus 로고
    • Analysis of plasmids in nosocomial strains of multiple-antibiotic- resistant Staphylococcus aureus
    • Lyon, B. R., May, J. W., and Skurray, R. A. (1983) Analysis of plasmids in nosocomial strains of multiple-antibiotic-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 23, 817-826.
    • (1983) Antimicrob. Agents Chemother. , vol.23 , pp. 817-826
    • Lyon, B.R.1    May, J.W.2    Skurray, R.A.3
  • 41
    • 0037348664 scopus 로고    scopus 로고
    • Stable low-copy-number Staphylococcus aureus shuttle vectors
    • DOI 10.1099/mic.0.25951-0
    • Grkovic, S., Brown, M. H., Hardie, K. M., Firth, N., and Skurray, R. A. (2003) Stable low-copy-number Staphylococcus aureus shuttle vectors. Microbiology 149, 785-794. (Pubitemid 36395112)
    • (2003) Microbiology , vol.149 , Issue.3 , pp. 785-794
    • Grkovic, S.1    Brown, M.H.2    Hardie, K.M.3    Firth, N.4    Skurray, R.A.5
  • 42
    • 0347594185 scopus 로고    scopus 로고
    • Interactions of the QacR Multidrug-Binding Protein with Structurally Diverse Ligands: Implications for the Evolution of the Binding Pocket
    • DOI 10.1021/bi035447+
    • Grkovic, S., Hardie, K. M., Brown, M. H., and Skurray, R. A. (2003) Interactions of the QacR multidrug-binding protein with structurally diverse ligands: Implications for the evolution of the binding pocket. Biochemistry 42, 15226-15236. (Pubitemid 38031722)
    • (2003) Biochemistry , vol.42 , Issue.51 , pp. 15226-15236
    • Grkovic, S.1    Hardie, K.M.2    Brown, M.H.3    Skurray, R.A.4
  • 43
    • 0025788344 scopus 로고
    • Regulation of the cadA cadmium resistance determinant of Staphylococcus aureus plasmid pI258
    • Yoon, K. P., Misra, T. K., and Silver, S. (1991) Regulation of the cadA cadmium resistance determinant of Staphylococcus aureus plasmid pI258. J. Bacteriol. 173, 7643-7649.
    • (1991) J. Bacteriol. , vol.173 , pp. 7643-7649
    • Yoon, K.P.1    Misra, T.K.2    Silver, S.3
  • 44
    • 0040436016 scopus 로고    scopus 로고
    • Mechanism of ligand recognition by BmrR, the multidrug-responding transcriptional regulator: Mutational analysis of the ligand-binding site
    • DOI 10.1021/bi991988g
    • Vázquez-Laslop, N., Markham, P. N., and Neyfakh, A. A. (1999) Mechanism of ligand recognition by BmrR, the multidrug-responding transcriptional regulator: Mutational analysis of the ligand-binding site. Biochemistry 38, 16925-16931. (Pubitemid 30013699)
    • (1999) Biochemistry , vol.38 , Issue.51 , pp. 16925-16931
    • Vazquez-Laslop, N.1    Markham, P.N.2    Neyfakh, A.A.3
  • 45
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P. Y., and Fasman, G. D. (1978) Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. 47, 45-148.
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.