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Volumn 49, Issue 21, 2010, Pages 4440-4449

The signaling interface of the yeast multidrug transporter Pdr5 adopts a Cis conformation, and there are functional overlap and equivalence of the deviant and canonical Q-loop residues

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ATP HYDROLYSIS; ATP-BINDING SITE; DRUG RESISTANCE; DRUG TRANSPORT; EFFLUX TRANSPORTER; GENETIC SCREENS; LOOP RESIDUES; MULTIDRUG TRANSPORTERS; POLYTOPIC PROTEINS; SIGNAL INTERFACE; SINGLE MUTATION; TRANS CONFIGURATION; WILD TYPES;

EID: 77952810407     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100394j     Document Type: Article
Times cited : (39)

References (27)
  • 1
    • 64649090980 scopus 로고    scopus 로고
    • Molecular basis of multidrug transport by ABC transporters
    • Seeger, M. A. and van Veen, H. W. (2009) Molecular basis of multidrug transport by ABC transporters Biochim. Biophys. Acta 1794, 725-737
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 725-737
    • Seeger, M.A.1    Van Veen, H.W.2
  • 2
    • 33748747880 scopus 로고    scopus 로고
    • Exploiting reaction intermediates of the ATPase reaction to elucidate the mechanism of transport by P-glycoprotein (ABCB1)
    • Sauna, Z. E., Nandigama, K., and Ambudkar, S. V. (2006) Exploiting reaction intermediates of the ATPase reaction to elucidate the mechanism of transport by P-glycoprotein (ABCB1) J. Biol. Chem. 281, 26501-26511
    • (2006) J. Biol. Chem. , vol.281 , pp. 26501-26511
    • Sauna, Z.E.1    Nandigama, K.2    Ambudkar, S.V.3
  • 3
    • 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
  • 4
    • 36849079744 scopus 로고    scopus 로고
    • Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein
    • Zolnerciks, J. K., Wooding, C, and Linton, K. J. (2007) Evidence for a Sav1866-like architecture for the human multidrug transporter P-glycoprotein FASEB J. 21, 3937-3948
    • (2007) FASEB J. , vol.21 , pp. 3937-3948
    • Zolnerciks, J.K.1    Wooding, C.2    Linton, K.J.3
  • 6
    • 58049197842 scopus 로고    scopus 로고
    • Mutations define cross-talk between the N-terminal nucleotide-binding domain and transmembrane helix-2 of the yeast multidrug transporter Pdr5
    • Sauna, Z. E., Bohn, S. S., Rutledge, R., Dougherty, M, P., Cronin, S., May, L., Xia, D., Ambudkar, S. V., and Golin, J. (2008) Mutations define cross-talk between the N-terminal nucleotide-binding domain and transmembrane helix-2 of the yeast multidrug transporter Pdr5 J. Biol. Chem. 283, 35010-35022
    • (2008) J. Biol. Chem. , vol.283 , pp. 35010-35022
    • Sauna, Z.E.1    Bohn, S.S.2    Rutledge, R.3    Dougherty, M.P.4    Cronin, S.5    May, L.6    Xia, D.7    Ambudkar, S.V.8    Golin, J.9
  • 7
    • 1842610700 scopus 로고    scopus 로고
    • The ABC transporter structure and mechanism: Perspectives on recent research
    • Jones, P. M. and George, A. M. (2004) The ABC transporter structure and mechanism: Perspectives on recent research Cell. Mol. Life Sci. 61, 682-699
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 682-699
    • Jones, P.M.1    George, A.M.2
  • 9
    • 0026602838 scopus 로고
    • Interaction of the yeast pleiotropic drug resistance genes PDR1 and PDR5
    • Meyers, S., Schauer, W., Balzi, E., Wagner, M., Goffeau, A., and Golin, J. (1992) Interaction of the yeast pleiotropic drug resistance genes PDR1 and PDR5 Curr. Genet. 21, 431-436
    • (1992) Curr. Genet. , vol.21 , pp. 431-436
    • Meyers, S.1    Schauer, W.2    Balzi, E.3    Wagner, M.4    Goffeau, A.5    Golin, J.6
  • 10
    • 0028082188 scopus 로고
    • PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1
    • Balzi, E., Wang, M, Leterme, S., Dyck, L. V., and Goffeau, A. (1994) PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1 J. Biol. Chem. 269, 2206-2214
    • (1994) J. Biol. Chem. , vol.269 , pp. 2206-2214
    • Balzi, E.1    Wang, M.2    Leterme, S.3    Dyck, L.V.4    Goffeau, A.5
  • 11
    • 36048941421 scopus 로고    scopus 로고
    • Complete inhibition of the Pdr5p multidrug efflux pump ATPase by its transport substrate clotrimazole suggests that GTP as well as ATP may be used as an energy source
    • Golin, J., Kon, Z. N., Wu, C. P., Martello, J., Hanson, L., Supernavage, S., Ambudkar, S. V., and Sauna, Z. E. (2007) Complete inhibition of the Pdr5p multidrug efflux pump ATPase by its transport substrate clotrimazole suggests that GTP as well as ATP may be used as an energy source Biochemistry 46, 13109-13119
    • (2007) Biochemistry , vol.46 , pp. 13109-13119
    • Golin, J.1    Kon, Z.N.2    Wu, C.P.3    Martello, J.4    Hanson, L.5    Supernavage, S.6    Ambudkar, S.V.7    Sauna, Z.E.8
  • 12
    • 44149122152 scopus 로고    scopus 로고
    • Pdr5-mediated multidrug resistance requires the CPY-vacuolar sorting protein Vps3: Are xenobiotic compounds routed from the vacuole to plasma membrane transporters for efflux?
    • Rutledge, R. M., Ghislain, M., Mullins, J. M., de Thozée, C. P., and Golin, J. (2008) Pdr5-mediated multidrug resistance requires the CPY-vacuolar sorting protein Vps3: Are xenobiotic compounds routed from the vacuole to plasma membrane transporters for efflux? Mol. Genet. Genomics 279, 573-583
    • (2008) Mol. Genet. Genomics , vol.279 , pp. 573-583
    • Rutledge, R.M.1    Ghislain, M.2    Mullins, J.M.3    De Thozée, C.P.4    Golin, J.5
  • 14
    • 0028100864 scopus 로고
    • Loss of function mutation in the yeast multiple drug resistance gene PDR5 causes a reduction in chloramphenicol efflux
    • Leonard, P. J., Rathod, P. K., and Golin, J. (1994) Loss of function mutation in the yeast multiple drug resistance gene PDR5 causes a reduction in chloramphenicol efflux Antimicrob. Agents Chemother. 38, 2492-2494
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2492-2494
    • Leonard, P.J.1    Rathod, P.K.2    Golin, J.3
  • 15
    • 0037458550 scopus 로고    scopus 로고
    • Studies with novel Pdr5p substrates demonstrate a strong size dependence for xenobiotic efflux
    • Golin, J., Ambudkar, S., Gottesman, M., Habib, A., Sczepanski, J., Ziccardi, W., and May, L. (2003) Studies with novel Pdr5p substrates demonstrate a strong size dependence for xenobiotic efflux J. Biol. Chem. 278, 5963-5969
    • (2003) J. Biol. Chem. , vol.278 , pp. 5963-5969
    • Golin, J.1    Ambudkar, S.2    Gottesman, M.3    Habib, A.4    Sczepanski, J.5    Ziccardi, W.6    May, L.7
  • 16
    • 27744528467 scopus 로고    scopus 로고
    • The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA
    • Dalmas, O., Orelle, C., Foucher, A. E., Geourjon, C., Crouzy, S., Pietro, A. D., and Jault, J. M. (2005) The Q-loop disengages from the first intracellular loop during the catalytic cycle of the multidrug ABC transporter BmrA J. Biol. Chem. 280, 36857-36864
    • (2005) J. Biol. Chem. , vol.280 , pp. 36857-36864
    • Dalmas, O.1    Orelle, C.2    Foucher, A.E.3    Geourjon, C.4    Crouzy, S.5    Pietro, A.D.6    Jault, J.M.7
  • 17
    • 0034601811 scopus 로고    scopus 로고
    • Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein
    • Urbatsch, I. L., Gimi, K., Wilke-Mounts, S., and Senior, A. E. (2000) Investigation of the role of glutamine-471 and glutamine-1114 in the two catalytic sites of P-glycoprotein Biochemistry 39, 11921-11927
    • (2000) Biochemistry , vol.39 , pp. 11921-11927
    • Urbatsch, I.L.1    Gimi, K.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 18
    • 52049084793 scopus 로고    scopus 로고
    • A novel catalytic mechanism for ATP hydrolysis employed by the N-terminal nucleotide-binding domain of Cdr1p, a multidrug ABC transporter of Candida albicans
    • Rai, V., Gaur, M., Kumar, A., Shukla, S., Komath, S. S., and Prasad, R. (2008) A novel catalytic mechanism for ATP hydrolysis employed by the N-terminal nucleotide-binding domain of Cdr1p, a multidrug ABC transporter of Candida albicans Biochim. Biophys. Acta 1778, 2143-2153
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2143-2153
    • Rai, V.1    Gaur, M.2    Kumar, A.3    Shukla, S.4    Komath, S.S.5    Prasad, R.6
  • 19
    • 42449109037 scopus 로고    scopus 로고
    • A mutation of the H-loop selectively affects rhodamine transport by the yeast multidrug ABC transporter Pdr5
    • Ernst, R., Kueppers, P., Klein, C. M., Schwarzmueller, T., Kuchler, K., and Schmitt, L. (2008) A mutation of the H-loop selectively affects rhodamine transport by the yeast multidrug ABC transporter Pdr5 Proc. Natl. Acad. Sci. U.S.A. 105, 5069-5074
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5069-5074
    • Ernst, R.1    Kueppers, P.2    Klein, C.M.3    Schwarzmueller, T.4    Kuchler, K.5    Schmitt, L.6
  • 20
    • 75149114141 scopus 로고    scopus 로고
    • Multidrug efflux pumps: Substrate selection in ATP-binding cassette multidrug efflux pumps - First come, first served
    • Ernst, R., Kueppers, P., Stindt, J., Kuchler, K., and Schmitt, L. (2010) Multidrug efflux pumps: Substrate selection in ATP-binding cassette multidrug efflux pumps - first come, first served FEBS J. 277, 540-549
    • (2010) FEBS J. , vol.277 , pp. 540-549
    • Ernst, R.1    Kueppers, P.2    Stindt, J.3    Kuchler, K.4    Schmitt, L.5
  • 21
    • 33947133660 scopus 로고    scopus 로고
    • The yeast Pdr5p multidrug transporter: How does it recognize so many substrates?
    • Golin, J., Ambudkar, S. V., and May, L. (2007) The yeast Pdr5p multidrug transporter: How does it recognize so many substrates? Biochem. Biophys. Res. Commun. 356, 1-5
    • (2007) Biochem. Biophys. Res. Commun. , vol.356 , pp. 1-5
    • Golin, J.1    Ambudkar, S.V.2    May, L.3
  • 22
    • 22244472651 scopus 로고    scopus 로고
    • The role of hydrogen bond acceptor groups in the interaction of substrates with Pdr5p, a major yeast drug transporter
    • Hanson, L., May, L., Tuma, P., Keeven, J., Mehl, P., Ferenz, M., Ambudkar, S. V., and Golin, J. (2005) The role of hydrogen bond acceptor groups in the interaction of substrates with Pdr5p, a major yeast drug transporter Biochemistry 44, 9703-9713
    • (2005) Biochemistry , vol.44 , pp. 9703-9713
    • Hanson, L.1    May, L.2    Tuma, P.3    Keeven, J.4    Mehl, P.5    Ferenz, M.6    Ambudkar, S.V.7    Golin, J.8
  • 23
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli ButCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., Lee, A. T., and Rees, D. C. (2002) The E. coli ButCD structure: A framework for ABC transporter architecture and mechanism Science 296, 1091-1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 24
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein, K., Frei, D. C., and Locher, K. P. (2007) Structure of an ABC transporter in complex with its binding protein Nature 446, 213-216
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 25
    • 0035831524 scopus 로고    scopus 로고
    • Walker A lysine mutations of Tap1 and Tap2 interfere with peptide translocation, but not peptide binding
    • Lapinski, P. E., Neubig, R., and Raghavan, M. (2001) Walker A lysine mutations of Tap1 and Tap2 interfere with peptide translocation, but not peptide binding J. Biol. Chem. 276, 7526-7533
    • (2001) J. Biol. Chem. , vol.276 , pp. 7526-7533
    • Lapinski, P.E.1    Neubig, R.2    Raghavan, M.3
  • 26
    • 0028352302 scopus 로고
    • Solubilization and characterization of the overexpressed PDR5 multidrug resistance nucleotide triphosphatase of yeast
    • Decottignies, A., Kolaczkowski, M., Balzi, E., and Goffeau, A. (1994) Solubilization and characterization of the overexpressed PDR5 multidrug resistance nucleotide triphosphatase of yeast J. Biol. Chem. 269, 12797-12803
    • (1994) J. Biol. Chem. , vol.269 , pp. 12797-12803
    • Decottignies, A.1    Kolaczkowski, M.2    Balzi, E.3    Goffeau, A.4
  • 27
    • 33745174833 scopus 로고    scopus 로고
    • The conserved tyrosine residues 401 and 1044 in the ATP sites of human P-glycoprotein are critical for ATP binding and hydrolysis: Evidence for a conserved subdomain, the A-loop in the ATP-binding cassette
    • Kim, I.-W., Peng, X.-H., Sauna, Z. E., FitzGerald, P. C., Xia, D., Muller, M., Nandigama, K., and Ambudkar, S. V. (2006) The conserved tyrosine residues 401 and 1044 in the ATP sites of human P-glycoprotein are critical for ATP binding and hydrolysis: Evidence for a conserved subdomain, the A-loop in the ATP-binding cassette Biochemistry 45, 7605-7616
    • (2006) Biochemistry , vol.45 , pp. 7605-7616
    • Kim, I.-W.1    Peng, X.-H.2    Sauna, Z.E.3    Fitzgerald, P.C.4    Xia, D.5    Muller, M.6    Nandigama, K.7    Ambudkar, S.V.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.