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Volumn 459, Issue 1, 2015, Pages 148-153

Characterization of a novel domain 'GATE' in the ABC protein DrrA and its role in drug efflux by the DrrAB complex

Author keywords

ABC transporter; C terminal domain; Doxorubicin efflux; DrrAB; Drug resistance; Nucleotide binding domain

Indexed keywords

ABC TRANSPORTER DRRA; ABC TRANSPORTER DRRAB; ADENOSINE TRIPHOSPHATE; CARRIER PROTEINS AND BINDING PROTEINS; DOXORUBICIN; GLYCINE; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; ABC TRANSPORTER; BACTERIAL PROTEIN; DNA BINDING PROTEIN; DRRA PROTEIN, BACTERIA; DRRB PROTEIN, ESCHERICHIA COLI; ESCHERICHIA COLI PROTEIN; MALK PROTEIN, E COLI;

EID: 84930178436     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.02.086     Document Type: Article
Times cited : (10)

References (25)
  • 1
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • table of contents
    • A.L. Davidson, E. Dassa, C. Orelle, and J. Chen Structure, function, and evolution of bacterial ATP-binding cassette systems Microbiol. Mol. Biol. Rev. 72 2008 317 364 table of contents
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 2
    • 0346887115 scopus 로고    scopus 로고
    • Structure and function of efflux pumps that confer resistance to drugs
    • M.I. Borges-Walmsley, K.S. McKeegan, and A.R. Walmsley Structure and function of efflux pumps that confer resistance to drugs Biochem. J. 376 2003 313 338
    • (2003) Biochem. J. , vol.376 , pp. 313-338
    • Borges-Walmsley, M.I.1    McKeegan, K.S.2    Walmsley, A.R.3
  • 3
    • 0025999987 scopus 로고
    • A bacterial analog of the mdr gene of mammalian tumor cells is present in Streptomyces peucetius, the producer of daunorubicin and doxorubicin
    • P.G. Guilfoile, and C.R. Hutchinson A bacterial analog of the mdr gene of mammalian tumor cells is present in Streptomyces peucetius, the producer of daunorubicin and doxorubicin Proc. Natl. Acad. Sci. U. S. A. 88 1991 8553 8557
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 8553-8557
    • Guilfoile, P.G.1    Hutchinson, C.R.2
  • 5
    • 0032504152 scopus 로고    scopus 로고
    • Biochemical coupling between the DrrA and DrrB proteins of the doxorubicin efflux pump of Streptomyces peucetius
    • P. Kaur, and J. Russell Biochemical coupling between the DrrA and DrrB proteins of the doxorubicin efflux pump of Streptomyces peucetius J. Biol. Chem. 273 1998 17933 17939
    • (1998) J. Biol. Chem. , vol.273 , pp. 17933-17939
    • Kaur, P.1    Russell, J.2
  • 6
    • 58149110766 scopus 로고    scopus 로고
    • Translational coupling controls expression and function of the DrrAB drug efflux pump
    • P. Pradhan, W. Li, and P. Kaur Translational coupling controls expression and function of the DrrAB drug efflux pump J. Mol. Biol. 385 2009 831 842
    • (2009) J. Mol. Biol. , vol.385 , pp. 831-842
    • Pradhan, P.1    Li, W.2    Kaur, P.3
  • 7
    • 40149088319 scopus 로고    scopus 로고
    • The Q-Loop of DrrA is involved in producing the closed conformation of the nucleotide binding domains and in transduction of conformational changes between DrrA and DrrB
    • D.K. Rao, and P. Kaur The Q-Loop of DrrA is involved in producing the closed conformation of the nucleotide binding domains and in transduction of conformational changes between DrrA and DrrB Biochemistry 47 2008 3038 3050
    • (2008) Biochemistry , vol.47 , pp. 3038-3050
    • Rao, D.K.1    Kaur, P.2
  • 8
    • 0036342413 scopus 로고    scopus 로고
    • ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer
    • P.C. Smith, N. Karpowich, L. Millen, J.E. Moody, J. Rosen, P.J. Thomas, and J.F. Hunt ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer Mol. Cell. 10 2002 139 149
    • (2002) Mol. Cell. , vol.10 , pp. 139-149
    • Smith, P.C.1    Karpowich, N.2    Millen, L.3    Moody, J.E.4    Rosen, J.5    Thomas, P.J.6    Hunt, J.F.7
  • 9
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • J. Chen, G. Lu, J. Lin, A.L. Davidson, and F.A. Quiocho A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle Mol. Cell. 12 2003 651 661
    • (2003) Mol. Cell. , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 10
    • 47249110343 scopus 로고    scopus 로고
    • Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter
    • S. Gerber, M. Comellas-Bigler, B.A. Goetz, and K.P. Locher Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter Science 321 2008 246 250
    • (2008) Science , vol.321 , pp. 246-250
    • Gerber, S.1    Comellas-Bigler, M.2    Goetz, B.A.3    Locher, K.P.4
  • 11
    • 47249084799 scopus 로고    scopus 로고
    • The high-affinity E. Coli methionine ABC transporter: Structure and allosteric regulation
    • N.S. Kadaba, J.T. Kaiser, E. Johnson, A. Lee, and D.C. Rees The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation Science 321 2008 250 253
    • (2008) Science , vol.321 , pp. 250-253
    • Kadaba, N.S.1    Kaiser, J.T.2    Johnson, E.3    Lee, A.4    Rees, D.C.5
  • 12
    • 37649017952 scopus 로고    scopus 로고
    • Substrate binding by a bacterial ABC transporter involved in polysaccharide export
    • L. Cuthbertson, M.S. Kimber, and C. Whitfield Substrate binding by a bacterial ABC transporter involved in polysaccharide export Proc. Natl. Acad. Sci. U. S. A. 104 2007 19529 19534
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 19529-19534
    • Cuthbertson, L.1    Kimber, M.S.2    Whitfield, C.3
  • 13
    • 78649661564 scopus 로고    scopus 로고
    • The extreme C terminus of the ABC protein DrrA contains unique motifs involved in function and assembly of the DrrAB complex
    • H. Zhang, P. Pradhan, and P. Kaur The extreme C terminus of the ABC protein DrrA contains unique motifs involved in function and assembly of the DrrAB complex J. Biol. Chem. 285 2010 38324 38336
    • (2010) J. Biol. Chem. , vol.285 , pp. 38324-38336
    • Zhang, H.1    Pradhan, P.2    Kaur, P.3
  • 14
    • 0024307717 scopus 로고
    • Use of lacZ fusions to measure in vivo expression of the first three genes of the Escherichia coli unc operon
    • K.A. Solomon, D.K. Hsu, and W.S. Brusilow Use of lacZ fusions to measure in vivo expression of the first three genes of the Escherichia coli unc operon J. Bacteriol. 171 1989 3039 3045
    • (1989) J. Bacteriol. , vol.171 , pp. 3039-3045
    • Solomon, K.A.1    Hsu, D.K.2    Brusilow, W.S.3
  • 15
    • 0031024018 scopus 로고    scopus 로고
    • Expression and characterization of DrrA and DrrB proteins of Streptomyces peucetius in Escherichia coli: DrrA is an ATP binding protein
    • P. Kaur Expression and characterization of DrrA and DrrB proteins of Streptomyces peucetius in Escherichia coli: DrrA is an ATP binding protein J. Bacteriol. 179 1997 569 575
    • (1997) J. Bacteriol. , vol.179 , pp. 569-575
    • Kaur, P.1
  • 16
    • 84899722249 scopus 로고    scopus 로고
    • The DrrAB efflux system of Streptomyces peucetius is a multidrug transporter of broad substrate specificity
    • W. Li, M. Sharma, and P. Kaur The DrrAB efflux system of Streptomyces peucetius is a multidrug transporter of broad substrate specificity J. Biol. Chem. 289 2014 12633 12646
    • (2014) J. Biol. Chem. , vol.289 , pp. 12633-12646
    • Li, W.1    Sharma, M.2    Kaur, P.3
  • 17
    • 67349217364 scopus 로고    scopus 로고
    • Caspase-3 binds diverse P4 residues in peptides as revealed by crystallography and structural modeling
    • B. Fang, G. Fu, J. Agniswamy, R.W. Harrison, and I.T. Weber Caspase-3 binds diverse P4 residues in peptides as revealed by crystallography and structural modeling Apoptosis 14 2009 741 752
    • (2009) Apoptosis , vol.14 , pp. 741-752
    • Fang, B.1    Fu, G.2    Agniswamy, J.3    Harrison, R.W.4    Weber, I.T.5
  • 18
    • 53849142861 scopus 로고    scopus 로고
    • Structural basis for executioner caspase recognition of P5 position in substrates
    • G. Fu, A.A. Chumanevich, J. Agniswamy, B. Fang, R.W. Harrison, and I.T. Weber Structural basis for executioner caspase recognition of P5 position in substrates Apoptosis 13 2008 1291 1302
    • (2008) Apoptosis , vol.13 , pp. 1291-1302
    • Fu, G.1    Chumanevich, A.A.2    Agniswamy, J.3    Fang, B.4    Harrison, R.W.5    Weber, I.T.6
  • 20
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 22
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • R.J. Dawson, and K.P. Locher Structure of a bacterial multidrug ABC transporter Nature 443 2006 180 185
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 23
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • J. Zaitseva, S. Jenewein, T. Jumpertz, I.B. Holland, and L. Schmitt H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB EMBO J. 24 2005 1901 1910
    • (2005) EMBO J. , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 24
    • 19644374667 scopus 로고    scopus 로고
    • Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching
    • M.D. Coleman, R.B. Bass, R.S. Mehan, and J.J. Falke Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching Biochemistry 44 2005 7687 7695
    • (2005) Biochemistry , vol.44 , pp. 7687-7695
    • Coleman, M.D.1    Bass, R.B.2    Mehan, R.S.3    Falke, J.J.4
  • 25
    • 0035933843 scopus 로고    scopus 로고
    • Distinct functions of the ATP binding cassettes of transporters associated with antigen processing: A mutational analysis of Walker A and B sequences
    • L. Saveanu, S. Daniel, and P.M. van Endert Distinct functions of the ATP binding cassettes of transporters associated with antigen processing: a mutational analysis of Walker A and B sequences J. Biol. Chem. 276 2001 22107 22113
    • (2001) J. Biol. Chem. , vol.276 , pp. 22107-22113
    • Saveanu, L.1    Daniel, S.2    Van Endert, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.