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Volumn 123, Issue 1, 1998, Pages 16-23

Metalloid resistance mechanisms in prokaryotes

Author keywords

Antimony; Arsenic; Metalloregulation; Resistance; Transport

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTIMONY; ARSENIC; CYSTEINE; METAL; PROTEIN; THIOL;

EID: 0031891809     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021904     Document Type: Review
Times cited : (108)

References (63)
  • 1
    • 0028822932 scopus 로고
    • New mechanisms of drug resistance in parasitic protozoa
    • Borst, P. and Ouellette, M. (1995) New mechanisms of drug resistance in parasitic protozoa. Annu. Rev. Microbiol. 49, 427-460
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 427-460
    • Borst, P.1    Ouellette, M.2
  • 2
    • 0002751054 scopus 로고
    • Mechanisms of drug transport in prokaryotes and eukaryotes
    • (Georgopapadakou, N.H., ed.) Dekker, New York
    • Dey, S. and Rosen, B.P. (1995) Mechanisms of drug transport in prokaryotes and eukaryotes in Drug Transport in Antimicrobial and Anticancer Chemotherapy (Georgopapadakou, N.H., ed.) pp. 103-132, Dekker, New York
    • (1995) Drug Transport in Antimicrobial and Anticancer Chemotherapy , pp. 103-132
    • Dey, S.1    Rosen, B.P.2
  • 3
    • 0000952639 scopus 로고    scopus 로고
    • Bacterial resistance to heavy metals
    • Rosen, B.P. (1996) Bacterial resistance to heavy metals. J. Biol. Inorg. Chem. 1, 273-277
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 273-277
    • Rosen, B.P.1
  • 4
    • 0038735888 scopus 로고
    • Energetics of plasmid-mediated arsenate resistance in Escherichia coli
    • Mobley, H.L.T. and Rosen, B.P. (1982) Energetics of plasmid-mediated arsenate resistance in Escherichia coli. Proc. Natl. Acad. Sci. USA 79, 6119-6122
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6119-6122
    • Mobley, H.L.T.1    Rosen, B.P.2
  • 6
    • 0020645470 scopus 로고
    • Conjugative plasmids in bacteria of the 'pre-antibiotic' era
    • Hughes, V.M. and Datta, N. (1983) Conjugative plasmids in bacteria of the 'pre-antibiotic' era. Nature 302, 725-726
    • (1983) Nature , vol.302 , pp. 725-726
    • Hughes, V.M.1    Datta, N.2
  • 7
    • 0040443698 scopus 로고
    • Antimicrobial activities of mineral elements
    • (Weinberg, E.D., ed.) Microbiology series, Marcel Dekker, New York
    • Foye, W.O. (1977) Antimicrobial activities of mineral elements in Microorganisms and Minerals (Weinberg, E.D., ed.) Microbiology series, Vol. 3, p. 387, Marcel Dekker, New York
    • (1977) Microorganisms and Minerals , vol.3 , pp. 387
    • Foye, W.O.1
  • 9
    • 0014275882 scopus 로고
    • Plasmid-linked resistance to inorganic salts in Staphylococcus aureus
    • Novick, R.P. and Roth, C. (1968) Plasmid-linked resistance to inorganic salts in Staphylococcus aureus. J. Bacteriol. 95, 1335-1342
    • (1968) J. Bacteriol. , vol.95 , pp. 1335-1342
    • Novick, R.P.1    Roth, C.2
  • 10
    • 0030574276 scopus 로고    scopus 로고
    • Bacterial resistances to toxic metal ions
    • Silver, S. (1996) Bacterial resistances to toxic metal ions. Gene 179, 9-19
    • (1996) Gene , vol.179 , pp. 9-19
    • Silver, S.1
  • 11
    • 0026558957 scopus 로고
    • Plasmid-encoded resistance to arsenic and antimony
    • Kaur, P. and Rosen, B.P. (1992) Plasmid-encoded resistance to arsenic and antimony. Plasmid 27, 29-40
    • (1992) Plasmid , vol.27 , pp. 29-40
    • Kaur, P.1    Rosen, B.P.2
  • 12
    • 0026747877 scopus 로고
    • Regulation and expression of the arsenic resistance operon from Staphylococcus aureus plasmid pI258
    • Ji, G. and Silver, S. (1992) Regulation and expression of the arsenic resistance operon from Staphylococcus aureus plasmid pI258. J. Bacteriol. 174, 3684-3694
    • (1992) J. Bacteriol. , vol.174 , pp. 3684-3694
    • Ji, G.1    Silver, S.2
  • 13
    • 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. 174, 3097-3101
    • (1992) J. Bacteriol. , vol.174 , pp. 3097-3101
    • Summers, A.O.1
  • 14
    • 0028837094 scopus 로고
    • The ars operon of Escherichia coli confers arsenical and antimonical resistance
    • Carlin, A., Shi, W., Dey, S., and Rosen, B.P. (1995) The ars operon of Escherichia coli confers arsenical and antimonical resistance. J. Bacteriol. 177, 981-986
    • (1995) J. Bacteriol. , vol.177 , pp. 981-986
    • Carlin, A.1    Shi, W.2    Dey, S.3    Rosen, B.P.4
  • 15
    • 0025061168 scopus 로고
    • Identification of the metalloregulatory element of the plasmid-encoded arsenical resistance operon
    • San Francisco, M.J.D., Hope, C.L., Owolabi, J.B., Tisa, L.S., and Rosen, B.P. (1990) Identification of the metalloregulatory element of the plasmid-encoded arsenical resistance operon. Nucleic Acids Res. 18, 619-624
    • (1990) Nucleic Acids Res. , vol.18 , pp. 619-624
    • San Francisco, M.J.D.1    Hope, C.L.2    Owolabi, J.B.3    Tisa, L.S.4    Rosen, B.P.5
  • 16
    • 0027273934 scopus 로고
    • The arsD gene encodes a second trans-acting regulatory protein of the plasmid-encoded arsenical resistance operon
    • Wu, J.H. and Rosen, B.P. (1993) The arsD gene encodes a second trans-acting regulatory protein of the plasmid-encoded arsenical resistance operon. Mol. Microbiol. 8, 615-623
    • (1993) Mol. Microbiol. , vol.8 , pp. 615-623
    • Wu, J.H.1    Rosen, B.P.2
  • 17
    • 0028116110 scopus 로고
    • ATP-dependent transport in everted membrane vesicles of Escherichia coli
    • Dey, S., Dou, D., and Rosen, B.P. (1994) ATP-dependent transport in everted membrane vesicles of Escherichia coli. J. Biol. Chem. 269, 25442-25446
    • (1994) J. Biol. Chem. , vol.269 , pp. 25442-25446
    • Dey, S.1    Dou, D.2    Rosen, B.P.3
  • 18
    • 0028306097 scopus 로고
    • Arsenate reduction mediated by the plasmid-encoded ArsC protein is coupled to glutathione
    • Oden, K.L., Gladysheva, T.B., and Rosen, B.P. (1994) Arsenate reduction mediated by the plasmid-encoded ArsC protein is coupled to glutathione. Mol. Microbiol. 12, 301-306
    • (1994) Mol. Microbiol. , vol.12 , pp. 301-306
    • Oden, K.L.1    Gladysheva, T.B.2    Rosen, B.P.3
  • 19
    • 0028289612 scopus 로고
    • Properties of the arsenate reductase of plasmid R77
    • Gladysheva, T.B., Oden, K.L., and Rosen, B.P. (1994) Properties of the arsenate reductase of plasmid R77. Biochemistry 33, 7287-7293
    • (1994) Biochemistry , vol.33 , pp. 7287-7293
    • Gladysheva, T.B.1    Oden, K.L.2    Rosen, B.P.3
  • 20
    • 0019826592 scopus 로고
    • Inducible plasmid-determined resistance to arsenate, arsenite, and antimony (III) in Escherichia coli and Staphylococeus aureus
    • Silver, S., Budd, K., Leahy, K.M., Shaw, W.V., Hammond, D., Novick, R.P., Willsky, G.R., Malamy, M.H., and Rosenberg, H. (1981) Inducible plasmid-determined resistance to arsenate, arsenite, and antimony (III) in Escherichia coli and Staphylococeus aureus. J. Bacteriol. 146, 983-996
    • (1981) J. Bacteriol. , vol.146 , pp. 983-996
    • Silver, S.1    Budd, K.2    Leahy, K.M.3    Shaw, W.V.4    Hammond, D.5    Novick, R.P.6    Willsky, G.R.7    Malamy, M.H.8    Rosenberg, H.9
  • 21
    • 0020529571 scopus 로고
    • DNA homology between the arsenate resistance plasmid pSX267 from Staphylococcus xylosus and the penicillinase plasmid pI258 from Staphylococcus aureus
    • Gotz, F., Zabielski, J., Philipson, L., and Lindberg, M. (1983) DNA homology between the arsenate resistance plasmid pSX267 from Staphylococcus xylosus and the penicillinase plasmid pI258 from Staphylococcus aureus. Plasmid 9, 126-137
    • (1983) Plasmid , vol.9 , pp. 126-137
    • Gotz, F.1    Zabielski, J.2    Philipson, L.3    Lindberg, M.4
  • 22
    • 0025815528 scopus 로고
    • The ArsR protein is a trans-acting regulatory protein
    • Wu, J. and Rosen, B.P. (1991) The ArsR protein is a trans-acting regulatory protein. Mol. Microbiol. 5, 1331-1336
    • (1991) Mol. Microbiol. , vol.5 , pp. 1331-1336
    • Wu, J.1    Rosen, B.P.2
  • 23
    • 0026642193 scopus 로고
    • Expression and regulation of the antimonite, arsenite, and arsenate resistance operon of Staphylococcus xylosus plasmid pSX267
    • Rosenstein, R., Peschel, A., Wieland, B., and Gotz, F. (1992) Expression and regulation of the antimonite, arsenite, and arsenate resistance operon of Staphylococcus xylosus plasmid pSX267. J. Bacteriol. 174, 3676-3683
    • (1992) J. Bacteriol. , vol.174 , pp. 3676-3683
    • Rosenstein, R.1    Peschel, A.2    Wieland, B.3    Gotz, F.4
  • 24
    • 0027535743 scopus 로고
    • Metalloregulated expression of the ars operon
    • Wu, J. and Rosen, B.P. (1993) Metalloregulated expression of the ars operon. J. Biol. Chem. 268, 52-58
    • (1993) J. Biol. Chem. , vol.268 , pp. 52-58
    • Wu, J.1    Rosen, B.P.2
  • 25
    • 0028027443 scopus 로고
    • Identification of a putative metal binding site in a new family of metalloregulatory proteins
    • Shi, W.P., Wu, J.H., and Rosen, B.P. (1994) Identification of a putative metal binding site in a new family of metalloregulatory proteins. J. Biol. Chem. 269, 19826-19829
    • (1994) J. Biol. Chem. , vol.269 , pp. 19826-19829
    • Shi, W.P.1    Wu, J.H.2    Rosen, B.P.3
  • 26
    • 0025836810 scopus 로고
    • A second gene in the Staphylococcus aureus cadA cadmium resistance determinant of plasmid pI258
    • Yoon, K.P. and Silver, S. (1991) A second gene in the Staphylococcus aureus cadA cadmium resistance determinant of plasmid pI258. J. Bacteriol. 173, 7636-7642
    • (1991) J. Bacteriol. , vol.173 , pp. 7636-7642
    • Yoon, K.P.1    Silver, S.2
  • 27
    • 0027247583 scopus 로고
    • SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: Identification of a Zn inhibited DNA-protein complex
    • Morby, A.P., Turner, J.S., Huckle, J.W., and Robinson, N.J. (1993) SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucleic Acids Res. 21, 921-925
    • (1993) Nucleic Acids Res. , vol.21 , pp. 921-925
    • Morby, A.P.1    Turner, J.S.2    Huckle, J.W.3    Robinson, N.J.4
  • 28
    • 0029873177 scopus 로고    scopus 로고
    • The role of arsenic-thiol interaction in metalloregulation of the ars operon
    • Shi, W.P., Dong, J., Scott, R.A., and Rosen, B.P. (1996) The role of arsenic-thiol interaction in metalloregulation of the ars operon. J. Biol. Chem. 271, 9291-9297
    • (1996) J. Biol. Chem. , vol.271 , pp. 9291-9297
    • Shi, W.P.1    Dong, J.2    Scott, R.A.3    Rosen, B.P.4
  • 29
    • 0031007219 scopus 로고    scopus 로고
    • Dimerization is essential for DNA binding and repression by the ArsR metalloregulatory protein of Escherichia coli
    • Xu, C. and Rosen, B.P. (1997) Dimerization is essential for DNA binding and repression by the ArsR metalloregulatory protein of Escherichia coli. J. Biol. Chem. 272, 15734-15738
    • (1997) J. Biol. Chem. , vol.272 , pp. 15734-15738
    • Xu, C.1    Rosen, B.P.2
  • 30
    • 0030917793 scopus 로고    scopus 로고
    • Metalloregulatory properties of the ArsD repressor
    • Chen, Y. and Rosen, B.P. (1997) Metalloregulatory properties of the ArsD repressor. J. Biol. Chem. 272, 14257-14262
    • (1997) J. Biol. Chem. , vol.272 , pp. 14257-14262
    • Chen, Y.1    Rosen, B.P.2
  • 31
    • 0026622930 scopus 로고
    • Membrane topology of the ArsB protein, the membrane subunit of an anion-translocating ATPase
    • Wu, J.H., Tisa, L.S., and Rosen, B.P. (1992) Membrane topology of the ArsB protein, the membrane subunit of an anion-translocating ATPase. J. Biol. Chem. 267, 12570-12576
    • (1992) J. Biol. Chem. , vol.267 , pp. 12570-12576
    • Wu, J.H.1    Tisa, L.S.2    Rosen, B.P.3
  • 32
    • 0001476958 scopus 로고
    • Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene results from a cadmium efflux ATPase
    • Nucifora, G., Chu, L., Misra, T.K., and Silver, S. (1989) Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene results from a cadmium efflux ATPase. Proc. Natl. Acad. Sci. USA 86, 3544-3548
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3544-3548
    • Nucifora, G.1    Chu, L.2    Misra, T.K.3    Silver, S.4
  • 33
    • 0029128733 scopus 로고
    • CadC, the transcriptional regulatory protein of the cadmium resistance system of Staphylococcus aureus plasmid pI258
    • Endo, G. and Silver, S. (1995) CadC, the transcriptional regulatory protein of the cadmium resistance system of Staphylococcus aureus plasmid pI258. J. Bacteriol. 177, 4437-4441
    • (1995) J. Bacteriol. , vol.177 , pp. 4437-4441
    • Endo, G.1    Silver, S.2
  • 34
    • 0029069508 scopus 로고
    • Metalloregulation of the cyanobacterial smt locus: Identification of SmtB binding sites and direct interaction with metals
    • Erbe, J.L., Taylor, K.B., and Hall, L.M. (1995) Metalloregulation of the cyanobacterial smt locus: identification of SmtB binding sites and direct interaction with metals. Nucleic Acids Res. 23, 2472-2478
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2472-2478
    • Erbe, J.L.1    Taylor, K.B.2    Hall, L.M.3
  • 35
    • 0029662326 scopus 로고    scopus 로고
    • 2+-sensing by the cyanobacterial metallothionein repressor SmtB: Different motifs mediate metal-induced protein-DNA dissociation
    • 2+-sensing by the cyanobacterial metallothionein repressor SmtB: different motifs mediate metal-induced protein-DNA dissociation. Nucleic Acids Res. 24, 3714-3721
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3714-3721
    • Turner, J.S.1    Glands, P.D.2    Samson, A.C.3    Robinson, N.J.4
  • 36
    • 0023038352 scopus 로고
    • Nucleotide sequence of the structural genes for an anion pump. The plasmid-encoded arsenical resistance operon
    • Chen, C.M., Misra, T.K., Silver, S., and Rosen, B.P. (1986) Nucleotide sequence of the structural genes for an anion pump. The plasmid-encoded arsenical resistance operon. J. Biol. Chem. 261, 15030-15038
    • (1986) J. Biol. Chem. , vol.261 , pp. 15030-15038
    • Chen, C.M.1    Misra, T.K.2    Silver, S.3    Rosen, B.P.4
  • 37
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of the ATP synthase, myosin kinase and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J., and Gay, N.J. (1982) Distantly related sequences in the α-and β-subunits of the ATP synthase, myosin kinase and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 38
    • 0023834869 scopus 로고
    • Molecular characterization of an anion pump. The arsA gene product is an arsenite(antimonate)-stimulated ATPase
    • Rosen, B.P., Weigel, U., Karkaria, C., and Gangola, P. (1988) Molecular characterization of an anion pump. The arsA gene product is an arsenite(antimonate)-stimulated ATPase. J. Biol. Chem. 263, 3067-3070
    • (1988) J. Biol. Chem. , vol.263 , pp. 3067-3070
    • Rosen, B.P.1    Weigel, U.2    Karkaria, C.3    Gangola, P.4
  • 39
    • 0025321162 scopus 로고
    • Mutagenesis of a nucleotide-binding site of an anion-translocating ATPase
    • Karkaria, C.E., Chen, C.M., and Rosen, B.P. (1990) Mutagenesis of a nucleotide-binding site of an anion-translocating ATPase. J. Biol. Chem. 265, 7832-7836
    • (1990) J. Biol. Chem. , vol.265 , pp. 7832-7836
    • Karkaria, C.E.1    Chen, C.M.2    Rosen, B.P.3
  • 40
    • 0026726796 scopus 로고
    • Mutagenesis of the C-terminal nucleotide-binding site of an anion-translocating ATPase
    • Kaur, P. and Rosen, B.P. (1992) Mutagenesis of the C-terminal nucleotide-binding site of an anion-translocating ATPase. J. Biol. Chem. 267, 19272-19277
    • (1992) J. Biol. Chem. , vol.267 , pp. 19272-19277
    • Kaur, P.1    Rosen, B.P.2
  • 41
    • 0025784605 scopus 로고
    • Trinitrophenyl-ATP binding to the ArsA protein: The catalytic subunit of an anion pump
    • Karkaria, C.E. and Rosen, B.P. (1991) Trinitrophenyl-ATP binding to the ArsA protein: the catalytic subunit of an anion pump. Arch. Biochem. Biophys. 288, 107-111
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 107-111
    • Karkaria, C.E.1    Rosen, B.P.2
  • 42
    • 0028178498 scopus 로고
    • 32P]ATP adduct formation in the ArsA protein
    • 32P]ATP adduct formation in the ArsA protein. Biochemistry 33, 6456-6461
    • (1994) Biochemistry , vol.33 , pp. 6456-6461
    • Kaur, P.1    Rosen, B.P.2
  • 43
    • 0027518522 scopus 로고
    • Complementation between nucleotide binding domains in an anion-translocating ATPase
    • Kaur, P. and Rosen, B.P. (1993) Complementation between nucleotide binding domains in an anion-translocating ATPase. J. Bacteriol. 175, 351-357
    • (1993) J. Bacteriol. , vol.175 , pp. 351-357
    • Kaur, P.1    Rosen, B.P.2
  • 44
    • 0028225995 scopus 로고
    • In vitro assembly of an anion-stimulated ATPase from peptide fragments
    • Kaur, P. and Rosen, B.P. (1994) In vitro assembly of an anion-stimulated ATPase from peptide fragments. J. Biol. Chem. 269, 9698-9704
    • (1994) J. Biol. Chem. , vol.269 , pp. 9698-9704
    • Kaur, P.1    Rosen, B.P.2
  • 45
    • 0029817926 scopus 로고    scopus 로고
    • Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump
    • Li, J., Liu, S., and Rosen, B.P. (1996) Interaction of ATP binding sites in the ArsA ATPase, the catalytic subunit of the Ars pump. J. Biol. Chem. 271, 25247-25252
    • (1996) J. Biol. Chem. , vol.271 , pp. 25247-25252
    • Li, J.1    Liu, S.2    Rosen, B.P.3
  • 46
    • 0025850512 scopus 로고
    • Substrate-induced dimerization of the ArsA protein, the catalytic component of an anion-translocating ATPase
    • Hsu, C.M., Kaur, P., Karkaria, C.E., Steiner, R.F., and Rosen, B.P. (1991) Substrate-induced dimerization of the ArsA protein, the catalytic component of an anion-translocating ATPase. J. Biol. Chem. 266, 2327-2332
    • (1991) J. Biol. Chem. , vol.266 , pp. 2327-2332
    • Hsu, C.M.1    Kaur, P.2    Karkaria, C.E.3    Steiner, R.F.4    Rosen, B.P.5
  • 48
    • 0027754119 scopus 로고
    • Reaction of the ArsA adenosinetriphosphatase with 2-(4′-maleimidoanilino)naphthalene-6-sulfonic acid
    • Ksenzenko, M.Y., Kessel, D.H., and Rosen, B.P. (1993) Reaction of the ArsA adenosinetriphosphatase with 2-(4′-maleimidoanilino)naphthalene-6-sulfonic acid. Biochemistry 32, 13362-13368
    • (1993) Biochemistry , vol.32 , pp. 13362-13368
    • Ksenzenko, M.Y.1    Kessel, D.H.2    Rosen, B.P.3
  • 49
    • 0029011877 scopus 로고
    • Role of cysteinyl residues in metalloactivation of the oxyanion-translocating ArsA ATPase
    • Bhattacharjee, H., Li, J., Ksenzenko, M.Y., and Rosen, B.P. (1995) Role of cysteinyl residues in metalloactivation of the oxyanion-translocating ArsA ATPase. J. Biol. Chem. 270, 11245-11250
    • (1995) J. Biol. Chem. , vol.270 , pp. 11245-11250
    • Bhattacharjee, H.1    Li, J.2    Ksenzenko, M.Y.3    Rosen, B.P.4
  • 50
    • 0029661442 scopus 로고    scopus 로고
    • Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase
    • Bhattacharjee, H. and Rosen, B.P. (1996) Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase. J. Biol. Chem. 271, 24465-24470
    • (1996) J. Biol. Chem. , vol.271 , pp. 24465-24470
    • Bhattacharjee, H.1    Rosen, B.P.2
  • 51
    • 0028864531 scopus 로고
    • Interaction of substrate and effector binding sites in the ArsA ATPase
    • Zhou, T., Liu, S., and Rosen, B.P. (1995) Interaction of substrate and effector binding sites in the ArsA ATPase. Biochemistry 34, 13622-13626
    • (1995) Biochemistry , vol.34 , pp. 13622-13626
    • Zhou, T.1    Liu, S.2    Rosen, B.P.3
  • 52
    • 0030795417 scopus 로고    scopus 로고
    • Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase
    • Zhou, T. and Rosen, B.P. (1997) Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase. J. Biol. Chem. 272, 19731-19737
    • (1997) J. Biol. Chem. , vol.272 , pp. 19731-19737
    • Zhou, T.1    Rosen, B.P.2
  • 53
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis, M.M., Komiya, H., Chakrabarti, P., Woo, D., Kornuc, J. J., and Rees, D.C. (1992) Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 257, 1653-1658
    • (1992) Science , vol.257 , pp. 1653-1658
    • Georgiadis, M.M.1    Komiya, H.2    Chakrabarti, P.3    Woo, D.4    Kornuc, J.J.5    Rees, D.C.6
  • 54
    • 0029915376 scopus 로고    scopus 로고
    • Elucidation of a MgATP signal pathway in the nitrogenase iron protein: Formation of a conformation resembling the MgATP-bound state by protein engineering
    • Ryle, M.J. and Seefeldt, L.C. (1996) Elucidation of a MgATP signal pathway in the nitrogenase iron protein: Formation of a conformation resembling the MgATP-bound state by protein engineering. Biochemistry 35, 4766-4775
    • (1996) Biochemistry , vol.35 , pp. 4766-4775
    • Ryle, M.J.1    Seefeldt, L.C.2
  • 55
    • 0029958571 scopus 로고    scopus 로고
    • The GTP binding motif: Variations on a theme
    • Kjeldgaard, M., Nyborg, J., and Clark, B.F.C. (1996) The GTP binding motif: variations on a theme. FASEB J. 10, 1347-1368
    • (1996) FASEB J. , vol.10 , pp. 1347-1368
    • Kjeldgaard, M.1    Nyborg, J.2    Clark, B.F.C.3
  • 56
    • 0025186765 scopus 로고
    • Molecular characterization of an anion pump: The ArsB protein is the membrane anchor for the ArsA protein
    • Tisa, L.S. and Rosen, B.P. (1990) Molecular characterization of an anion pump: the ArsB protein is the membrane anchor for the ArsA protein. J. Biol. Chem. 265, 190-194
    • (1990) J. Biol. Chem. , vol.265 , pp. 190-194
    • Tisa, L.S.1    Rosen, B.P.2
  • 57
    • 0028309454 scopus 로고
    • Interaction between the catalytic and the membrane components of an anion-translocating ATPase
    • Dey, S., Dou, D., Tisa, L.S., and Rosen, B.P. (1994) Interaction between the catalytic and the membrane components of an anion-translocating ATPase. Arch. Biochem. Biophys. 311, 418-424
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 418-424
    • Dey, S.1    Dou, D.2    Tisa, L.S.3    Rosen, B.P.4
  • 58
    • 0038735888 scopus 로고
    • Energetics of plasmid-mediated arsenate resistance in Escherichia coli
    • Mobley, H.L.T. and Rosen, B.P. (1982) Energetics of plasmid-mediated arsenate resistance in Escherichia coli. Proc. Natl. Acad. Sci. USA 79, 6119-6122
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6119-6122
    • Mobley, H.L.T.1    Rosen, B.P.2
  • 59
    • 0021762514 scopus 로고
    • A plasmid-encoded arsenite pump produces arsenite resistance in Escherichia coli
    • Rosen, B.P. and Borbolla, M.G. (1984) A plasmid-encoded arsenite pump produces arsenite resistance in Escherichia coli. Biochem. Biophys. Res. Commun. 124, 760-765
    • (1984) Biochem. Biophys. Res. Commun. , vol.124 , pp. 760-765
    • Rosen, B.P.1    Borbolla, M.G.2
  • 60
    • 0028796058 scopus 로고
    • Dual mode of energy coupling by the oxyanion-translocating ArsB protein
    • Dey, S. and Rosen, B.P. (1995) Dual mode of energy coupling by the oxyanion-translocating ArsB protein. J. Bacteriol. 177, 385-389
    • (1995) J. Bacteriol. , vol.177 , pp. 385-389
    • Dey, S.1    Rosen, B.P.2
  • 62
    • 0031033050 scopus 로고    scopus 로고
    • Alternate energy coupling of ArsB, the membrane subunit of the Ars anion-translocating ATPase
    • Kuroda, M., Dey, S., Sanders, O.I., and Rosen, B.P. (1997) Alternate energy coupling of ArsB, the membrane subunit of the Ars anion-translocating ATPase. J. Biol. Chem. 272, 326-331
    • (1997) J. Biol. Chem. , vol.272 , pp. 326-331
    • Kuroda, M.1    Dey, S.2    Sanders, O.I.3    Rosen, B.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.