메뉴 건너뛰기




Volumn 10, Issue 3, 2015, Pages 875-882

An alternate pathway of arsenate resistance in E. coli mediated by the glutathione S-transferase GstB

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ARSENATE REDUCTASE; ARSENATE SODIUM; ARSENIC ACID; ARSENIC TRIOXIDE; CYSTEINE; GLUTAREDOXIN; GLUTATHIONE; GLUTATHIONE TRANSFERASE; ARSENIC ACID DERIVATIVE; ARSENOUS ACID DERIVATIVE; PROTEIN BINDING;

EID: 84925679331     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb500755j     Document Type: Article
Times cited : (23)

References (40)
  • 1
    • 33747357184 scopus 로고    scopus 로고
    • Arsenate reduction: Thiol cascade chemistry with convergent evolution
    • Messens, J. and Silver, S. (2006) Arsenate reduction: Thiol cascade chemistry with convergent evolution J. Mol. Biol. 362, 1-17
    • (2006) J. Mol. Biol. , vol.362 , pp. 1-17
    • Messens, J.1    Silver, S.2
  • 4
    • 0028837094 scopus 로고
    • The ars operon of Escherichia coli confers arsenical and antimonial resistance
    • Carlin, A., Shi, W., Dey, S., and Rosen, B. P. (1995) The ars operon of Escherichia coli confers arsenical and antimonial 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
  • 5
    • 84885904079 scopus 로고    scopus 로고
    • Bacterial metabolism of environmental arsenic - Mechanisms and biotechnological applications
    • Kruger, M. C., Bertin, P. N., Heipieper, H. J., and Arsène-Ploetze, F. (2013) Bacterial metabolism of environmental arsenic - Mechanisms and biotechnological applications Appl. Microbiol. Biotechnol. 97, 3827-3841
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 3827-3841
    • Kruger, M.C.1    Bertin, P.N.2    Heipieper, H.J.3    Arsène-Ploetze, F.4
  • 6
    • 0037010116 scopus 로고    scopus 로고
    • Biochemistry of arsenic detoxification
    • Rosen, B. P. (2002) Biochemistry of arsenic detoxification FEBS Lett. 529, 86-92
    • (2002) FEBS Lett. , vol.529 , pp. 86-92
    • Rosen, B.P.1
  • 7
    • 0026640112 scopus 로고
    • Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258
    • Ji, G. and Silver, S. (1992) Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258 Proc. Natl. Acad. Sci. U.S.A. 89, 9474-9478
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9474-9478
    • Ji, G.1    Silver, S.2
  • 8
    • 0035923503 scopus 로고    scopus 로고
    • Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases
    • Bennett, M. S., Guan, Z., Laurberg, M., and Su, X. D. (2001) Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases Proc. Natl. Acad. Sci. U.S.A. 98, 13577-13582
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13577-13582
    • Bennett, M.S.1    Guan, Z.2    Laurberg, M.3    Su, X.D.4
  • 9
    • 0042591267 scopus 로고    scopus 로고
    • Directed evolution of a yeast arsenate reductase into a protein-tyrosine phosphatase
    • Mukhopadhyay, R., Zhou, Y., and Rosen, B. P. (2003) Directed evolution of a yeast arsenate reductase into a protein-tyrosine phosphatase J. Biol. Chem. 278, 24476-24480
    • (2003) J. Biol. Chem. , vol.278 , pp. 24476-24480
    • Mukhopadhyay, R.1    Zhou, Y.2    Rosen, B.P.3
  • 10
    • 0030824252 scopus 로고    scopus 로고
    • Ligand interactions of the ArsC arsenate reductase
    • Liu, J. and Rosen, B. P. (1997) Ligand interactions of the ArsC arsenate reductase J. Biol. Chem. 272, 21084-21089
    • (1997) J. Biol. Chem. , vol.272 , pp. 21084-21089
    • Liu, J.1    Rosen, B.P.2
  • 11
    • 0033579499 scopus 로고    scopus 로고
    • Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction
    • Shi, J., Vlamis-Gardikas, A., Åslund, F., Holmgren, A., and Rosen, B. P. (1999) Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction J. Biol. Chem. 274, 36039-36042
    • (1999) J. Biol. Chem. , vol.274 , pp. 36039-36042
    • Shi, J.1    Vlamis-Gardikas, A.2    Åslund, F.3    Holmgren, A.4    Rosen, B.P.5
  • 12
    • 4344611961 scopus 로고    scopus 로고
    • Arginine 60 in the ArsC arsenate reductase of E. Coli plasmid R773 determines the chemical nature of the bound As(III) product
    • DeMel, S., Shi, J., Martin, P., Rosen, B. P., and Edwards, B. F. P. (2004) Arginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) product Protein Sci. Publ. Protein Soc. 13, 2330-2340
    • (2004) Protein Sci. Publ. Protein Soc. , vol.13 , pp. 2330-2340
    • Demel, S.1    Shi, J.2    Martin, P.3    Rosen, B.P.4    Edwards, B.F.P.5
  • 13
    • 0030836016 scopus 로고    scopus 로고
    • Isolation of three contiguous genes, ACR1, ACR2, and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae
    • Bobrowicz, P., Wysocki, R., Owsianik, G., Goffeau, A., and Uaszewski, S. (1997) Isolation of three contiguous genes, ACR1, ACR2, and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae Yeast (Chichester Engl.) 13, 819-828
    • (1997) Yeast (Chichester Engl.) , vol.13 , pp. 819-828
    • Bobrowicz, P.1    Wysocki, R.2    Owsianik, G.3    Goffeau, A.4    Uaszewski, S.5
  • 15
    • 0344393487 scopus 로고    scopus 로고
    • An arsenate reductase from Synechocystis sp. Strain PCC 6803 exhibits a novel combination of catalytic characteristics
    • Li, R., Haile, J. D., and Kennelly, P. J. (2003) An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristics J. Bacteriol. 185, 6780-6789
    • (2003) J. Bacteriol. , vol.185 , pp. 6780-6789
    • Li, R.1    Haile, J.D.2    Kennelly, P.J.3
  • 16
    • 0032844160 scopus 로고    scopus 로고
    • Bacterial respiration of arsenic and selenium
    • Stolz, J. F. and Oremland, R. S. (1999) Bacterial respiration of arsenic and selenium FEMS Microbiol. Rev. 23, 615-627
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 615-627
    • Stolz, J.F.1    Oremland, R.S.2
  • 17
    • 78751578977 scopus 로고    scopus 로고
    • Laboratory evolution of glutathione biosynthesis reveals natural compensatory pathways
    • Veeravalli, K., Boyd, D., Iverson, B. L., Beckwith, J., and Georgiou, G. (2011) Laboratory evolution of glutathione biosynthesis reveals natural compensatory pathways Nat. Chem. Biol. 7, 101-105
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 101-105
    • Veeravalli, K.1    Boyd, D.2    Iverson, B.L.3    Beckwith, J.4    Georgiou, G.5
  • 18
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (A complete set of E. Coli K-12 ORF archive): Unique resources for biological research
    • Kitagawa, M., Ara, T., Arifuzzaman, M., Ioka-Nakamichi, T., Inamoto, E., Toyonaga, H., and Mori, H. (2006) Complete set of ORF clones of Escherichia coli ASKA library (A complete set of E. coli K-12 ORF archive): Unique resources for biological research DNA Res. 12, 291-299
    • (2006) DNA Res. , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 20
    • 40049106856 scopus 로고    scopus 로고
    • A study in molecular contingency: Glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase
    • Patrick, W. M. and Matsumura, I. (2008) A study in molecular contingency: Glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase J. Mol. Biol. 377, 323-336
    • (2008) J. Mol. Biol. , vol.377 , pp. 323-336
    • Patrick, W.M.1    Matsumura, I.2
  • 21
    • 78149274796 scopus 로고    scopus 로고
    • Recruitment of genes and enzymes conferring resistance to the nonnatural toxin bromoacetate
    • Desai, K. K. and Miller, B. G. (2010) Recruitment of genes and enzymes conferring resistance to the nonnatural toxin bromoacetate Proc. Natl. Acad. Sci. U.S.A. 107, 17968-17973
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17968-17973
    • Desai, K.K.1    Miller, B.G.2
  • 22
    • 0032493846 scopus 로고    scopus 로고
    • Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: Catalytic roles of Cys10 and His106
    • Nishida, M., Harada, S., Noguchi, S., Satow, Y., Inoue, H., and Takahashi, K. (1998) Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: Catalytic roles of Cys10 and His106 J. Mol. Biol. 281, 135-147
    • (1998) J. Mol. Biol. , vol.281 , pp. 135-147
    • Nishida, M.1    Harada, S.2    Noguchi, S.3    Satow, Y.4    Inoue, H.5    Takahashi, K.6
  • 24
    • 0039714219 scopus 로고    scopus 로고
    • Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases
    • Mössner, E., Huber-Wunderlich, M., and Glockshuber, R. (1998) Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases Prot. Sci. 7, 1233-1244
    • (1998) Prot. Sci. , vol.7 , pp. 1233-1244
    • Mössner, E.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 27
  • 28
    • 0025971827 scopus 로고
    • Glutathione S-transferases: Reaction mechanism, structure, and function
    • Armstrong, R. N. (1991) Glutathione S-transferases: Reaction mechanism, structure, and function Chem. Res. Toxicol. 4, 131-140
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 131-140
    • Armstrong, R.N.1
  • 29
    • 33750800395 scopus 로고    scopus 로고
    • The evolution of catalytic efficiency and substrate promiscuity in human θ class 1-1 glutathione transferase
    • Griswold, K. E., Aiyappan, N. S., Iverson, B. L., and Georgiou, G. (2006) The evolution of catalytic efficiency and substrate promiscuity in human θ class 1-1 glutathione transferase J. Mol. Biol. 364, 400-410
    • (2006) J. Mol. Biol. , vol.364 , pp. 400-410
    • Griswold, K.E.1    Aiyappan, N.S.2    Iverson, B.L.3    Georgiou, G.4
  • 32
    • 0035919812 scopus 로고    scopus 로고
    • Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione S-transferases
    • Xia, B., Vlamis-Gardikas, A., Holmgren, A., Wright, P. E., and Dyson, H. J. (2001) Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione S-transferases J. Mol. Biol. 310, 907-918
    • (2001) J. Mol. Biol. , vol.310 , pp. 907-918
    • Xia, B.1    Vlamis-Gardikas, A.2    Holmgren, A.3    Wright, P.E.4    Dyson, H.J.5
  • 33
    • 3242748862 scopus 로고    scopus 로고
    • Reduction of anti-leishmanial pentavalent antimonial drugs by a parasite-specific thiol-dependent reductase, TDR1
    • Denton, H., McGregor, J. C., and Coombs, G. H. (2004) Reduction of anti-leishmanial pentavalent antimonial drugs by a parasite-specific thiol-dependent reductase, TDR1 Biochem. J. 381, 405-412
    • (2004) Biochem. J. , vol.381 , pp. 405-412
    • Denton, H.1    McGregor, J.C.2    Coombs, G.H.3
  • 34
    • 84863884120 scopus 로고    scopus 로고
    • Leishmania TDR1 structure, a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation
    • Fyfe, P. K., Westrop, G. D., Silva, A. M., Coombs, G. H., and Hunter, W. N. (2012) Leishmania TDR1 structure, a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation Proc. Natl. Acad. Sci. U.S.A. 109, 11693-11698
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 11693-11698
    • Fyfe, P.K.1    Westrop, G.D.2    Silva, A.M.3    Coombs, G.H.4    Hunter, W.N.5
  • 35
    • 0344118144 scopus 로고    scopus 로고
    • Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli
    • Rife, C. L., Parsons, J. F., Xiao, G., Gilliland, G. L., and Armstrong, R. N. (2003) Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli Proteins 53, 777-782
    • (2003) Proteins , vol.53 , pp. 777-782
    • Rife, C.L.1    Parsons, J.F.2    Xiao, G.3    Gilliland, G.L.4    Armstrong, R.N.5
  • 36
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function, and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan, D., Meade, G., Foley, V. M., and Dowd, C. A. (2001) Structure, function, and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily Biochem. J. 360, 1-16
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.A.4
  • 38
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A. and Wanner, B. L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products Proc. Natl. Acad. Sci. U.S.A. 97, 6640-6645
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 39


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.