메뉴 건너뛰기




Volumn 14, Issue 2, 2002, Pages 177-184

cuiD is a crucial gene for survival at high copper environment in Salmonella enterica serovar typhimurium

Author keywords

Copper; Copper Homeostasis; Multicopper Oxidase; Salmonella

Indexed keywords

AMINO ACID; COPPER ION; HYDROGEN PEROXIDE; LIGAND; OXIDOREDUCTASE; BACTERIAL PROTEIN; COPPER; CUEO PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN;

EID: 0037206561     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (26)

References (28)
  • 1
    • 0026094746 scopus 로고
    • Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins
    • Cha, J. S. and Cooksey, K. A. (1991) Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins. Proc. Natl. Acad. Sci. USA 88, 8915-8919.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8915-8919
    • Cha, J.S.1    Cooksey, K.A.2
  • 3
    • 0028152451 scopus 로고
    • The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake
    • Dancis, A., Haile, D., Yuan, D. S., and Klausner, R. D. (1994) The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake. J. Biol. Chem. 269, 25660-25667.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25660-25667
    • Dancis, A.1    Haile, D.2    Yuan, D.S.3    Klausner, R.D.4
  • 4
    • 0032506116 scopus 로고    scopus 로고
    • Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: An unexpected role for intracellular chloride channels
    • Davis-Kaplan, S. R., Askwith, C. C., Bengtzen, A. C., Radisky, D., and Kaplan, J. (1998) Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: an unexpected role for intracellular chloride channels. Proc. Natl. Acad. Sci. USA 95, 13641-13645.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13641-13645
    • Davis-Kaplan, S.R.1    Askwith, C.C.2    Bengtzen, A.C.3    Radisky, D.4    Kaplan, J.5
  • 5
    • 0030924805 scopus 로고    scopus 로고
    • The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Mac1p activator
    • Georgatsou, E., Mavrogiannis, L. A., Fragiadakis, G. S., and Alexandraki, D. (1997) The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Mac1p activator. J. Biol. Chem. 272, 13786-13792.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13786-13792
    • Georgatsou, E.1    Mavrogiannis, L.A.2    Fragiadakis, G.S.3    Alexandraki, D.4
  • 6
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • Glerum, D. M., Shtanko, A., and Txgoloff, A. (1996a) Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J. Biol. Chem. 271, 14504-14509.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14504-14509
    • Glerum, D.M.1    Shtanko, A.2    Txgoloff, A.3
  • 7
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • Glerum, D. M., Shtanko, A., and Txgoloff, A. (1996b) SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J. Biol. Chem. 271, 20531-20535.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20531-20535
    • Glerum, D.M.1    Shtanko, A.2    Txgoloff, A.3
  • 8
    • 0035101356 scopus 로고    scopus 로고
    • Genes involved in copper homeostasis in Escherichia coll
    • Grass, G. and Rensing, C. (2001) Genes involved in copper homeostasis in Escherichia coll. J. Bacteriol. 183, 2145-2147.
    • (2001) J. Bacteriol. , vol.183 , pp. 2145-2147
    • Grass, G.1    Rensing, C.2
  • 9
    • 0030857512 scopus 로고    scopus 로고
    • A Salmonella typhimurium genetic locus which confers copper tolerance on copper-sensitive mutants of Escherichia coli
    • Gupta, S. D., Wu, H. C., and Rick, P. D. (1997) A Salmonella typhimurium genetic locus which confers copper tolerance on copper-sensitive mutants of Escherichia coli. J. Bacteriol. 179, 4977-4984.
    • (1997) J. Bacteriol. , vol.179 , pp. 4977-4984
    • Gupta, S.D.1    Wu, H.C.2    Rick, P.D.3
  • 11
    • 0020428438 scopus 로고
    • Bacteriophage P22 as a vector for Mu mutagenesis in Salmonella typhimurium: Isolation of nad-lac and pnc-lac gene fusions
    • Holley, E. A. and Foster, J. W. (1982) Bacteriophage P22 as a vector for Mu mutagenesis in Salmonella typhimurium: isolation of nad-lac and pnc-lac gene fusions. J. Bacteriol. 152, 959-962.
    • (1982) J. Bacteriol. , vol.152 , pp. 959-962
    • Holley, E.A.1    Foster, J.W.2
  • 13
    • 0029786735 scopus 로고    scopus 로고
    • A widespread transposable element masks espression of a yeast copper transport gene
    • Knight, S. A., Labbe, S., Kwon, L. F., Kosman, D. J., and Thiele, D. J. (1996) A widespread transposable element masks espression of a yeast copper transport gene. Genes Dev. 10, 1917-1929.
    • (1996) Genes Dev. , vol.10 , pp. 1917-1929
    • Knight, S.A.1    Labbe, S.2    Kwon, L.F.3    Kosman, D.J.4    Thiele, D.J.5
  • 14
    • 0028157319 scopus 로고
    • Molecular cloning, chromosomal mapping, and sequence analysis of copper resistance genes from Xanthomonas campestris pv. juglandis: Homology with small blue copper proteins and multicopper oxidase
    • Lee, Y. A., Hendson, M., Panopoulos, N. J., and Schroth, M. N. (1994) Molecular cloning, chromosomal mapping, and sequence analysis of copper resistance genes from Xanthomonas campestris pv. juglandis: homology with small blue copper proteins and multicopper oxidase. J. Bacteriol. 176, 173-188.
    • (1994) J. Bacteriol. , vol.176 , pp. 173-188
    • Lee, Y.A.1    Hendson, M.2    Panopoulos, N.J.3    Schroth, M.N.4
  • 15
    • 0030910597 scopus 로고    scopus 로고
    • Arole for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport
    • Lin, S. J., Pufahl, R. A., Dancis, A., O'Halloran, T. V., and Culotta, V. C. (1997) Arole for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J. Biol. Chem. 272, 9215-9220.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9215-9220
    • Lin, S.J.1    Pufahl, R.A.2    Dancis, A.3    O'Halloran, T.V.4    Culotta, V.C.5
  • 17
    • 0024961798 scopus 로고
    • X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands
    • Messerschmidt, A., Rossi, A., Ladenstein, R., Huber, R., Bolognesi, M., Gatti, G., Marchesini, A., Petruzzelli, R., and Finazzi-Agro, A. (1989) X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands. J. Mol. Biol. 206, 513-529.
    • (1989) J. Mol. Biol. , vol.206 , pp. 513-529
    • Messerschmidt, A.1    Rossi, A.2    Ladenstein, R.3    Huber, R.4    Bolognesi, M.5    Gatti, G.6    Marchesini, A.7    Petruzzelli, R.8    Finazzi-Agro, A.9
  • 18
    • 0028938093 scopus 로고
    • Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPase of Enterococcus hirae
    • Odermatt, A. and Solioz, M. (1995) Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPase of Enterococcus hirae. J. Biol. Chem. 270, 4349-4354.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4349-4354
    • Odermatt, A.1    Solioz, M.2
  • 19
    • 0027288228 scopus 로고
    • Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae
    • Odermatt, A., Suter, H., Krapf, R., and Solioz, M. (1993) Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J. Biol. Chem. 268, 12775-12779.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12775-12779
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 20
    • 0024618002 scopus 로고
    • Primary structure of cucumber (Cucumis sativus) ascorbate oxidase deduced from cDNA sequence: Homology with blue copper proteins and tissue-specific expression
    • Ohkawa, J., Okada, N., Shinmyo, A., and Takano, M. (1989) Primary structure of cucumber (Cucumis sativus) ascorbate oxidase deduced from cDNA sequence: homology with blue copper proteins and tissue-specific expression. Proc. Natl. Acad. Sci. USA 86, 1239-1243.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1239-1243
    • Ohkawa, J.1    Okada, N.2    Shinmyo, A.3    Takano, M.4
  • 21
    • 0034613337 scopus 로고    scopus 로고
    • Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, CueR
    • Outten, F. W., Outten, C. E., Hale, J., and O'Halloran, T. V. (2000) Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal MerR homologue, CueR. J. Biol. Chem. 275, 31024-31029.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31024-31029
    • Outten, F.W.1    Outten, C.E.2    Hale, J.3    O'Halloran, T.V.4
  • 22
    • 0037477740 scopus 로고    scopus 로고
    • Adelicate balance: Homeostatic control of copper uptake and distribution
    • Pena, M. M. O., Lee, J., and Thiele, D. J. (1999) Adelicate balance: homeostatic control of copper uptake and distribution. J. Nutr. 129, 1251-1260.
    • (1999) J. Nutr. , vol.129 , pp. 1251-1260
    • Pena, M.M.O.1    Lee, J.2    Thiele, D.J.3
  • 26
    • 0028906811 scopus 로고
    • Copper and silver transport by CopB-ATPase in membrane vesicles of Enterococcus hirae
    • Solioz, M. and Odermatt, A. (1995) Copper and silver transport by CopB-ATPase in membrane vesicles of Enterococcus hirae. J. Biol. Chem. 270, 9217-9221.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9217-9221
    • Solioz, M.1    Odermatt, A.2
  • 27
    • 0034697156 scopus 로고    scopus 로고
    • The twin arginine consensus motif of tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli
    • Stanley, N. R., Palmer, T., and Berks, B. C. (2000) The twin arginine consensus motif of tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 275, 11591-11596.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 28
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • Von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14, 4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.