메뉴 건너뛰기




Volumn 448, Issue , 1999, Pages 255-264

Copper homeostasis in Enterococcus hirae

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; COPPER;

EID: 0033278333     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-4859-1_23     Document Type: Conference Paper
Times cited : (26)

References (29)
  • 1
    • 0023202898 scopus 로고
    • Structure of the repressor-operator complex of bacteriophage 434
    • Anderson, J.E., Ptashne, M., and Harrison, S.C. (1987). Structure of the repressor-operator complex of bacteriophage 434. Nature 326, 846-852.
    • (1987) Nature , vol.326 , pp. 846-852
    • Anderson, J.E.1    Ptashne, M.2    Harrison, S.C.3
  • 2
    • 0028140357 scopus 로고
    • P-type ATPases of eukaryotes and bacteria: Sequence analyses and construction of phylogenetic trees
    • Fagan, M.J. and Saier, M.H., Jr. (1994). P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees. J. Mol. Evol. 38, 57-99.
    • (1994) J. Mol. Evol. , vol.38 , pp. 57-99
    • Fagan, M.J.1    Saier M.H., Jr.2
  • 3
    • 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 Tzagoloff, A. (1996). 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    Tzagoloff, A.3
  • 4
    • 0030967609 scopus 로고    scopus 로고
    • Copper-mediated repression of the activation domain in the yeast Mac1p transcription factor
    • Graden, J.A. and Winge, D.R. (1997). Copper-mediated repression of the activation domain in the yeast Mac1p transcription factor. Proc. Natl. Acad. Sci. USA 94, 5550-5555.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5550-5555
    • Graden, J.A.1    Winge, D.R.2
  • 5
    • 0027193708 scopus 로고
    • blaI and blaRI regulate β-lactamase and PBP 2a production in methicillin-resistant Staphylococcus aureus
    • Hackbarth, C.J. and Chambers, H.F. (1993). blaI and blaRI regulate β-lactamase and PBP 2a production in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 37, 1144-1149.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1144-1149
    • Hackbarth, C.J.1    Chambers, H.F.2
  • 6
    • 0022929392 scopus 로고
    • Nucleotide sequence of the penicillinase repressor gene penI of Bacillus licheniformis and regulation of penP and penI by the repressor
    • (published erratum appears in J Bacteriol 1987 Jul; 169(7) :3392)
    • Himeno, T., Imanaka, T., and Aiba, S. (1986). Nucleotide sequence of the penicillinase repressor gene penI of Bacillus licheniformis and regulation of penP and penI by the repressor (published erratum appears in J Bacteriol 1987 Jul; 169(7) :3392). J. Bacteriol. 168, 1128-1132.
    • (1986) J. Bacteriol. , vol.168 , pp. 1128-1132
    • Himeno, T.1    Imanaka, T.2    Aiba, S.3
  • 7
    • 0027500845 scopus 로고
    • MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast
    • Jungmann, J., Reins, H.A., Lee, J.W., Romeo, A., Hassett, R., Kosman, D., and Jentsch, S. (1993). MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast. EMBO J. 12, 5051-5056.
    • (1993) EMBO J. , vol.12 , pp. 5051-5056
    • Jungmann, J.1    Reins, H.A.2    Lee, J.W.3    Romeo, A.4    Hassett, R.5    Kosman, D.6    Jentsch, S.7
  • 8
    • 0030898098 scopus 로고    scopus 로고
    • Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis
    • Klomp, L.W., Lin, S.J., Yuan, D.S., Klausner, R.D., Culotta, V.C., and Gitlin, J.D. (1997). Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis. J. Biol. Chem. 272, 9221-9226.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9221-9226
    • Klomp, L.W.1    Lin, S.J.2    Yuan, D.S.3    Klausner, R.D.4    Culotta, V.C.5    Gitlin, J.D.6
  • 9
    • 0029039920 scopus 로고
    • The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity
    • Lin, S.J. and Culotta, V.C. (1995). The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc. Natl. Acad. Sci. USA 92, 3784-3788.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3784-3788
    • Lin, S.J.1    Culotta, V.C.2
  • 10
    • 0029883795 scopus 로고    scopus 로고
    • Copper biochemistry and molecular biology
    • Linder, M.C. and Hazegh Azam, M. (1996). Copper biochemistry and molecular biology. Am. J. Clin. Nutr. 63, 797S-811S.
    • (1996) Am. J. Clin. Nutr. , vol.63
    • Linder, M.C.1    Hazegh Azam, M.2
  • 11
    • 0028866670 scopus 로고
    • Organization of P-type ATPases: Significance of structural diversity
    • Lutsenko, S. and Kaplan, J.H. (1995). Organization of P-type ATPases: Significance of structural diversity. Biochemistry 34, 15607-15613.
    • (1995) Biochemistry , vol.34 , pp. 15607-15613
    • Lutsenko, S.1    Kaplan, J.H.2
  • 12
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Moller, J.V., Juul, B., and Le Maire, M. (1996). Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta Rev. Biomembr. 1286, 1-51.
    • (1996) Biochim. Biophys. Acta Rev. Biomembr. , vol.1286 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    Le Maire, M.3
  • 13
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase chain reaction
    • Ochman, H., Gerber, A.S., and Hartl, D.L. (1988). Genetic applications of an inverse polymerase chain reaction. Genetics 120, 621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hartl, D.L.3
  • 14
    • 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
  • 16
    • 0028938093 scopus 로고
    • Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae
    • Odermatt, A. and Solioz, M. (1995). Two trans-acting metalloregulatory proteins controlling expression of the copper-ATPases of Enterococcus hirae. J. Biol. Chem. 270, 4349-4354.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4349-4354
    • Odermatt, A.1    Solioz, M.2
  • 17
    • 33646830005 scopus 로고
    • Ion motive ATPases. I. Ubiquity, properties, and significance to cell function
    • Pedersen, P.L. and Carafoli, E. (1987a). Ion motive ATPases. I. Ubiquity, properties, and significance to cell function. Trends Biochem. Sci. 12, 146-150.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 146-150
    • Pedersen, P.L.1    Carafoli, E.2
  • 18
    • 0000412252 scopus 로고
    • Ion motive ATPases. II. Energy coupling and work output
    • Pedersen, P.L. and Carafoli, E. (1987b). Ion motive ATPases. II. Energy coupling and work output. Trends Biochem. Sci. 12, 186-189.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 186-189
    • Pedersen, P.L.1    Carafoli, E.2
  • 19
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling
    • Peitsch, M.C. (1996). ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling. Biochem. Soc. Trans. 24, 274-279.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 20
    • 0000619623 scopus 로고
    • Isopoly-vanadates, -niobates, and tantalates
    • Pope, M.T. and Dale, B.W. (1968). Isopoly-vanadates, -niobates, and tantalates, Rev. Chem. Soc. 22, 527-545.
    • (1968) Rev. Chem. Soc. , vol.22 , pp. 527-545
    • Pope, M.T.1    Dale, B.W.2
  • 22
    • 0003472479 scopus 로고    scopus 로고
    • Copper homeostasis by CPX-type ATPases, the subclass of heavy metal P-type ATPases
    • J.P. Andersen, ed. (London: JAI Press, Inc.)
    • Solioz, M. (1998). Copper homeostasis by CPX-type ATPases, the subclass of heavy metal P-type ATPases. In 1on pumps. J.P. Andersen, ed. (London: JAI Press, Inc.),
    • (1998) Ion Pumps
    • Solioz, M.1
  • 23
    • 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
  • 24
    • 0030199612 scopus 로고    scopus 로고
    • CPx-type ATPases: A class of P-type ATPases that pump heavy metals
    • Solioz, M. and Vulpe, C. (1996). CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci. 21, 237-241.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 237-241
    • Solioz, M.1    Vulpe, C.2
  • 25
    • 0030971055 scopus 로고    scopus 로고
    • Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system
    • Steele, R.A. and Opella, S.J. (1997). Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system. Biochemistry 36, 6885-6895.
    • (1997) Biochemistry , vol.36 , pp. 6885-6895
    • Steele, R.A.1    Opella, S.J.2
  • 26
    • 0031002899 scopus 로고    scopus 로고
    • CopY is a copper-inducible repressor of the Enterococcus hirae copper ATPases
    • Strausak, D. and Solioz, M. (1997). CopY is a copper-inducible repressor of the Enterococcus hirae copper ATPases. J. Biol. Chem. 272, 8932-8936.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8932-8936
    • Strausak, D.1    Solioz, M.2
  • 27
    • 0027299721 scopus 로고
    • Distribution of mec regulator genes in methicillin-resistant Staphylococcus clinical strains
    • Suzuki, E., Kuwahara Arai, K., Richardson, J.F., and Hiramatsu, K. (1993). Distribution of mec regulator genes in methicillin-resistant Staphylococcus clinical strains. Antimicrob. Agents Chemother. 37, 1219-1226.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1219-1226
    • Suzuki, E.1    Kuwahara Arai, K.2    Richardson, J.F.3    Hiramatsu, K.4
  • 28
    • 0029134884 scopus 로고
    • Cellular copper transport
    • Vulpe, C.D. and Packman, S. (1995). Cellular copper transport. Annu. Rev. Nutr. 15, 293-322.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 293-322
    • Vulpe, C.D.1    Packman, S.2
  • 29
    • 0023918768 scopus 로고
    • Regulation of the penicillinase genes of Bacillus Iicheniformis: Interaction of the pen repressor with its operators
    • Wittman, V. and Wong, H.C. (1988). Regulation of the penicillinase genes of Bacillus licheniformis: interaction of the pen repressor with its operators. J. Bacteriol. 770, 3206-3212.
    • (1988) J. Bacteriol. , vol.770 , pp. 3206-3212
    • Wittman, V.1    Wong, H.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.