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Volumn 406, Issue 4, 2011, Pages 633-637

CutC is induced late during copper exposure and can modify intracellular copper content in Enterococcus faecalis

Author keywords

Copper content; Copper homeostasis; CutC; Enterococcus faecalis; Gene expression; QPCR

Indexed keywords

BACTERIAL PROTEIN; COPPER; PROTEIN CUTC; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

EID: 79953028628     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.02.109     Document Type: Article
Times cited : (24)

References (41)
  • 4
    • 0021759809 scopus 로고
    • Free radicals, lipid peroxidation, and cell damage
    • Halliwell B., Gutteridge J.M. Free radicals, lipid peroxidation, and cell damage. Lancet 1984, 2:1095.
    • (1984) Lancet , vol.2 , pp. 1095
    • Halliwell, B.1    Gutteridge, J.M.2
  • 5
    • 0027372312 scopus 로고
    • Effects of metal chelating agents on the oxidation of lipids induced by copper and iron
    • Yoshida Y., Furuta S., Niki E. Effects of metal chelating agents on the oxidation of lipids induced by copper and iron. Biochim. Biophys. Acta 1993, 1210:81-88.
    • (1993) Biochim. Biophys. Acta , vol.1210 , pp. 81-88
    • Yoshida, Y.1    Furuta, S.2    Niki, E.3
  • 6
    • 39349112330 scopus 로고    scopus 로고
    • Mechanisms for copper acquisition, distribution and regulation
    • Kim B.E., Nevitt T., Thiele D.J. Mechanisms for copper acquisition, distribution and regulation. Nat. Chem. Biol. 2008, 4:176-185.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 176-185
    • Kim, B.E.1    Nevitt, T.2    Thiele, D.J.3
  • 7
    • 0037565100 scopus 로고    scopus 로고
    • Copper homeostasis in Enterococcus hirae
    • Solioz M., Stoyanov J.V. Copper homeostasis in Enterococcus hirae. FEMS Microbiol. Rev. 2003, 27:183-195.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 183-195
    • Solioz, M.1    Stoyanov, J.V.2
  • 10
    • 56649117662 scopus 로고    scopus 로고
    • Knock down of Caenorhabditis elegans cutc-1 exacerbates the sensitivity toward high levels of copper
    • Calafato S., Swain S., Hughes S., Kille P., Sturzenbaum S.R. Knock down of Caenorhabditis elegans cutc-1 exacerbates the sensitivity toward high levels of copper. Toxicol. Sci. 2008, 106:384-391.
    • (2008) Toxicol. Sci. , vol.106 , pp. 384-391
    • Calafato, S.1    Swain, S.2    Hughes, S.3    Kille, P.4    Sturzenbaum, S.R.5
  • 11
    • 77049089212 scopus 로고    scopus 로고
    • Crystal structure of human copper homeostasis protein CutC reveals a potential copper-binding site
    • Li Y., Du J., Zhang P., Ding J. Crystal structure of human copper homeostasis protein CutC reveals a potential copper-binding site. J. Struct. Biol. 2010, 169:399-405.
    • (2010) J. Struct. Biol. , vol.169 , pp. 399-405
    • Li, Y.1    Du, J.2    Zhang, P.3    Ding, J.4
  • 12
    • 27744510126 scopus 로고    scopus 로고
    • Purification and preliminary crystallographic studies of CutC, a novel copper homeostasis protein from Shigella flexneri
    • Zhu Y.Q., Zhu D.Y., Lu H.X., Yang N., Li G.P., Wang D.C. Purification and preliminary crystallographic studies of CutC, a novel copper homeostasis protein from Shigella flexneri. Protein Pept. Lett. 2005, 12:823-826.
    • (2005) Protein Pept. Lett. , vol.12 , pp. 823-826
    • Zhu, Y.Q.1    Zhu, D.Y.2    Lu, H.X.3    Yang, N.4    Li, G.P.5    Wang, D.C.6
  • 13
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997, 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 16
    • 0028928174 scopus 로고
    • Comprehensive study on iterative algorithms of multiple sequence alignment
    • Hirosawa M., Totoki Y., Hoshida M., Ishikawa M. Comprehensive study on iterative algorithms of multiple sequence alignment. Comput. Appl. Biosci. 1995, 11:13-18.
    • (1995) Comput. Appl. Biosci. , vol.11 , pp. 13-18
    • Hirosawa, M.1    Totoki, Y.2    Hoshida, M.3    Ishikawa, M.4
  • 17
    • 33747586510 scopus 로고    scopus 로고
    • Improving the accuracy of protein secondary structure prediction using structural alignment
    • Montgomerie S., Sundararaj S., Gallin W.J., Wishart D.S. Improving the accuracy of protein secondary structure prediction using structural alignment. BMC Bioinf. 2006, 7:301.
    • (2006) BMC Bioinf. , vol.7 , pp. 301
    • Montgomerie, S.1    Sundararaj, S.2    Gallin, W.J.3    Wishart, D.S.4
  • 19
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Rozen S., Skaletsky H. Primer3 on the WWW for general users and for biologist programmers. Methods Mol. Biol. 2000, 132:365-386.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 365-386
    • Rozen, S.1    Skaletsky, H.2
  • 21
    • 77649342955 scopus 로고    scopus 로고
    • Gene expression profiling analysis of copper homeostasis in Arabidopsis thaliana
    • del Pozo T., Cambiazo V., Gonzalez M. Gene expression profiling analysis of copper homeostasis in Arabidopsis thaliana. Biochem. Biophys. Res. Commun. 2010, 393:248-252.
    • (2010) Biochem. Biophys. Res. Commun. , vol.393 , pp. 248-252
    • del Pozo, T.1    Cambiazo, V.2    Gonzalez, M.3
  • 23
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl M.W., Horgan G.W., Dempfle L. Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res. 2002, 30:e36.
    • (2002) Nucleic Acids Res. , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 24
    • 0031755702 scopus 로고    scopus 로고
    • Generation and testing of mutants of Enterococcus faecalis in a mouse peritonitis model
    • Singh K.V., Qin X., Weinstock G.M., Murray B.E. Generation and testing of mutants of Enterococcus faecalis in a mouse peritonitis model. J. Infect. Dis. 1998, 178:1416-1420.
    • (1998) J. Infect. Dis. , vol.178 , pp. 1416-1420
    • Singh, K.V.1    Qin, X.2    Weinstock, G.M.3    Murray, B.E.4
  • 25
    • 33745859661 scopus 로고    scopus 로고
    • Cop-like operon: structure and organization in species of the Lactobacillale order
    • Reyes A., Leiva A., Cambiazo V., Mendez M.A., Gonzalez M. Cop-like operon: structure and organization in species of the Lactobacillale order. Biol. Res. 2006, 39:87-93.
    • (2006) Biol. Res. , vol.39 , pp. 87-93
    • Reyes, A.1    Leiva, A.2    Cambiazo, V.3    Mendez, M.A.4    Gonzalez, M.5
  • 26
  • 27
    • 1842690128 scopus 로고    scopus 로고
    • The functional role of the binuclear metal center in d-aminoacylase: one-metal activation and second-metal attenuation
    • Lai W.L., Chou L.Y., Ting C.Y., Kirby R., Tsai Y.C., Wang A.H., Liaw S.H. The functional role of the binuclear metal center in d-aminoacylase: one-metal activation and second-metal attenuation. J. Biol. Chem. 2004, 279:13962-13967.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13962-13967
    • Lai, W.L.1    Chou, L.Y.2    Ting, C.Y.3    Kirby, R.4    Tsai, Y.C.5    Wang, A.H.6    Liaw, S.H.7
  • 29
    • 0346725017 scopus 로고    scopus 로고
    • Copper-induced oxidative stress in Saccharomyces cerevisiae targets enzymes of the glycolytic pathway
    • Shanmuganathan A., Avery S.V., Willetts S.A., Houghton J.E. Copper-induced oxidative stress in Saccharomyces cerevisiae targets enzymes of the glycolytic pathway. FEBS Lett. 2004, 556:253-259.
    • (2004) FEBS Lett. , vol.556 , pp. 253-259
    • Shanmuganathan, A.1    Avery, S.V.2    Willetts, S.A.3    Houghton, J.E.4
  • 30
    • 0037565099 scopus 로고    scopus 로고
    • Escherichia coli mechanisms of copper homeostasis in a changing environment
    • Rensing C., Grass G. Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol. Rev. 2003, 27:197-213.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 197-213
    • Rensing, C.1    Grass, G.2
  • 32
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis
    • D'Autreaux B., Toledano M.B. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat. Rev. Mol. Cell Biol. 2007, 8:813-824.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 33
    • 79251504566 scopus 로고    scopus 로고
    • Identification of gene products involved in the oxidative stress response of Moraxella catarrhalis
    • Hoopman T.C., Liu W., Joslin S.N., Pybus C., Brautigam C.A., Hansen E.J. Identification of gene products involved in the oxidative stress response of Moraxella catarrhalis. Infect. Immun. 2011, 79:745-755.
    • (2011) Infect. Immun. , vol.79 , pp. 745-755
    • Hoopman, T.C.1    Liu, W.2    Joslin, S.N.3    Pybus, C.4    Brautigam, C.A.5    Hansen, E.J.6
  • 34
    • 0029119263 scopus 로고
    • Regulation of hydroperoxidase (catalase) expression in Escherichia coli
    • Schellhorn H.E. Regulation of hydroperoxidase (catalase) expression in Escherichia coli. FEMS Microbiol. Lett. 1995, 131:113-119.
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 113-119
    • Schellhorn, H.E.1
  • 36
    • 41949128961 scopus 로고    scopus 로고
    • The global responses of Mycobacterium tuberculosis to physiological levels of copper
    • Ward S.K., Hoye E.A., Talaat A.M. The global responses of Mycobacterium tuberculosis to physiological levels of copper. J. Bacteriol. 2008, 190:2939-2946.
    • (2008) J. Bacteriol. , vol.190 , pp. 2939-2946
    • Ward, S.K.1    Hoye, E.A.2    Talaat, A.M.3
  • 37
    • 0037735344 scopus 로고    scopus 로고
    • Copper toxicity, oxidative stress, and antioxidant nutrients
    • Gaetke L.M., Chow C.K. Copper toxicity, oxidative stress, and antioxidant nutrients. Toxicology 2003, 189:147-163.
    • (2003) Toxicology , vol.189 , pp. 147-163
    • Gaetke, L.M.1    Chow, C.K.2
  • 40
    • 24044536614 scopus 로고    scopus 로고
    • Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU
    • Ding H., Harrison K., Lu J. Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. J. Biol. Chem. 2005, 280:30432-30437.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30432-30437
    • Ding, H.1    Harrison, K.2    Lu, J.3
  • 41
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber L., Imlay J.A. The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. Proc. Natl. Acad. Sci. USA 2009, 106:8344-8349.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.