메뉴 건너뛰기




Volumn 9, Issue 9, 2009, Pages 2568-2577

Drosophila proteins interacting with metallothioneins: a metal-dependent recognition

Author keywords

Drosophila; Metallothionein; Peroxiredoxin; Protein interaction; Saccharomyces cerevisiae

Indexed keywords

COPPER; METAL COMPLEX; METALLOTHIONEIN; METALLOTHIONEIN A; METALLOTHIONEIN B; PEROXIREDOXIN; POLYHISTIDINE; PROTEIN CRS5P; PROTEIN CUP1P; PROTEIN TSA1P; PROTEIN TSA2P; PROTEOME; UNCLASSIFIED DRUG; ZINC;

EID: 66249125960     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800729     Document Type: Article
Times cited : (3)

References (35)
  • 1
    • 33947463103 scopus 로고    scopus 로고
    • Margoshes, M., Vallee, B. L., A cadmium protein from equine kidney cortex. J. Am. Chem. Soc. 1957, 79, 48134814.
    • Margoshes, M., Vallee, B. L., A cadmium protein from equine kidney cortex. J. Am. Chem. Soc. 1957, 79, 48134814.
  • 2
    • 0032555204 scopus 로고    scopus 로고
    • The elusive function of metallothioneins
    • Palmiter, R. D., The elusive function of metallothioneins. Proc. Natl. Acad. Sci. USA 1998, 95, 8428-8430.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8428-8430
    • Palmiter, R.D.1
  • 4
    • 14644397252 scopus 로고    scopus 로고
    • 7me- tallothionein-3 and the synaptic vesicle cycle: Interaction of metallothionein-3 with the small GTPase Rab3A
    • 7me- tallothionein-3 and the synaptic vesicle cycle: Interaction of metallothionein-3 with the small GTPase Rab3A. Biochemistry 2005, 44, 3159-3165.
    • (2005) Biochemistry , vol.44 , pp. 3159-3165
    • Knipp, M.1    Meloni, G.2    Roschitzki, B.3    Vasak, M.4
  • 5
    • 17744380813 scopus 로고    scopus 로고
    • Identification of mouse brain proteins associated with isoform 3 of metallothionein
    • Lahti, D. W., Hoekman, J. D., Tokheim, A. M., Martin, B. L., Armitage, I. M., Identification of mouse brain proteins associated with isoform 3 of metallothionein. Protein Sci. 2005, 14, 1151-1157.
    • (2005) Protein Sci , vol.14 , pp. 1151-1157
    • Lahti, D.W.1    Hoekman, J.D.2    Tokheim, A.M.3    Martin, B.L.4    Armitage, I.M.5
  • 6
    • 0037413730 scopus 로고    scopus 로고
    • Knockout of'metal-responsive transcription factor' MTF-1 in Drosophila by homologous recombination reveals its central role in heavy metal homeostasis
    • Egli, D., Selvaraj, A., Yepiskoposyan, H., Zhang, B. et al., Knockout of'metal-responsive transcription factor' MTF-1 in Drosophila by homologous recombination reveals its central role in heavy metal homeostasis. EMBOJ. 2003, 22, 100108.
    • (2003) EMBOJ , vol.22 , pp. 100108
    • Egli, D.1    Selvaraj, A.2    Yepiskoposyan, H.3    Zhang, B.4
  • 7
    • 33646735728 scopus 로고    scopus 로고
    • The four members of the Drosophila metallothionein family exhibit distinct yet overlapping in heavy metal homeostasis and detoxification
    • Egli, D., Domenech, J., Selvaraj, A., Balamurugan, K. et al., The four members of the Drosophila metallothionein family exhibit distinct yet overlapping in heavy metal homeostasis and detoxification. Genes Cells 2006, 11, 647-658.
    • (2006) Genes Cells , vol.11 , pp. 647-658
    • Egli, D.1    Domenech, J.2    Selvaraj, A.3    Balamurugan, K.4
  • 8
    • 0028787303 scopus 로고
    • Expression of metallothionein genes during the post-embryonic development of Drosophila melanogaster
    • Durliat, M., Bonneton, F., Boissonneau, E., Andre, M., Weg- nez, M., Expression of metallothionein genes during the post-embryonic development of Drosophila melanogaster. Biometals 1995, 8, 339-351.
    • (1995) Biometals , vol.8 , pp. 339-351
    • Durliat, M.1    Bonneton, F.2    Boissonneau, E.3    Andre, M.4    Weg- nez, M.5
  • 9
    • 0033953938 scopus 로고    scopus 로고
    • Drosophila MTN: A metazoan copper-thionein related to fungal forms
    • Valls, M., Bofill, R., Romero-Isart, N., Gonzalez-Duarte, R. et al., Drosophila MTN: A metazoan copper-thionein related to fungal forms. FEBS Lett. 2000, 467, 189-194.
    • (2000) FEBS Lett , vol.467 , pp. 189-194
    • Valls, M.1    Bofill, R.2    Romero-Isart, N.3    Gonzalez-Duarte, R.4
  • 10
    • 0037413863 scopus 로고    scopus 로고
    • The second member of a Drosophila dual copper-thionein system
    • MTO
    • Domenech, J., Palacios, O., Villarreal, L., Gonzalez-Duarte, P. et al., MTO: The second member of a Drosophila dual copper-thionein system. FEBS Lett. 2003, 533, 72-78.
    • (2003) FEBS Lett , vol.533 , pp. 72-78
    • Domenech, J.1    Palacios, O.2    Villarreal, L.3    Gonzalez-Duarte, P.4
  • 11
    • 0035980048 scopus 로고    scopus 로고
    • A new insight into metallothionein (MT) classification and evolution. The in vivo and in vitro metal binding features of Homarus americanus recombinant MT
    • Valls, M., Bofill, R., Gonzalez-Duarte, R., Gonzalez-Duarte, P. et al., A new insight into metallothionein (MT) classification and evolution. The in vivo and in vitro metal binding features of Homarus americanus recombinant MT. J. Biol. Chem. 2001, 276, 32835-32843.
    • (2001) J. Biol. Chem , vol.276 , pp. 32835-32843
    • Valls, M.1    Bofill, R.2    Gonzalez-Duarte, R.3    Gonzalez-Duarte, P.4
  • 12
    • 0026318278 scopus 로고
    • Metal removal and substitution in vertebrate and invertebrate metallothioneins
    • Vasak, M., Metal removal and substitution in vertebrate and invertebrate metallothioneins. Methods Enzimol. 1991, 205, 452-458.
    • (1991) Methods Enzimol , vol.205 , pp. 452-458
    • Vasak, M.1
  • 13
    • 33845693008 scopus 로고    scopus 로고
    • The Sac- charomyces cerevisiae Crs5 metallothionein metal-binding abilities and its role in the response to zinc overload
    • Pagani, A., Villarreal, L., Capdevila, M., Atrian, S., The Sac- charomyces cerevisiae Crs5 metallothionein metal-binding abilities and its role in the response to zinc overload. Mol. Microbiol. 2007, 63, 256-269.
    • (2007) Mol. Microbiol , vol.63 , pp. 256-269
    • Pagani, A.1    Villarreal, L.2    Capdevila, M.3    Atrian, S.4
  • 14
    • 0345276583 scopus 로고    scopus 로고
    • Signaling events for metallothionein induction
    • Haq, F., Mahoney, M., Koropatnick, J., Signaling events for metallothionein induction. Mutat. Res. 2003, 533, 211-226.
    • (2003) Mutat. Res , vol.533 , pp. 211-226
    • Haq, F.1    Mahoney, M.2    Koropatnick, J.3
  • 15
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 60 amino acid metallothionein-like protein
    • Uchida, Y., Takio, K., Titani, K., Ihara, Y., Tomonaga, M., The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 60 amino acid metallothionein-like protein. Neuron 1991, 7, 337-347.
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3    Ihara, Y.4    Tomonaga, M.5
  • 17
    • 0021829810 scopus 로고
    • Distinct metal-binding configurations in metallothionein
    • Nielson, K. B., Atkin, C. L., Winge, D. R., Distinct metal-binding configurations in metallothionein. J. Biol. Chem. 1985, 260, 5342-5350.
    • (1985) J. Biol. Chem , vol.260 , pp. 5342-5350
    • Nielson, K.B.1    Atkin, C.L.2    Winge, D.R.3
  • 18
    • 0029661206 scopus 로고    scopus 로고
    • 111Cd NMR studies of the domain specificity of Ag + and Cu + binding to metallothionein
    • 111Cd NMR studies of the domain specificity of Ag + and Cu + binding to metallothionein. Biochemistry 1996, 35, 13929-13936.
    • (1996) Biochemistry , vol.35 , pp. 13929-13936
    • Li, H.1    Otvos, J.D.2
  • 19
    • 34247326875 scopus 로고    scopus 로고
    • Coordination of three and four Cu(I) to the a-and p-domain of vertebrate Zn- metallothionein-1, respectively, induces significant structural changes
    • Doldener, B., Echner, H., Beck, A., Hartmann, H. J. et al., Coordination of three and four Cu(I) to the a-and p-domain of vertebrate Zn- metallothionein-1, respectively, induces significant structural changes. FEBS J. 2007, 274, 2349-2362.
    • (2007) FEBS J , vol.274 , pp. 2349-2362
    • Doldener, B.1    Echner, H.2    Beck, A.3    Hartmann, H.J.4
  • 20
    • 38749125910 scopus 로고    scopus 로고
    • Peroxiredoxin systems. Structures and functions
    • Flohe, L, Harris, J. R, Eds
    • Flohe, L., Harris, J. R. (Eds.), Peroxiredoxin systems. Structures and functions. Subcel. Biochem. 2007, 44, 1-385.
    • (2007) Subcel. Biochem , vol.44 , pp. 1-385
  • 21
    • 0027259213 scopus 로고
    • Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible rol in vivo. Biochem. Bio- phys
    • Lim, Y. S.,Cha, M. K., Kim, H. K., Uhm, T. B. etal., Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible rol in vivo. Biochem. Bio- phys. Res. Commun. 1993, 192, 273-280.
    • (1993) Res. Commun , vol.192 , pp. 273-280
    • Lim, Y.S.1    Cha, M.K.2    Kim, H.K.3    Uhm, T.B.4
  • 22
    • 0028072911 scopus 로고
    • Thioredoxin-depend- ent peroxide reductase from yeast
    • Chae, H. Z., Chung, S. J., Rhee, S. G., Thioredoxin-depend- ent peroxide reductase from yeast. J. Biol. Chem. 1994, 269, 27670-27678.
    • (1994) J. Biol. Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 23
    • 0035500514 scopus 로고    scopus 로고
    • The peroxiredoxin gene family in Drosophila melanoga- ster. FreeRadic
    • Radyuk, S. N., Klichko, V. I., Spinola, B., Sohal, R. S., Orr, W. C., The peroxiredoxin gene family in Drosophila melanoga- ster. FreeRadic. Biol. Med. 2001, 31, 1090-1100.
    • (2001) Biol. Med , vol.31 , pp. 1090-1100
    • Radyuk, S.N.1    Klichko, V.I.2    Spinola, B.3    Sohal, R.S.4    Orr, W.C.5
  • 24
    • 0037124040 scopus 로고    scopus 로고
    • Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster: Isolation and characterization of a second thioredoxin in D. melanogaster and evidence for distinct biological functions of Trx-1 and Trx-2
    • Bauer, H., Kanzok, S. M., Schirmer, R. H., Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster: Isolation and characterization of a second thioredoxin in D. melanogaster and evidence for distinct biological functions of Trx-1 and Trx-2. J. Biol. Chem. 2002, 277, 17457-17463.
    • (2002) J. Biol. Chem , vol.277 , pp. 17457-17463
    • Bauer, H.1    Kanzok, S.M.2    Schirmer, R.H.3
  • 25
    • 0021944046 scopus 로고
    • Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals
    • Thornalley, P. J., Vasak, M., Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals. Biochim. Biophys. Acta 1985, 827, 36-44.
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 36-44
    • Thornalley, P.J.1    Vasak, M.2
  • 26
    • 0001036316 scopus 로고
    • Copper metallothionein of yeast, structure of the gene, and regulation of expression
    • Butt, T. R., Sternberg, E. J., Gorman, J. A., Clark, P. et al., Copper metallothionein of yeast, structure of the gene, and regulation of expression. Proc. Natl. Acad. Sci. USA 1984, 87, 3332-3336.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3332-3336
    • Butt, T.R.1    Sternberg, E.J.2    Gorman, J.A.3    Clark, P.4
  • 27
    • 0027946045 scopus 로고
    • CRS5 encodes a metallothionein-like protein in Saccharomyces cerevisiae
    • Culotta, V. C., Howard, W. R., Liu, X. F., CRS5 encodes a metallothionein-like protein in Saccharomyces cerevisiae. J. Biol. Chem. 1994, 269, 25295-25302.
    • (1994) J. Biol. Chem , vol.269 , pp. 25295-25302
    • Culotta, V.C.1    Howard, W.R.2    Liu, X.F.3
  • 28
    • 33745044661 scopus 로고    scopus 로고
    • Thionein can serve as a reducing agent for the methionine sulfoxide reductases
    • Sagher, D., Brunell, D., Hejtmancik, J. F., Kantorow, M. etal., Thionein can serve as a reducing agent for the methionine sulfoxide reductases. Proc. Natl. Acad. Sci. USA 2006, 103, 8656-8661.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8656-8661
    • Sagher, D.1    Brunell, D.2    Hejtmancik, J.F.3    Kantorow, M.4
  • 29
    • 0029767918 scopus 로고    scopus 로고
    • Enhanced effectiveness of copper ion buffering by CUP1 metallothionein compared with CRS5 metal- lothionein in Saccharomycescerevisiae
    • Jensen, L. T., Howard, W. R., Strain, J. J., Winge, D. R., Culotta, V. C., Enhanced effectiveness of copper ion buffering by CUP1 metallothionein compared with CRS5 metal- lothionein in Saccharomycescerevisiae. J. Biol. Chem. 1996, 271, 18514-18519.
    • (1996) J. Biol. Chem , vol.271 , pp. 18514-18519
    • Jensen, L.T.1    Howard, W.R.2    Strain, J.J.3    Winge, D.R.4    Culotta, V.C.5
  • 30
    • 33749641286 scopus 로고    scopus 로고
    • Metallothionein redox cycle and function
    • Kang, Y. J., Metallothionein redox cycle and function. Exp. Biol. Med. 2006, 31, 1459-1467.
    • (2006) Exp. Biol. Med , vol.31 , pp. 1459-1467
    • Kang, Y.J.1
  • 31
    • 0032584186 scopus 로고    scopus 로고
    • Control of zinc transfer between thionein, metallothionein, and zinc proteins
    • Jacob, C., Maret, W., Vallee, B. L., Control of zinc transfer between thionein, metallothionein, and zinc proteins. Proc. Natl. Acad. Sci. USA 1998, 95, 3489-3494.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3489-3494
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 32
    • 19744375548 scopus 로고    scopus 로고
    • Metallothionein transfers zinc to mitochondrial aconitase through a direct interaction in mouse hearts
    • Feng, W., Cai, J., Pierce, W. M., Franklin, R. B. et al., Metallothionein transfers zinc to mitochondrial aconitase through a direct interaction in mouse hearts. Biochem. Biophys. Res. Commun. 2005, 332, 853-858.
    • (2005) Biochem. Biophys. Res. Commun , vol.332 , pp. 853-858
    • Feng, W.1    Cai, J.2    Pierce, W.M.3    Franklin, R.B.4
  • 33
    • 0034099055 scopus 로고    scopus 로고
    • The antioxidant properties of zinc
    • Powell, S. R., The antioxidant properties of zinc. J. Nutr. 2000, 130, 1447S-1454S.
    • (2000) J. Nutr , vol.130
    • Powell, S.R.1
  • 34
    • 34047243851 scopus 로고    scopus 로고
    • Regulation of the yeast TSA1 peroxiredoxin by Zap1 is an adaptive response to the oxidative stress of zinc deficiency
    • Wu, C.-Y., Bird, A. J., Winge, D., Eide, D. J., Regulation of the yeast TSA1 peroxiredoxin by Zap1 is an adaptive response to the oxidative stress of zinc deficiency. J. Biol. Chem. 2007, 282, 2184-2195.
    • (2007) J. Biol. Chem , vol.282 , pp. 2184-2195
    • Wu, C.-Y.1    Bird, A.J.2    Winge, D.3    Eide, D.J.4
  • 35
    • 47749156827 scopus 로고    scopus 로고
    • HDAC6 is a specific deacetylase of per- oxiredoxins and is involved in redox regulation
    • Parmigiani, R. B., Xu, W. S., Venta-Perez, G., Erdjument- Bromage, H. et al., HDAC6 is a specific deacetylase of per- oxiredoxins and is involved in redox regulation. Proc. Natl. Acad. Sci. USA 2008, 105, 9633-9638.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9633-9638
    • Parmigiani, R.B.1    Xu, W.S.2    Venta-Perez, G.3    Erdjument- Bromage, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.