메뉴 건너뛰기




Volumn 53, Issue 5, 1997, Pages 459-465

Effects of amino acid replacements on cadmium binding of metallothionein α-fragment

Author keywords

fragment; Amino acid replacement; Cadmium; Cysteine; Escherichia coli; Expression; Metal; Metallothionein

Indexed keywords

CADMIUM; CYSTEINE; GLYCINE; METALLOTHIONEIN; MUTANT PROTEIN;

EID: 0030799199     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050056     Document Type: Article
Times cited : (10)

References (32)
  • 1
    • 0023087396 scopus 로고
    • Chemistry and biochemistry of metallothionein
    • Kägi J. H. R. and Kojima Y. (1987) Chemistry and biochemistry of metallothionein. Experientia Suppl. 52: 25-62
    • (1987) Experientia Suppl. , vol.52 , pp. 25-62
    • Kägi, J.H.R.1    Kojima, Y.2
  • 2
    • 0022555879 scopus 로고
    • Metallothionein
    • Hamer D. H. (1986) Metallothionein. A. Rev. Biochem. 55: 913-951
    • (1986) A. Rev. Biochem. , vol.55 , pp. 913-951
    • Hamer, D.H.1
  • 4
    • 0022349249 scopus 로고
    • Independence of the domain of metallothionein in metal binding
    • Nielson K. B. and Winge D. R. (1985) Independence of the domain of metallothionein in metal binding. J. Biol. Chem. 260: 8698-8701
    • (1985) J. Biol. Chem. , vol.260 , pp. 8698-8701
    • Nielson, K.B.1    Winge, D.R.2
  • 5
    • 0000119940 scopus 로고
    • Structure of the metal cluster in rabbit liver metallothionein
    • Otvos J. D. and Armitage I. M. (1980) Structure of the metal cluster in rabbit liver metallothionein. Proc. Natl. Acad. Sci. USA 77: 7094-7098
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7094-7098
    • Otvos, J.D.1    Armitage, I.M.2
  • 6
    • 0023645234 scopus 로고
    • Metal co-ordination in rat liver metallothionein-2 prepared with or without reconstitution of the metal cluster, and comparison with rabbit liver metallothionein-2
    • Vasak M., Worgotter E., Wagner G., Kägi J. H. R. and Wüthrich K. (1987) Metal co-ordination in rat liver metallothionein-2 prepared with or without reconstitution of the metal cluster, and comparison with rabbit liver metallothionein-2. J. Molec. Biol. 196: 711-719
    • (1987) J. Molec. Biol. , vol.196 , pp. 711-719
    • Vasak, M.1    Worgotter, E.2    Wagner, G.3    Kägi, J.H.R.4    Wüthrich, K.5
  • 7
    • 0023937834 scopus 로고
    • Three-dimensional structure of rabbit liver [Cd7] metallothionein-2a in aqueous solution determined by nuclear magnetic resonance
    • Arsenive A., Schultze P., Worgotter E., Braun E., Wagner G., Vasak M. et al. (1988) Three-dimensional structure of rabbit liver [Cd7] metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. J. Molec. Biol. 201: 637-657
    • (1988) J. Molec. Biol. , vol.201 , pp. 637-657
    • Arsenive, A.1    Schultze, P.2    Worgotter, E.3    Braun, E.4    Wagner, G.5    Vasak, M.6
  • 10
    • 0023133003 scopus 로고
    • Expression of cloned monkey metallothionein in Escherichia coli
    • Murooka Y. and Nagaoka T. (1987) Expression of cloned monkey metallothionein in Escherichia coli. Appl. Environ. Microbiol. 53: 204-207
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 204-207
    • Murooka, Y.1    Nagaoka, T.2
  • 11
    • 0023691990 scopus 로고
    • Expression of the mouse metallothionein-1 gene in Escherichia coli: Increased tolerance to heavy metals
    • Hou Y., Kim R. and Kim S. (1988) Expression of the mouse metallothionein-1 gene in Escherichia coli: Increased tolerance to heavy metals. Biochim. Biophys. Acta 951: 230-234
    • (1988) Biochim. Biophys. Acta , vol.951 , pp. 230-234
    • Hou, Y.1    Kim, R.2    Kim, S.3
  • 12
    • 0025278204 scopus 로고
    • The expression of a synthetic rainbow trout metallothionein gene in E. coli
    • Kille P., Stephens P., Cyer A. and Kay J. (1990) The expression of a synthetic rainbow trout metallothionein gene in E. coli. Biochim. Biophys. Acta 1048: 178-186
    • (1990) Biochim. Biophys. Acta , vol.1048 , pp. 178-186
    • Kille, P.1    Stephens, P.2    Cyer, A.3    Kay, J.4
  • 13
    • 0029609336 scopus 로고
    • Expression of human metallothionein-2 in Escherichia coli: Cadmium tolerance of transformed cells
    • Odawara F., Kurasaki M., Suzuki-Kurasaki M., Oikawa S., Emoto T., Yamasaki F. et al. (1995) Expression of human metallothionein-2 in Escherichia coli: Cadmium tolerance of transformed cells. J. Biochem. 118: 1131-1137
    • (1995) J. Biochem. , vol.118 , pp. 1131-1137
    • Odawara, F.1    Kurasaki, M.2    Suzuki-Kurasaki, M.3    Oikawa, S.4    Emoto, T.5    Yamasaki, F.6
  • 14
    • 0026322835 scopus 로고
    • Differential effect of cysteine-to-serine substitutions in metallothionein on cadmium resistance
    • Chernaik M. L. and Huang P. C. (1991) Differential effect of cysteine-to-serine substitutions in metallothionein on cadmium resistance. Proc. Natl. Acad. Sci. USA 88: 3024-3028
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3024-3028
    • Chernaik, M.L.1    Huang, P.C.2
  • 15
    • 0025788675 scopus 로고
    • Effect of cysteine replacements at positions 13 and 50 in metallothionein structure
    • Cismowski M. J. and Huang P. C. (1991) Effect of cysteine replacements at positions 13 and 50 in metallothionein structure. Biochemistry 30: 6626-6632
    • (1991) Biochemistry , vol.30 , pp. 6626-6632
    • Cismowski, M.J.1    Huang, P.C.2
  • 17
    • 0027225407 scopus 로고
    • Metallothionein detoxification function is impaired by replacement of both conserved lysines with glutamines in the hinge between the two domains
    • Cody C. W. and Huang P. C. (1993) Metallothionein detoxification function is impaired by replacement of both conserved lysines with glutamines in the hinge between the two domains. Biochemistry 32: 5127-5131
    • (1993) Biochemistry , vol.32 , pp. 5127-5131
    • Cody, C.W.1    Huang, P.C.2
  • 18
    • 0028170096 scopus 로고
    • Replacement of all α-domain lysines with glutamate reduces metallothionein detoxification function
    • Cody C. W. and Huang P. C. (1994) Replacement of all α-domain lysines with glutamate reduces metallothionein detoxification function. Biochem. Biophys. Res. Commun. 202: 954-959
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 954-959
    • Cody, C.W.1    Huang, P.C.2
  • 19
    • 0028015987 scopus 로고
    • Substitution of glutamic acids for the conserved lysies in the α domain affects metal binding in both α and β domains of mammalian metallothionein
    • Pan K. P., Hou F., Cody C. W. and Huang P. C. (1994) Substitution of glutamic acids for the conserved lysies in the α domain affects metal binding in both α and β domains of mammalian metallothionein. Biochem. Biophys. Res. Commun. 202: 621-628
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 621-628
    • Pan, K.P.1    Hou, F.2    Cody, C.W.3    Huang, P.C.4
  • 21
    • 0026733431 scopus 로고
    • Sequestration of cadmium and copper by recombinant rainbow trout and human metallothioneins and by chimeric (mermaid and fishman) proteins within interchanged domains
    • Kille P., Lees W. E., Darke B. M., Winge D. R., Dametron C. T., Stephens P. et al. (1992) Sequestration of cadmium and copper by recombinant rainbow trout and human metallothioneins and by chimeric (mermaid and fishman) proteins within interchanged domains. J. Biol. Chem. 267: 8042-8049
    • (1992) J. Biol. Chem. , vol.267 , pp. 8042-8049
    • Kille, P.1    Lees, W.E.2    Darke, B.M.3    Winge, D.R.4    Dametron, C.T.5    Stephens, P.6
  • 22
    • 0002106617 scopus 로고
    • Evolution, structure and chemical activity of class I metallothioneins: An overview
    • Suzuki K. T., Imura N. and Kimura M. (eds). Birhäuser Verlag, Basel
    • Kägi J. H. R. (1993) Evolution, structure and chemical activity of class I metallothioneins: An overview. In: Metallothionein III, pp. 29-35. Suzuki K. T., Imura N. and Kimura M. (eds). Birhäuser Verlag, Basel
    • (1993) Metallothionein III , pp. 29-35
    • Kägi, J.H.R.1
  • 23
    • 0021046411 scopus 로고
    • Order of metal binding in metallothionein
    • Nielson K. B. and Winge D. R. (1983) Order of metal binding in metallothionein. J. Biol. Chem. 10: 13063-13069
    • (1983) J. Biol. Chem. , vol.10 , pp. 13063-13069
    • Nielson, K.B.1    Winge, D.R.2
  • 24
    • 0030474910 scopus 로고    scopus 로고
    • Independent self assembly of cadmium-binding 2-fragment of metallothionein without participation of β-fragment in Escherichia coli
    • Kurasaki M., Emoto T., Einde Arias A. R., Okabe M., Yamasaki F., Oikawa S. et al. (1996) Independent self assembly of cadmium-binding 2-fragment of metallothionein without participation of β-fragment in Escherichia coli. Protein Eng. 9: 1173-1180
    • (1996) Protein Eng. , vol.9 , pp. 1173-1180
    • Kurasaki, M.1    Emoto, T.2    Einde Arias, A.R.3    Okabe, M.4    Yamasaki, F.5    Oikawa, S.6
  • 25
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of protein in the range from 1 to 100 kDa
    • Schägger H. and von Jagow G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of protein in the range from 1 to 100 kDa. Analyt. Biochem. 166: 368-379
    • (1987) Analyt. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 26
    • 77049171228 scopus 로고
    • Chromatographic determination of cysteine as cysteic acid
    • Scharm E., Moore S. and Bigwood E. J. (1954) Chromatographic determination of cysteine as cysteic acid. Biochem. J. 57: 33-37
    • (1954) Biochem. J. , vol.57 , pp. 33-37
    • Scharm, E.1    Moore, S.2    Bigwood, E.J.3
  • 27
    • 0020490670 scopus 로고
    • Human metallothionein genes: Molecular cloning and sequence analysis of the mRNA
    • Karin M. and Richards R. I. (1988) Human metallothionein genes: Molecular cloning and sequence analysis of the mRNA. Nucleic Acids Res. 10: 3165-3173
    • (1988) Nucleic Acids Res. , vol.10 , pp. 3165-3173
    • Karin, M.1    Richards, R.I.2
  • 28
    • 0019878625 scopus 로고
    • Zinc(II), Cadmium(II) and Mercury(II) thiolate transitions in metallothionein
    • Schultze P., Worgotter E., Braun W., Wagner G., Vasak M., Kägi J. H. R. et al. (1988) Zinc(II), Cadmium(II) and Mercury(II) thiolate transitions in metallothionein. Biochemistry 20: 2852-2856
    • (1988) Biochemistry , vol.20 , pp. 2852-2856
    • Schultze, P.1    Worgotter, E.2    Braun, W.3    Wagner, G.4    Vasak, M.5    Kägi, J.H.R.6
  • 29
    • 0020478923 scopus 로고
    • Domain nature of metallothionein
    • Winge D. R. and Miklossy K. A. (1982) Domain nature of metallothionein. J. Biol. Chem. 257: 3471-3475
    • (1982) J. Biol. Chem. , vol.257 , pp. 3471-3475
    • Winge, D.R.1    Miklossy, K.A.2
  • 30
    • 0019527166 scopus 로고
    • On the reactivity of metallothioneins with 5,5′-dithiobis-(2-nitrobenzoic acid)
    • Li T.-Y., Minkel D. T., Shaw C. F. and Petering D. H. (1981) On the reactivity of metallothioneins with 5,5′-dithiobis-(2-nitrobenzoic acid). Biochem. J. 193: 441-446
    • (1981) Biochem. J. , vol.193 , pp. 441-446
    • Li, T.-Y.1    Minkel, D.T.2    Shaw, C.F.3    Petering, D.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.