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Volumn 21, Issue 5, 2000, Pages 1051-1057

Cadmium mutagenicity and human nucleotide excision repair protein XPA: CD, EXAFS and 1H/15N-NMR spectroscopic studies on the zinc(II)- and cadmium(II)-associated minimal DNA-binding domain (M98-F219)

Author keywords

[No Author keywords available]

Indexed keywords

CADMIUM; CYSTEINE; DNA; DNA BINDING PROTEIN; GLYCEROL; NITROGEN 15; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; SULFUR; ZINC;

EID: 0034118938     PISSN: 01433334     EISSN: None     Source Type: Journal    
DOI: 10.1093/carcin/21.5.1051     Document Type: Article
Times cited : (49)

References (61)
  • 1
    • 0001415829 scopus 로고
    • Xeroderma pigmentosum and cockayne syndrome
    • Scriver, S.C., Beaudet, A.L., Sly, W.S. and Valle, D. (eds) McGraw-Hill, New York
    • Cleaver, J.E. and Kraemer, K.H. (1989) Xeroderma pigmentosum and cockayne syndrome. In Scriver, S.C., Beaudet, A.L., Sly, W.S. and Valle, D. (eds) The Metabolic Basis of Inherited Disease. McGraw-Hill, New York, pp. 4393-4419.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 4393-4419
    • Cleaver, J.E.1    Kraemer, K.H.2
  • 3
    • 0029001182 scopus 로고
    • DNA excision repair
    • Sancar, A. (1995) DNA excision repair. J. Biol. Chem., 270, 15915-15918.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15915-15918
    • Sancar, A.1
  • 4
    • 0030768038 scopus 로고    scopus 로고
    • Nucleotide excision repair in mammalian cells
    • Wood, R.D. (1997) Nucleotide excision repair in mammalian cells. J. Biol. Chem., 272, 23454-23468.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23454-23468
    • Wood, R.D.1
  • 5
    • 0029870677 scopus 로고    scopus 로고
    • Reaction mechanism of human DNA repair excision nuclease
    • Mu, D., Hsu, D.S. and Sancar, A. (1996) Reaction mechanism of human DNA repair excision nuclease. J. Biol. Chem., 271, 8285-8294.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8285-8294
    • Mu, D.1    Hsu, D.S.2    Sancar, A.3
  • 6
    • 0030723714 scopus 로고    scopus 로고
    • The DNA damage-recognition problem in human and other eukaryotic cells: The XPA damage binding protein
    • Cleaver, J.E. and States, J.C. (1997) The DNA damage-recognition problem in human and other eukaryotic cells: the XPA damage binding protein. Biochem. J., 328, 1-12.
    • (1997) Biochem. J. , vol.328 , pp. 1-12
    • Cleaver, J.E.1    States, J.C.2
  • 7
    • 0026076553 scopus 로고
    • Complementation of DNA repair in xeroderma pigmentosum group A cell extracts by a protein with affinity for damaged DNA
    • Robins, P., Jones, C.J., Biggerstaff, M., Lindahl, T. and Wood, R.D. (1991) Complementation of DNA repair in xeroderma pigmentosum group A cell extracts by a protein with affinity for damaged DNA. EMBO J., 10, 3913-3921.
    • (1991) EMBO J. , vol.10 , pp. 3913-3921
    • Robins, P.1    Jones, C.J.2    Biggerstaff, M.3    Lindahl, T.4    Wood, R.D.5
  • 8
    • 0027483739 scopus 로고
    • Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA
    • Jones, C.J. and Wood, R.D. (1993) Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA. Biochemistry, 32, 12096-12104.
    • (1993) Biochemistry , vol.32 , pp. 12096-12104
    • Jones, C.J.1    Wood, R.D.2
  • 11
    • 0028932889 scopus 로고
    • The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor
    • Park, C.-H., Mu, D., Reardon, J.T. and Sancar, A. (1995) The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor. J. Biol. Chem., 270, 4896-4901.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4896-4901
    • Park, C.-H.1    Mu, D.2    Reardon, J.T.3    Sancar, A.4
  • 13
    • 0033603338 scopus 로고    scopus 로고
    • Order of assembly of human DNA repair excision nuclease
    • Wakasugi, M. and Sancar, A. (1999) Order of assembly of human DNA repair excision nuclease. J Biol. Chem., 274, 18759-18768.
    • (1999) J Biol. Chem. , vol.274 , pp. 18759-18768
    • Wakasugi, M.1    Sancar, A.2
  • 16
    • 0032102927 scopus 로고    scopus 로고
    • Structural features of the minimal DNA binding domain (M98-F219) of human nucleotide excision repair protein XPA
    • Buchko, G.W., Ni, S., Thrall, B.D. and Kennedy, M.A. (1998) Structural features of the minimal DNA binding domain (M98-F219) of human nucleotide excision repair protein XPA. Nucleic Acids Res., 26, 2779-2788.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2779-2788
    • Buchko, G.W.1    Ni, S.2    Thrall, B.D.3    Kennedy, M.A.4
  • 19
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology. A growing appreciation of the roles of zinc
    • Berg, J.M. and Shi, Y. (1996) The galvanization of biology. A growing appreciation of the roles of zinc. Science, 271, 1081-1086.
    • (1996) Science , vol.271 , pp. 1081-1086
    • Berg, J.M.1    Shi, Y.2
  • 20
    • 0026625629 scopus 로고
    • Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein
    • Miyamoto, I., Miura, N., Niwa, H., Miyazaki, J. and Tanaka, K. (1992) Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein. J. Biol. Chem., 67, 12182-12187.
    • (1992) J. Biol. Chem. , vol.67 , pp. 12182-12187
    • Miyamoto, I.1    Miura, N.2    Niwa, H.3    Miyazaki, J.4    Tanaka, K.5
  • 22
    • 0030039165 scopus 로고    scopus 로고
    • Substitution of cadmium for zinc in farnesyl:Protein transferase alters its substrate specificity
    • Zhang, F.L., Fu, H.-W., Casey, P.J. and Bishop, W.R. (1996) Substitution of cadmium for zinc in farnesyl:protein transferase alters its substrate specificity. Biochemistry, 35, 8166-8171.
    • (1996) Biochemistry , vol.35 , pp. 8166-8171
    • Zhang, F.L.1    Fu, H.-W.2    Casey, P.J.3    Bishop, W.R.4
  • 23
    • 0000349342 scopus 로고
    • Beryllium, Cadmium, Mercury, and Exposures in the Glass Manufacturing Industry
    • International Agency for Research on Cancer, Lyon
    • IARC (1993) Beryllium, Cadmium, Mercury, and Exposures in the Glass Manufacturing Industry. Monographs on the Evaluation of Carcinogenic Risks to Humans, Vol. 58. International Agency for Research on Cancer, Lyon.
    • (1993) Monographs on the Evaluation of Carcinogenic Risks to Humans , vol.58
  • 24
    • 0024447941 scopus 로고
    • Comutagenicity and inhibition of DNA repair by metal ions in mammalian cells
    • Hartwig, A. and Beyersmann, D. (1989) Comutagenicity and inhibition of DNA repair by metal ions in mammalian cells. Biol Trace Elem. Res., 21, 359-365.
    • (1989) Biol Trace Elem. Res. , vol.21 , pp. 359-365
    • Hartwig, A.1    Beyersmann, D.2
  • 25
    • 0023665633 scopus 로고
    • Inhibition of DNA replication and repair by cadmium in mammalian cells. Protective interaction of zinc
    • Nocentini, S. (1987) Inhibition of DNA replication and repair by cadmium in mammalian cells. Protective interaction of zinc. Nucleic Acids Res., 15, 4211-4225.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 4211-4225
    • Nocentini, S.1
  • 26
    • 0031843623 scopus 로고    scopus 로고
    • Disturbance of DNA damage recognition after UV-irradiation by nickel (II) and cadmium (II) in mammalian cells
    • Hartmann, M. and Hartwig, A. (1998) Disturbance of DNA damage recognition after UV-irradiation by nickel (II) and cadmium (II) in mammalian cells. Carcinogenesis, 19, 617-621.
    • (1998) Carcinogenesis , vol.19 , pp. 617-621
    • Hartmann, M.1    Hartwig, A.2
  • 27
    • 85173889103 scopus 로고    scopus 로고
    • Cadmium carcinogenicity and genotoxicity
    • Chang, L.W, Magos, L. and Suzuki, T. (eds) CRC Press, Boca Raton, FL
    • Waalkes, M.P. and Misra, R.R. (1996) Cadmium carcinogenicity and genotoxicity. In Chang, L.W, Magos, L. and Suzuki, T. (eds) Toxicology of Metals. CRC Press, Boca Raton, FL, pp. 231-243.
    • (1996) Toxicology of Metals , pp. 231-243
    • Waalkes, M.P.1    Misra, R.R.2
  • 28
    • 0028812499 scopus 로고
    • Current aspects in metal genotoxicity
    • Hartwig, A. (1995) Current aspects in metal genotoxicity. Biometals, 8, 3-11.
    • (1995) Biometals , vol.8 , pp. 3-11
    • Hartwig, A.1
  • 29
    • 0031693584 scopus 로고    scopus 로고
    • Human nucleotide excision repair protein XPA: Extended X-ray absorption fine-structure evidence for a metal-binding domain
    • Hess, N.J., Buchko, G.W., Conradson, S.D., Espinosa, F.J., Ni, S., Thrall, B.D. and Kennedy, M.A. (1998) Human nucleotide excision repair protein XPA: extended X-ray absorption fine-structure evidence for a metal-binding domain. Protein Sci., 7, 1970-1975.
    • (1998) Protein Sci. , vol.7 , pp. 1970-1975
    • Hess, N.J.1    Buchko, G.W.2    Conradson, S.D.3    Espinosa, F.J.4    Ni, S.5    Thrall, B.D.6    Kennedy, M.A.7
  • 32
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlated spectroscopy with improved sensitivity
    • Kay, L.E., Keifer, P. and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlated spectroscopy with improved sensitivity. J. Am. Chem. Soc., 114, 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 33
    • 0028541866 scopus 로고
    • 3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biol. NMR, 4, 845-858.
    • (1994) J. Biol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 34
    • 11344291497 scopus 로고
    • The ultraviolet circular dichroism of polypeptides
    • Holzwarth, G.M. and Doty, P. (1965) The ultraviolet circular dichroism of polypeptides. J. Am. Chem. Soc., 87, 218-228.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 218-228
    • Holzwarth, G.M.1    Doty, P.2
  • 35
    • 0020184861 scopus 로고
    • Experimental errors and their effect on analyzing circular dichroism spectra of proteins
    • Hennessey, J.P. Jr and Johnson, W.C. Jr (1982) Experimental errors and their effect on analyzing circular dichroism spectra of proteins. Anal. Biochem., 125, 177-188.
    • (1982) Anal. Biochem. , vol.125 , pp. 177-188
    • Hennessey J.P., Jr.1    Johnson W.C., Jr.2
  • 36
    • 0025752606 scopus 로고
    • Side chain backbone hydrogen bonding contributes to helix stability in peptides derived from an α-helical region of carboxypeptidase A
    • Bruch, M.D., Dhingra, M.M. and Gierasch, L.M. (1991) Side chain backbone hydrogen bonding contributes to helix stability in peptides derived from an α-helical region of carboxypeptidase A. Proteins: Struct. Funct. Genet., 10, 130-139.
    • (1991) Proteins: Struct. Funct. Genet. , vol.10 , pp. 130-139
    • Bruch, M.D.1    Dhingra, M.M.2    Gierasch, L.M.3
  • 37
    • 0027180807 scopus 로고
    • Conformational behavior of Escherichia coli Omp A signal peptides in membrane mimetic environments
    • Rizo, J., Blanco, F.J., Kobe, B., Bruch, M.D. and Gierasch, L.M. (1993) Conformational behavior of Escherichia coli Omp A signal peptides in membrane mimetic environments. Biochemistry, 32, 4881-4894.
    • (1993) Biochemistry , vol.32 , pp. 4881-4894
    • Rizo, J.1    Blanco, F.J.2    Kobe, B.3    Bruch, M.D.4    Gierasch, L.M.5
  • 40
    • 0024441308 scopus 로고
    • Evidence from extended X-ray absorption fine structure and site-specific mutagenesis for zinc fingers in uvrA protein of Escherichia coli
    • Navaratnam, S., Myles, G.M., Strange, R.W. and Sancar, A. (1989) Evidence from extended X-ray absorption fine structure and site-specific mutagenesis for zinc fingers in uvrA protein of Escherichia coli. J. Biol. Chem., 264, 16067-16071.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16067-16071
    • Navaratnam, S.1    Myles, G.M.2    Strange, R.W.3    Sancar, A.4
  • 41
    • 0029590007 scopus 로고
    • Structure of binary and ternary complexes of zinc and cobalt carboxypeptidase A as determined by X-ray absorption fine structure
    • Zhang, K. and Auld, D.S. (1995) Structure of binary and ternary complexes of zinc and cobalt carboxypeptidase A as determined by X-ray absorption fine structure. Biochemistry, 34, 16306-16312.
    • (1995) Biochemistry , vol.34 , pp. 16306-16312
    • Zhang, K.1    Auld, D.S.2
  • 42
    • 0030456521 scopus 로고    scopus 로고
    • Effect of pH and ligand binding on the structure of the Cu site of the Met121Glu mutant of azurin from Pseudomonas aeruginosa
    • Strange, R.W., Murphy, L.M., Karlsson, B.G., Reinhammar, B. and Hasnain, S.S. (1996) Effect of pH and ligand binding on the structure of the Cu site of the Met121Glu mutant of azurin from Pseudomonas aeruginosa. Biochemistry, 34, 16391-16398.
    • (1996) Biochemistry , vol.34 , pp. 16391-16398
    • Strange, R.W.1    Murphy, L.M.2    Karlsson, B.G.3    Reinhammar, B.4    Hasnain, S.S.5
  • 43
    • 0033534763 scopus 로고    scopus 로고
    • Extended X-ray absorption fine structure evidence for a single metal binding domain in Xenopus laevis nucleotide excision repair protein XPA
    • Buchko, G.W., Iakoucheva, L.M., Kennedy, M.A., Ackerman, E.J. and Hess, N.J. (1999) Extended X-ray absorption fine structure evidence for a single metal binding domain in Xenopus laevis nucleotide excision repair protein XPA. Biochem. Biophys. Res. Commun., 254, 109-113.
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 109-113
    • Buchko, G.W.1    Iakoucheva, L.M.2    Kennedy, M.A.3    Ackerman, E.J.4    Hess, N.J.5
  • 44
    • 0022355660 scopus 로고
    • Nature of the cadmium sites in rat liver metallothionein 1 from Cd K-edge EXAFS
    • Abrahams, I.L., Garner, C.D., Bremmer, I., Diakun, G.P. and Hasnain, S.S. (1985) Nature of the cadmium sites in rat liver metallothionein 1 from Cd K-edge EXAFS. J. Am. Chem. Soc., 107, 4596-4597.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 4596-4597
    • Abrahams, I.L.1    Garner, C.D.2    Bremmer, I.3    Diakun, G.P.4    Hasnain, S.S.5
  • 48
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S.B., Hajduk, P.J., Meadows, R.P. and Fesik, S.W. (1996) Discovering high-affinity ligands for proteins: SAR by NMR. Science, 274, 1531-1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 49
    • 0030133842 scopus 로고    scopus 로고
    • Implications of the zinc-finger motif found in the DNA-binding domain of the human XPA protein
    • Morita, E.H., Ohkubo, T., Kuraoko, I., Shirakawa, M., Tanaka, K. and Morikawa, K. (1996) Implications of the zinc-finger motif found in the DNA-binding domain of the human XPA protein. Genes Cells, 1, 437-442.
    • (1996) Genes Cells , vol.1 , pp. 437-442
    • Morita, E.H.1    Ohkubo, T.2    Kuraoko, I.3    Shirakawa, M.4    Tanaka, K.5    Morikawa, K.6
  • 50
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D.S., Sykes, B.D. and Richards, F.M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry, 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 51
  • 52
    • 0032910982 scopus 로고    scopus 로고
    • Resonance assignments, solution structure, and backbone dynamics of the DNA- and RPA-binding domain of human repair factor XPA
    • Ikegami, T., Kuroaka, I., Saijo, M., Kodo, N., Kyogoku, Y., Morikawa, K., Tanaka, K. and Shirakawa, M. (1999) Resonance assignments, solution structure, and backbone dynamics of the DNA- and RPA-binding domain of human repair factor XPA. J. Biochem., 125, 495-506.
    • (1999) J. Biochem. , vol.125 , pp. 495-506
    • Ikegami, T.1    Kuroaka, I.2    Saijo, M.3    Kodo, N.4    Kyogoku, Y.5    Morikawa, K.6    Tanaka, K.7    Shirakawa, M.8
  • 53
    • 21844437785 scopus 로고
    • Hydrogen-bond geometry in organic crystals
    • Taylor, R. and Kennard, O. (1984) Hydrogen-bond geometry in organic crystals. Acc. Chem. Res., 17, 320-326.
    • (1984) Acc. Chem. Res. , vol.17 , pp. 320-326
    • Taylor, R.1    Kennard, O.2
  • 54
    • 0342996701 scopus 로고
    • Acids and bases
    • Pearson, G.K. (1966) Acids and bases. Science, 151, 172-177.
    • (1966) Science , vol.151 , pp. 172-177
    • Pearson, G.K.1
  • 55
    • 0001505616 scopus 로고
    • Ligand variation and metal ion binding specificity in zinc finger peptides
    • Krizek, B.A., Merkle, D.L. and Berg, J.M. (1993) Ligand variation and metal ion binding specificity in zinc finger peptides. Inorg. Chem., 32, 937-940.
    • (1993) Inorg. Chem. , vol.32 , pp. 937-940
    • Krizek, B.A.1    Merkle, D.L.2    Berg, J.M.3
  • 56
    • 0030465869 scopus 로고    scopus 로고
    • Negative interference of metal (II) ions with nucleotide excision repair in human cell-free extracts
    • Calsou, P., Frit, P., Bozzato, C. and Salles, B. (1996) Negative interference of metal (II) ions with nucleotide excision repair in human cell-free extracts. Carcinogenesis, 17, 2779-2782.
    • (1996) Carcinogenesis , vol.17 , pp. 2779-2782
    • Calsou, P.1    Frit, P.2    Bozzato, C.3    Salles, B.4
  • 57
    • 0017173641 scopus 로고
    • Infidelity of DNA synthesis in vitro: Screening for potential metal mutagens and carcinogens
    • Sirover, M.A. and Loeb, L.A. (1976) Infidelity of DNA synthesis in vitro: screening for potential metal mutagens and carcinogens. Science, 194, 1434-1436.
    • (1976) Science , vol.194 , pp. 1434-1436
    • Sirover, M.A.1    Loeb, L.A.2
  • 58
    • 0011970056 scopus 로고
    • Interactions of metal ions with nucleic acids
    • Sigel, H. (ed.) Dekker, New York
    • Duane, M. (1974) Interactions of metal ions with nucleic acids. In Sigel, H. (ed.) Metal Ions in Biological Systems. Dekker, New York, pp. 1-43.
    • (1974) Metal Ions in Biological Systems , pp. 1-43
    • Duane, M.1
  • 59
    • 0021179711 scopus 로고
    • In vitro cadmium-DNA interactions: Cooperatively of cadmium binding and competitive antagonism by calcium, magnesium, and zinc
    • Waalkes, M.P. and Poirier, L.A. (1984) In vitro cadmium-DNA interactions: cooperatively of cadmium binding and competitive antagonism by calcium, magnesium, and zinc. Toxicol. Appl. Pharmacol., 75, 539-546.
    • (1984) Toxicol. Appl. Pharmacol. , vol.75 , pp. 539-546
    • Waalkes, M.P.1    Poirier, L.A.2
  • 61
    • 85173799200 scopus 로고    scopus 로고
    • Oxidative DNA damage in metal-induced carcinogenesis
    • Chang, L.W., Magos, L. and Suzuki, T. (eds) CRC Press, Boca Raton, FL
    • Kasprzak, K.S. (1996) Oxidative DNA damage in metal-induced carcinogenesis. In Chang, L.W., Magos, L. and Suzuki, T. (eds) Toxicology of Metals. CRC Press, Boca Raton, FL, pp. 299-320.
    • (1996) Toxicology of Metals , pp. 299-320
    • Kasprzak, K.S.1


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