메뉴 건너뛰기




Volumn 430, Issue 1, 1999, Pages 99-107

Methionine reduces spontaneous and alkylation-induced mutagenesis in Saccharomyces cerevisiae cells deficient in O6-methylguanine-DNA methyltransferase

Author keywords

Chemoprevention; DNA repair methyltransferase; Mutagenesis; S adenosylmethionine; Yeast

Indexed keywords

ANTIMUTAGENIC AGENT; METHIONINE; METHYLATED DNA PROTEIN CYSTEINE METHYLTRANSFERASE; METHYLNITRONITROSOGUANIDINE; S ADENOSYLMETHIONINE;

EID: 0032737127     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0027-5107(99)00163-3     Document Type: Article
Times cited : (7)

References (48)
  • 2
    • 0023919219 scopus 로고
    • Regulation and expression of the adaptive response to alkylating agents
    • Lindhal L., Sedgwick B., Sekiguchi M., Nakabeppu Y. Regulation and expression of the adaptive response to alkylating agents. Annu. Rev. Biochem. 57:1988;133-157.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 133-157
    • Lindhal, L.1    Sedgwick, B.2    Sekiguchi, M.3    Nakabeppu, Y.4
  • 5
    • 0025980239 scopus 로고
    • 6-methylguanine DNA repair methyltransferase
    • 6-methylguanine DNA repair methyltransferase. J. Bacteriol. 173:1991;2068-2076.
    • (1991) J. Bacteriol. , vol.173 , pp. 2068-2076
    • Rebeck, G.W.1    Samson, L.2
  • 6
    • 0027477075 scopus 로고
    • In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells
    • Xiao W., Samson L. In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells. Proc. Natl. Acad. Sci. U.S.A. 90:1993;2117-2121.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2117-2121
    • Xiao, W.1    Samson, L.2
  • 7
    • 0002951002 scopus 로고
    • S-adenosylmethionine: Present status and future perspectives
    • F. Salvatore, E. Borek, V. Zappia, H.G. Williams-Ashman, & F. Schlenk. New York: Columbia University Press
    • Cantoni G.L. S-adenosylmethionine: present status and future perspectives. Salvatore F., Borek E., Zappia V., Williams-Ashman H.G., Schlenk F. The Biochemistry of Adenosylmethionine. 1977;557-577 Columbia University Press, New York.
    • (1977) The Biochemistry of Adenosylmethionine , pp. 557-577
    • Cantoni, G.L.1
  • 8
    • 0020324376 scopus 로고
    • Non-enzymatic methylation of DNA by S-adenosylmethionine in vitro
    • Barrows L.R., Magee P.N. Non-enzymatic methylation of DNA by S-adenosylmethionine in vitro. Carcinogenesis. 3:1982;349-351.
    • (1982) Carcinogenesis , vol.3 , pp. 349-351
    • Barrows, L.R.1    Magee, P.N.2
  • 9
    • 0020341190 scopus 로고
    • Non-enzymatic methylation of DNA by the intracellular methyl group donor S-adenosyl-L-methionine is a potentially mutagenic reaction
    • Rydberg B., Lindahl T. Non-enzymatic methylation of DNA by the intracellular methyl group donor S-adenosyl-L-methionine is a potentially mutagenic reaction. EMBO J. 2:1982;211-216.
    • (1982) EMBO J. , vol.2 , pp. 211-216
    • Rydberg, B.1    Lindahl, T.2
  • 10
    • 0014672640 scopus 로고
    • 6 alkylation of deoxyguanine to the mutagenicity and carcinogenicity of nitrosamines and nitrosamides
    • 6 alkylation of deoxyguanine to the mutagenicity and carcinogenicity of nitrosamines and nitrosamides. Nature. 223:1966;206-207.
    • (1966) Nature , vol.223 , pp. 206-207
    • Loveless, A.1
  • 11
    • 0025288239 scopus 로고
    • Distribution of methyl and ethyl adducts following alkylation with monofunctional alkylating agents
    • Beranek D.T. Distribution of methyl and ethyl adducts following alkylation with monofunctional alkylating agents. Mutat. Res. 231:1990;11-30.
    • (1990) Mutat. Res. , vol.231 , pp. 11-30
    • Beranek, D.T.1
  • 12
    • 0021894988 scopus 로고
    • 6-methylguanine-DNA methyltransferase in cell survival, mutagenesis and carcinogenesis
    • 6-methylguanine-DNA methyltransferase in cell survival, mutagenesis and carcinogenesis. Mutat. Res. 145:1985;1-16.
    • (1985) Mutat. Res. , vol.145 , pp. 1-16
    • Yarosh, D.B.1
  • 13
    • 0023070001 scopus 로고
    • 6-methylguanine in human cell killing, sister chromatid exchange induction and mutagenesis: A review
    • 6-methylguanine in human cell killing, sister chromatid exchange induction and mutagenesis: a review. J. Cell Sci. Suppl. 6:1987;333-353.
    • (1987) J. Cell Sci. Suppl. , vol.6 , pp. 333-353
    • Day R.S. III1    Babich, M.A.2    Yarosh, D.B.3    Scudiero, D.A.4
  • 14
    • 0023244832 scopus 로고
    • Lack of mutagenic activity of adenosylmethionine in vitro and in vivo
    • Pezzoli C., Galli-Kienle M., Stramentinoli G. Lack of mutagenic activity of adenosylmethionine in vitro and in vivo. Arzneim.-Forsch. 37:1987;826-829.
    • (1987) Arzneim.-Forsch. , vol.37 , pp. 826-829
    • Pezzoli, C.1    Galli-Kienle, M.2    Stramentinoli, G.3
  • 16
    • 0013905989 scopus 로고
    • Methods for the analysis and preparation of adenosylmethionine and adenosylhomocysteine
    • Shapiro S.K., Ehninger D.J. Methods for the analysis and preparation of adenosylmethionine and adenosylhomocysteine. Anal. Biochem. 15:1966;323-333.
    • (1966) Anal. Biochem. , vol.15 , pp. 323-333
    • Shapiro, S.K.1    Ehninger, D.J.2
  • 17
    • 0018199041 scopus 로고
    • Measuring spontaneous mutation rates in yeast
    • von Borstel R.C. Measuring spontaneous mutation rates in yeast. Methods Cell. Biol. 20:1978;1-24.
    • (1978) Methods Cell. Biol. , vol.20 , pp. 1-24
    • Von Borstel, R.C.1
  • 18
    • 0032510731 scopus 로고    scopus 로고
    • MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway
    • Broomfield S., Chow B.L., Xiao W. MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway. Proc. Natl. Acad. Sci. U.S.A. 95:1998;5678-5683.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5678-5683
    • Broomfield, S.1    Chow, B.L.2    Xiao, W.3
  • 20
    • 0017841141 scopus 로고
    • S-adenosylmethionine requiring mutants in Saccharomyces cerevisiae: Evidence for the existence of two methionine adenosyl transferases
    • Cherest H., Surdin-Kerjan Y. S-adenosylmethionine requiring mutants in Saccharomyces cerevisiae: evidence for the existence of two methionine adenosyl transferases. Mol. Gen. Genet. 163:1978;153-167.
    • (1978) Mol. Gen. Genet. , vol.163 , pp. 153-167
    • Cherest, H.1    Surdin-Kerjan, Y.2
  • 21
    • 0023646110 scopus 로고
    • SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae
    • Thomas D., Surdin-Kerjan Y. SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae. J. Biol. Chem. 262:1978;16704-16709.
    • (1978) J. Biol. Chem. , vol.262 , pp. 16704-16709
    • Thomas, D.1    Surdin-Kerjan, Y.2
  • 22
    • 0024267104 scopus 로고
    • SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: Physiology and regulation of both enzymes
    • Thomas D., Rothstein R., Rosenberg N., Surdin-Kerjan Y. SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: physiology and regulation of both enzymes. Mol. Cell. Biol. 8:1988;5132-5139.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5132-5139
    • Thomas, D.1    Rothstein, R.2    Rosenberg, N.3    Surdin-Kerjan, Y.4
  • 23
    • 0015632377 scopus 로고
    • S-adenosylmethionine-mediated repression of methionine biosynthetic enzymes in Saccharomyces cerevisiae
    • Cherest H., Surdin-Kerjan Y., Antoniewski J., Robichon-Szulmajster H. S-adenosylmethionine-mediated repression of methionine biosynthetic enzymes in Saccharomyces cerevisiae. J. Bacteriol. 114:1973;928-933.
    • (1973) J. Bacteriol. , vol.114 , pp. 928-933
    • Cherest, H.1    Surdin-Kerjan, Y.2    Antoniewski, J.3    Robichon-Szulmajster, H.4
  • 24
    • 0344074804 scopus 로고
    • The formation of S-adenosylmethionine in yeast
    • Schlenk F., DePalma R.E. The formation of S-adenosylmethionine in yeast. J. Biol. Chem. 229:1957;1037-1050.
    • (1957) J. Biol. Chem. , vol.229 , pp. 1037-1050
    • Schlenk, F.1    Depalma, R.E.2
  • 25
    • 0004732033 scopus 로고
    • Cloning a eukaryotic DNA glycosylase repair gene by the suppression of a DNA repair defect in Escherichia coli
    • Chen J., Derfler B., Maskati A., Samson L. Cloning a eukaryotic DNA glycosylase repair gene by the suppression of a DNA repair defect in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 86:1989;7961-7965.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7961-7965
    • Chen, J.1    Derfler, B.2    Maskati, A.3    Samson, L.4
  • 26
    • 0025324303 scopus 로고
    • The yeast structural gene (APN1) for the major apurinic endonuclease: Homology to E. coli endonuclease IV
    • Popoff S.C., Spira A.S., Johnson A.W., Demple B. The yeast structural gene (APN1) for the major apurinic endonuclease: homology to E. coli endonuclease IV. Proc. Natl. Acad. Sci. U.S.A. 87:1990;4193-4197.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4193-4197
    • Popoff, S.C.1    Spira, A.S.2    Johnson, A.W.3    Demple, B.4
  • 27
    • 0025864553 scopus 로고
    • Cellular role of yeast APN1 apurinic endonuclease/3′-diesterase: Repair of oxidative and alkylation DNA damage and control of spontaneous mutation
    • Ramotar D., Popoff S.C., Gralla E.B., Demple B. Cellular role of yeast APN1 apurinic endonuclease/3′-diesterase: repair of oxidative and alkylation DNA damage and control of spontaneous mutation. Mol. Cell Biol. 9:1991;4537-4544.
    • (1991) Mol. Cell Biol. , vol.9 , pp. 4537-4544
    • Ramotar, D.1    Popoff, S.C.2    Gralla, E.B.3    Demple, B.4
  • 28
    • 0025195404 scopus 로고
    • 6-alkylguanine-DNA alkyltransferase: Regulation and importance in response to alkylating carcinogenic and therapeutic agents
    • 6-alkylguanine-DNA alkyltransferase: regulation and importance in response to alkylating carcinogenic and therapeutic agents. Cancer Res. 50:1990;6119-6129.
    • (1990) Cancer Res. , vol.50 , pp. 6119-6129
    • Pegg, A.E.1
  • 30
    • 0022807809 scopus 로고
    • 4-methylthymine in vivo determined by an enzymatic approach to site-specific mutagenesis
    • 4-methylthymine in vivo determined by an enzymatic approach to site-specific mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 83:1986;8501-8505.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8501-8505
    • Preston, B.D.1    Singer, B.2    Loeb, L.A.3
  • 31
    • 0026650587 scopus 로고
    • The Saccharomyces cerevisiae MGT1 DNA repair methyltransferase gene: Its promoter and entire coding sequence, regulation and in vivo biological functions
    • Xiao W., Samson L. The Saccharomyces cerevisiae MGT1 DNA repair methyltransferase gene: its promoter and entire coding sequence, regulation and in vivo biological functions. Nucleic Acids Res. 20:1992;3599-3606.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3599-3606
    • Xiao, W.1    Samson, L.2
  • 32
    • 0023015325 scopus 로고
    • Mutagenesis by apurinic/apyrimidinic sites
    • Loeb L.A., Preston B.D. Mutagenesis by apurinic/apyrimidinic sites. Annu. Rev. Genet. 20:1986;201-230.
    • (1986) Annu. Rev. Genet. , vol.20 , pp. 201-230
    • Loeb, L.A.1    Preston, B.D.2
  • 33
    • 0025321703 scopus 로고
    • Adaptive response induction by bacterial catalysis of nitrosation
    • Tsimis J., Yarosh D.B. Adaptive response induction by bacterial catalysis of nitrosation. Environ. Mol. Mutat. 15:1990;69-70.
    • (1990) Environ. Mol. Mutat. , vol.15 , pp. 69-70
    • Tsimis, J.1    Yarosh, D.B.2
  • 34
    • 0023841337 scopus 로고
    • Interaction of lipid peroxidation products with DNA. A review
    • Vaca C.E., Wilhelm J., Harms-Ringdahl M. Interaction of lipid peroxidation products with DNA. A review. Mutat. Res. 195:1988;137-149.
    • (1988) Mutat. Res. , vol.195 , pp. 137-149
    • Vaca, C.E.1    Wilhelm, J.2    Harms-Ringdahl, M.3
  • 35
    • 0029810398 scopus 로고    scopus 로고
    • Generation of an endogenous DNA-methylating agent by nitrosation in E. coli
    • Taverna P., Sedgwick B. Generation of an endogenous DNA-methylating agent by nitrosation in E. coli. J. Bacteriol. 178:1996;5105-5111.
    • (1996) J. Bacteriol. , vol.178 , pp. 5105-5111
    • Taverna, P.1    Sedgwick, B.2
  • 37
    • 0024506292 scopus 로고
    • Inhibition of promotion and persistent nodule growth by S-adenosyl-L-methionine in rat liver carcinogenesis: Role of remodelling and apoptosis
    • Garcea R., Daino L., Pascale R.M., Similie M.M., Puddu M., Frassetto S., Cozzolino P., Seddaiu M.A., Gaspa L., Feo F. Inhibition of promotion and persistent nodule growth by S-adenosyl-L-methionine in rat liver carcinogenesis: role of remodelling and apoptosis. Cancer Res. 49:1989;1850-1856.
    • (1989) Cancer Res. , vol.49 , pp. 1850-1856
    • Garcea, R.1    Daino, L.2    Pascale, R.M.3    Similie, M.M.4    Puddu, M.5    Frassetto, S.6    Cozzolino, P.7    Seddaiu, M.A.8    Gaspa, L.9    Feo, F.10
  • 39
    • 0029987613 scopus 로고    scopus 로고
    • Persistent chemopreventive effect of S-adenosyl-L-methionine on the development of liver putative neoplastic lesions induced by thiobenzamide in diethylnitrosamine-initiated rats
    • Similie M.M., Saviozzi M., De Miglio M.R., Muroni M.R., Nufris A., Pascale P.M., Malvadi G., Feo F. Persistent chemopreventive effect of S-adenosyl-L-methionine on the development of liver putative neoplastic lesions induced by thiobenzamide in diethylnitrosamine-initiated rats. Carcinogenesis. 17:1996;1533-1537.
    • (1996) Carcinogenesis , vol.17 , pp. 1533-1537
    • Similie, M.M.1    Saviozzi, M.2    De Miglio, M.R.3    Muroni, M.R.4    Nufris, A.5    Pascale, P.M.6    Malvadi, G.7    Feo, F.8
  • 42
    • 0030442652 scopus 로고    scopus 로고
    • The relationship of DNA methylation to cancer
    • Lindahl T. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Bird A.P. The relationship of DNA methylation to cancer. Lindahl T. Genetic Instability in Cancer. Cancer Surveys. 28:1996;87-101 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1996) Genetic Instability in Cancer. Cancer Surveys , vol.28 , pp. 87-101
    • Bird, A.P.1
  • 44
    • 0017822860 scopus 로고
    • The effect of homocysteine, methionine, serine and glycine on DNA synthesis by human normoblastic and megaloblastic bone marrow cells
    • Taguchi H., Chanarin I. The effect of homocysteine, methionine, serine and glycine on DNA synthesis by human normoblastic and megaloblastic bone marrow cells. J. Nutr. Sci. Vitaminol. 24:1978;83-89.
    • (1978) J. Nutr. Sci. Vitaminol. , vol.24 , pp. 83-89
    • Taguchi, H.1    Chanarin, I.2
  • 45
    • 0030442815 scopus 로고    scopus 로고
    • Many mutations in cancers
    • Lindahl T. Cold Spring Harbor, NY: Cold Spring Harbor Laboraroty Press
    • Loeb L.A. Many mutations in cancers. Lindahl T. Genetic Instability in Cancer. Cancer Surveys. 28:1996;329-342 Cold Spring Harbor Laboraroty Press, Cold Spring Harbor, NY.
    • (1996) Genetic Instability in Cancer. Cancer Surveys , vol.28 , pp. 329-342
    • Loeb, L.A.1
  • 47
    • 0027138012 scopus 로고
    • Chemical carcinogenesis in methyl-deficient rats
    • Rogers A.E. Chemical carcinogenesis in methyl-deficient rats. J. Nutr. Biochem. 4:1993;666-671.
    • (1993) J. Nutr. Biochem. , vol.4 , pp. 666-671
    • Rogers, A.E.1
  • 48
    • 0025630512 scopus 로고
    • Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to the AlkA glycosylase of E. coli and is induced in response to DNA alkylation damage
    • Chen J., Derfler B., Samson L. Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to the AlkA glycosylase of E. coli and is induced in response to DNA alkylation damage. EMBO J. 9:1990;4569-4575.
    • (1990) EMBO J. , vol.9 , pp. 4569-4575
    • Chen, J.1    Derfler, B.2    Samson, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.