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Volumn 187, Issue 2, 2000, Pages 127-132

The FAPY-DNA glycosylase (Fpg) is required for survival of the cyanobacterium Synechococcus elongatus under high light irradiance

Author keywords

Cyanobacterium; DNA repair; Fpg protein; Oxidative stress; Photosynthesis; Photosystem I

Indexed keywords

DNA GLYCOSYLTRANSFERASE; REACTIVE OXYGEN METABOLITE;

EID: 17644442715     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(00)00189-0     Document Type: Article
Times cited : (18)

References (20)
  • 1
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • Demple B., Harrison L. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63:1994;915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 2
    • 0032836651 scopus 로고    scopus 로고
    • Initiation of base excision repair: Glycosylase mechanisms and structures
    • McCullough A.K., Dodson M.L., Lloyd R.S. Initiation of base excision repair: glycosylase mechanisms and structures. Annu. Rev. Biochem. 68:1999;255-285.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 255-285
    • McCullough, A.K.1    Dodson, M.L.2    Lloyd, R.S.3
  • 4
    • 0026533905 scopus 로고
    • Substrate specificity of the Escherichia coli Fpg protein (formamydopyrimidine-DNA glycosylase): Excision of purine lesions in DNA produced by ionizing radiation or photosensitization
    • Boiteux S., Gajewski E., Laval J., Dizdaroglu M. Substrate specificity of the Escherichia coli Fpg protein (formamydopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization. Biochemistry. 31:1992;106-110.
    • (1992) Biochemistry , vol.31 , pp. 106-110
    • Boiteux, S.1    Gajewski, E.2    Laval, J.3    Dizdaroglu, M.4
  • 6
    • 0027324378 scopus 로고
    • Mutagenesis by 8-oxoguanine: An enemy within
    • Grollman A.P., Moriya M. Mutagenesis by 8-oxoguanine: an enemy within. Trends Genet. 9:1993;246-249.
    • (1993) Trends Genet. , vol.9 , pp. 246-249
    • Grollman, A.P.1    Moriya, M.2
  • 7
    • 0025909996 scopus 로고
    • Escherichia coli Fpg and UvrABC endonuclease repair DNA damage induced by methylene blue plus visible light in vivo and in vitro
    • Czeczot H., Tudek B., Lambert B., Laval J., Boiteux S. Escherichia coli Fpg and UvrABC endonuclease repair DNA damage induced by methylene blue plus visible light in vivo and in vitro. J. Bacteriol. 173:1993;3419-3424.
    • (1993) J. Bacteriol. , vol.173 , pp. 3419-3424
    • Czeczot, H.1    Tudek, B.2    Lambert, B.3    Laval, J.4    Boiteux, S.5
  • 8
    • 0000682385 scopus 로고
    • Production and scavenging of active oxygen in photosynthesis
    • (Osmond, C.B. and Arntzen, C.J., Eds.) Elsevier Science Publishers, Amsterdam
    • Asada, K. and Takahashi, M. (1987) Production and scavenging of active oxygen in photosynthesis. In: Photoinhibition (Osmond, C.B. and Arntzen, C.J., Eds.), pp. 227-286. Elsevier Science Publishers, Amsterdam.
    • (1987) In: Photoinhibition , pp. 227-286
    • Asada, K.1    Takahashi, M.2
  • 10
    • 0028942512 scopus 로고
    • Repair of oxidative DNA damage in gram-positive bacteria: The Lactococcus lactis Fpg protein
    • Duwat P., de Oliviera R., Ehrlich S.D., Boiteux S. Repair of oxidative DNA damage in gram-positive bacteria: the Lactococcus lactis Fpg protein. Microbiology. 141:1995;411-417.
    • (1995) Microbiology , vol.141 , pp. 411-417
    • Duwat, P.1    De Oliviera, R.2    Ehrlich, S.D.3    Boiteux, S.4
  • 13
    • 0027207845 scopus 로고
    • Genes encoding eleven subunits of photosystem I from the thermophilic cyanobacterium Synechococcus sp.
    • Mühlenhoff U., Haehnel W., Witt H.T., Herrmann R.G. Genes encoding eleven subunits of photosystem I from the thermophilic cyanobacterium Synechococcus sp. Gene. 127:1993;71-78.
    • (1993) Gene , vol.127 , pp. 71-78
    • Mühlenhoff, U.1    Haehnel, W.2    Witt, H.T.3    Herrmann, R.G.4
  • 14
    • 0029904481 scopus 로고    scopus 로고
    • Gene transfer and manipulation in the thermophilic cyanobacterium Synechococcus elongatus
    • Mühlenhoff U., Chauvat F. Gene transfer and manipulation in the thermophilic cyanobacterium Synechococcus elongatus. Mol. Gen. Genet. 252:1996;93-100.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 93-100
    • Mühlenhoff, U.1    Chauvat, F.2
  • 15
    • 0033018137 scopus 로고    scopus 로고
    • Organization and expression of nitrogen-fixing genes in the aerobic nitrogen-fixing unicellular cyanobacterium Synechococcus sp. strain RF-1
    • Huang T.-C., Lin R.-F., Chu M.-C., Cheng H.-M. Organization and expression of nitrogen-fixing genes in the aerobic nitrogen-fixing unicellular cyanobacterium Synechococcus sp. strain RF-1. Microbiology. 145:1999;743-753.
    • (1999) Microbiology , vol.145 , pp. 743-753
    • Huang, T.-C.1    Lin, R.-F.2    Chu, M.-C.3    Cheng, H.-M.4
  • 16
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (1988) Antibodies, A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies, a Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 17
    • 0030614471 scopus 로고    scopus 로고
    • 2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalysed by Escherichia coli formamydopyrimidine-DNA glycosylase (Fpg) protein
    • 2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalysed by Escherichia coli formamydopyrimidine-DNA glycosylase (Fpg) protein. J. Biol. Chem. 272:1997;5335-5341.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5335-5341
    • Zharkov, D.O.1    Rieger, R.A.2    Iden, C.R.3    Grollman, A.P.4
  • 18
    • 0027274754 scopus 로고
    • Cloning and characterization of the psaE gene of the cyanobacterium Synechococcus sp. PCC 7002: Characterization of a psaE mutant and overexpression of the protein in E. coli
    • Zhao Z., Snyder W.L., Mühlenhoff U., Rhiel E., Warren P.V., Golbeck J.H., Bryant D.A. Cloning and characterization of the psaE gene of the cyanobacterium Synechococcus sp. PCC 7002: Characterization of a psaE mutant and overexpression of the protein in E. coli. Mol. Microbiol. 9:1993;183-194.
    • (1993) Mol. Microbiol. , vol.9 , pp. 183-194
    • Zhao, Z.1    Snyder, W.L.2    Mühlenhoff, U.3    Rhiel, E.4    Warren, P.V.5    Golbeck, J.H.6    Bryant, D.A.7
  • 19
    • 0027462131 scopus 로고
    • Fpg protein of Escherichia coli is a zinc-finger whose cysteine residues have a structural and/or functional role
    • O'Conor T.R., Graves R.J., de Murcia G., Castaing B., Laval J. Fpg protein of Escherichia coli is a zinc-finger whose cysteine residues have a structural and/or functional role. J. Biol. Chem. 268:1993;9063-9070.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9063-9070
    • O'Conor, T.R.1    Graves, R.J.2    De Murcia, G.3    Castaing, B.4    Laval, J.5
  • 20
    • 0028972858 scopus 로고
    • Co-transcription of a homologue of the formamidopyrimidine-DNA glycosylase (fpg) and lysophosphatidic acyltransferase (nlaA) in Neisseria meningitidis
    • Swartley J.S., Stevens D.S. Co-transcription of a homologue of the formamidopyrimidine-DNA glycosylase (fpg) and lysophosphatidic acyltransferase (nlaA) in Neisseria meningitidis. FEMS Microbiol. Lett. 134:1995;171-176.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 171-176
    • Swartley, J.S.1    Stevens, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.