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Volumn 9, Issue 10, 1999, Pages 531-534

Thermostable uracil-DNA glycosylase from Thermotoga maritima, a member of a novel class of DNA repair enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEA; BACTERIA (MICROORGANISMS); DEINOCOCCUS RADIODURANS; ESCHERICHIA COLI; EUKARYOTA; PROKARYOTA; RICKETTSIA; RICKETTSIA PROWAZEKII; THERMOTOGA MARITIMA; TREPONEMA;

EID: 0033587149     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80237-1     Document Type: Article
Times cited : (65)

References (24)
  • 2
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan HE, Standal R, Slupphaug G: DNA glycosylases in the base excision repair of DNA. Biochem J 1997, 325:1-16.
    • (1997) Biochem J , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 3
    • 0030979263 scopus 로고    scopus 로고
    • DNA glycosylases
    • Cunningham RP: DNA glycosylases. Mutation Res 1997, 383:189-196.
    • (1997) Mutation Res , vol.383 , pp. 189-196
    • Cunningham, R.P.1
  • 4
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T: Instability and decay of the primary structure of DNA. Nature 1993, 362:709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 5
    • 0013608322 scopus 로고    scopus 로고
    • Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA
    • Tye BK, Nyman PO, Lehman IR, Hochhauser S, Weiss B: Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA. Proc Natl Acad Sci USA 1997, 74:154-157.
    • (1997) Proc Natl Acad Sci USA , vol.74 , pp. 154-157
    • Tye, B.K.1    Nyman, P.O.2    Lehman, I.R.3    Hochhauser, S.4    Weiss, B.5
  • 7
    • 0020526545 scopus 로고
    • Base excision repair in the thermophile Thermus sp. strain X-1
    • Warner HR: Base excision repair in the thermophile Thermus sp. strain X-1. J Bacteriol 1983, 154:1451-1454.
    • (1983) J Bacteriol , vol.154 , pp. 1451-1454
    • Warner, H.R.1
  • 8
    • 0030272402 scopus 로고    scopus 로고
    • Uracil-DNA glycosylase activities in hyperthermophilic micro-organisms
    • Koulis A, Cowan DA, Pearl LH, Savva R: Uracil-Dna glycosylase activities in hyperthermophilic micro-organisms. FEMS Microbiol Lett 1996, 143:267-271.
    • (1996) FEMS Microbiol Lett , vol.143 , pp. 267-271
    • Koulis, A.1    Cowan, D.A.2    Pearl, L.H.3    Savva, R.4
  • 9
    • 0033105094 scopus 로고    scopus 로고
    • Conserved domains in DNA repair proteins and evolution of repair systems
    • Aravind L, Walker DR, Koonin EV: Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Res 1999, 27:1223-1242.
    • (1999) Nucleic Acids Res , vol.27 , pp. 1223-1242
    • Aravind, L.1    Walker, D.R.2    Koonin, E.V.3
  • 11
    • 0029805081 scopus 로고    scopus 로고
    • A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase
    • Gallinari P, Jiricny J: A new class of uracil-Dna glycosylases related to human thymine-Dna glycosylase. Nature 1996, 383:735-738.
    • (1996) Nature , vol.383 , pp. 735-738
    • Gallinari, P.1    Jiricny, J.2
  • 12
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G:T/U mismatch-specific DNA glycosylase: Mismatch recognition by complementary-strand interactions
    • Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH: Crystal structure of a G:T/U mismatch-specific DNA glycosylase: Mismatch recognition by complementary-strand interactions. Cell 1998, 92:11 7-129.
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1    Savva, R.2    Panayotou, G.3    Barlow, T.4    Brown, T.5    Jiricny, J.6    Pearl, L.H.7
  • 13
    • 0017392934 scopus 로고
    • DNA N-glycosidases: Properties of uracil-DNA glycosidase from Escherichia coli
    • Lindahl T, Ljungquist S, Siegert W, Nyberg B, Sperens B: DNA N-glycosidases: Properties of uracil-Dna glycosidase from Escherichia coli. J Biol Chem 1977, 252:3286-3294.
    • (1977) J Biol Chem , vol.252 , pp. 3286-3294
    • Lindahl, T.1    Ljungquist, S.2    Siegert, W.3    Nyberg, B.4    Sperens, B.5
  • 14
    • 0025732374 scopus 로고
    • Specificities and kinetics of uracil excision from uracil-containing DNA oligomers by Escherichia coli uracil DNA glycosylase
    • Varshney U, van de Sande JH: Specificities and kinetics of uracil excision from uracil-containing DNA oligomers by Escherichia coli uracil DNA glycosylase. Biochemistry 1991, 30:4055-4061.
    • (1991) Biochemistry , vol.30 , pp. 4055-4061
    • Varshney, U.1    Van De Sande, J.H.2
  • 15
    • 0027253841 scopus 로고
    • Consensus sequences for good and poor removal of uracil from double stranded DNA by uracil-DNA glycosylase
    • Eftedal I, Guddal PH, Slupphaug G, Volden G, Krokan HE: Consensus sequences for good and poor removal of uracil from double stranded DNA by uracil-Dna glycosylase. Nucleic Adds Res 1993, 21:2095-2101.
    • (1993) Nucleic Adds Res , vol.21 , pp. 2095-2101
    • Eftedal, I.1    Guddal, P.H.2    Slupphaug, G.3    Volden, G.4    Krokan, H.E.5
  • 16
    • 0026589375 scopus 로고
    • Generation of single-nucleotide repair patches following excision of uracil residues from DNA
    • Dianov G, Price A, Lindahl T: Generation of single-nucleotide repair patches following excision of uracil residues from DNA. Mol Cell Biol 1992, 12:1605-1612.
    • (1992) Mol Cell Biol , vol.12 , pp. 1605-1612
    • Dianov, G.1    Price, A.2    Lindahl, T.3
  • 17
    • 0026101901 scopus 로고
    • Stereochemical studies of the beta-elimination reactions at aldehydic abasic sites in DNA: Endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys
    • Mazumder A, Gerlt JA, Absalon MJ, Stubbe J, Cunningham RP, Withka J: Stereochemical studies of the beta-elimination reactions at aldehydic abasic sites in DNA: Endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys. Biochemistry 1991, 30:1119-1126.
    • (1991) Biochemistry , vol.30 , pp. 1119-1126
    • Mazumder, A.1    Gerlt, J.A.2    Absalon, M.J.3    Stubbe, J.4    Cunningham, R.P.5    Withka, J.6
  • 18
    • 0029966418 scopus 로고    scopus 로고
    • Repair of ionizing-radiation damage in the radiation resistant bacterium Deinococcus radiodurans
    • Minton KW: Repair of ionizing-radiation damage in the radiation resistant bacterium Deinococcus radiodurans. Mutation Res 1996, 363:1-7.
    • (1996) Mutation Res , vol.363 , pp. 1-7
    • Minton, K.W.1
  • 19
    • 0030755081 scopus 로고    scopus 로고
    • Against all odds: The survival strategies of Deinococcus radiodurans
    • Battista JR: Against all odds: The survival strategies of Deinococcus radiodurans. Annu Rev Microbiol 1997, 51:203-224.
    • (1997) Annu Rev Microbiol , vol.51 , pp. 203-224
    • Battista, J.R.1
  • 20
    • 0025854322 scopus 로고
    • AP endonuclease and uracil DNA glycosylase activities in Deinococcus radiodurans
    • Masters CI, Moseley BE, Minton KW: AP endonuclease and uracil DNA glycosylase activities in Deinococcus radiodurans. Mutation Res 1991, 254:263-272.
    • (1991) Mutation Res , vol.254 , pp. 263-272
    • Masters, C.I.1    Moseley, B.E.2    Minton, K.W.3
  • 21
    • 0033602148 scopus 로고    scopus 로고
    • Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors
    • Haushalter KA, Stukenberg PT, Kirschner MW, Verdine GL: Identification of a new uracil-Dna glycosylase family by expression cloning using synthetic inhibitors. Curr Biol 1999, 9:174-185.
    • (1999) Curr Biol , vol.9 , pp. 174-185
    • Haushalter, K.A.1    Stukenberg, P.T.2    Kirschner, M.W.3    Verdine, G.L.4
  • 22
    • 0032898304 scopus 로고    scopus 로고
    • Purification and characterization of Thermotoga maritima endonuclease IV; a thermostable apurinic/apyrimidinic endonuclease and 3′-repair diesterase
    • Haas BJ, Sandigursky M, Tainer JA, Franklin WA, Cunningham RP: Purification and characterization of Thermotoga maritima endonuclease IV; a thermostable apurinic/apyrimidinic endonuclease and 3′-repair diesterase. J Bacteriol 1999, 181:2834-2839.
    • (1999) J Bacteriol , vol.181 , pp. 2834-2839
    • Haas, B.J.1    Sandigursky, M.2    Tainer, J.A.3    Franklin, W.A.4    Cunningham, R.P.5
  • 23
    • 0032030328 scopus 로고    scopus 로고
    • The post-incision steps of the DNA base excision repair pathway in Escherichia coli: Studies with a closed circular DNA substrate containing a single U:G base pair
    • Sandigursky M, Freyer GA, Franklin WA: The post-incision steps of the DNA base excision repair pathway in Escherichia coli: Studies with a closed circular DNA substrate containing a single U:G base pair. Nucleic Acids Res 1998, 26:1282-1287.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1282-1287
    • Sandigursky, M.1    Freyer, G.A.2    Franklin, W.A.3
  • 24
    • 0029976603 scopus 로고    scopus 로고
    • Using clustal for multiple sequence alignments
    • Higgins DG, Thompson JD, Gibson TJ: Using clustal for multiple sequence alignments. Meth Enzymol 1996, 266:383-402.
    • (1996) Meth Enzymol , vol.266 , pp. 383-402
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.