메뉴 건너뛰기




Volumn 189, Issue 19, 2007, Pages 6976-6988

The mutT defect does not elevate chromosomal fragmentation in Escherichia coli because of the surprisingly low levels of MutM/MutY-recognized DNA modifications

Author keywords

[No Author keywords available]

Indexed keywords

8 HYDROXYGUANINE; BACTERIAL DNA; BACTERIAL ENZYME; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DNA GLYCOSYLASE MUTY; DNA GLYCOSYLTRANSFERASE; PLASMID DNA; PROTEIN MUTM; PROTEIN MUTT; UNCLASSIFIED DRUG;

EID: 34948904292     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00776-07     Document Type: Article
Times cited : (14)

References (86)
  • 1
    • 33747332833 scopus 로고    scopus 로고
    • The replication intermediates in Escherichia coli are not the product of DNA processing or uracil excision
    • Amado, L., and A. Kuzminov. 2006. The replication intermediates in Escherichia coli are not the product of DNA processing or uracil excision. J. Biol. Chem. 281:22635-22646.
    • (2006) J. Biol. Chem , vol.281 , pp. 22635-22646
    • Amado, L.1    Kuzminov, A.2
  • 2
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann, E., B. Ochs, and K. J. Abel. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 3
    • 0024332124 scopus 로고
    • Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs
    • Au, K. G., S. Clark, J. H. Miller, and P. Modrich. 1989. Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs. Proc. Natl. Acad. Sci. USA 86:8877-8881.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8877-8881
    • Au, K.G.1    Clark, S.2    Miller, J.H.3    Modrich, P.4
  • 4
    • 34948897373 scopus 로고    scopus 로고
    • Bachmann, B. J. 1987. Derivations and genotypes of some mutant derivatives of Escherichia coli K-12, p. 1190-1219. In F. C. Neidhardt, L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, DC.
    • Bachmann, B. J. 1987. Derivations and genotypes of some mutant derivatives of Escherichia coli K-12, p. 1190-1219. In F. C. Neidhardt, L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, DC.
  • 5
    • 0001110365 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. II. Formation and interconversion of deoxyuridine phosphates
    • Bertani, L. E., A. Haggmark, and P. Reichard. 1963. Enzymatic synthesis of deoxyribonucleotides. II. Formation and interconversion of deoxyuridine phosphates. J. Biol. Chem. 238:3407-3413.
    • (1963) J. Biol. Chem , vol.238 , pp. 3407-3413
    • Bertani, L.E.1    Haggmark, A.2    Reichard, P.3
  • 6
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes
    • Bessman, M. J., D. N. Frick, and S. F. O'Handley. 1996. The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes. J. Biol. Chem. 271:25059-25062.
    • (1996) J. Biol. Chem , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 7
    • 0025738381 scopus 로고
    • Characterization of the MutT nucleoside triphosphatase of Escherichia coli
    • Bhatnagar, S. K., L. C. Bullions, and M. J. Bessman. 1991. Characterization of the MutT nucleoside triphosphatase of Escherichia coli. J. Biol. Chem. 266:9050-9054.
    • (1991) J. Biol. Chem , vol.266 , pp. 9050-9054
    • Bhatnagar, S.K.1    Bullions, L.C.2    Bessman, M.J.3
  • 8
    • 0020971311 scopus 로고
    • A rapid alkaline extraction method for the isolation of plasmid DNA
    • Birnboim, H. C. 1983. A rapid alkaline extraction method for the isolation of plasmid DNA. Methods Enzymol. 100:243-255.
    • (1983) Methods Enzymol , vol.100 , pp. 243-255
    • Birnboim, H.C.1
  • 9
    • 0026533905 scopus 로고
    • Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): Excision of purine lesions in DNA produced by ionizing radiation or photosensitization
    • Boiteux, S., E. Gajewski, J. Laval, and M. Dizdaroglu. 1992. Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization. Biochemistry 31:106-110.
    • (1992) Biochemistry , vol.31 , pp. 106-110
    • Boiteux, S.1    Gajewski, E.2    Laval, J.3    Dizdaroglu, M.4
  • 10
    • 0038575033 scopus 로고    scopus 로고
    • RdgB acts to avoid chromosome fragmentation in Escherichia coli
    • Bradshaw, J. S., and A. Kuzminov. 2003. RdgB acts to avoid chromosome fragmentation in Escherichia coli. Mol. Microbiol. 48:1711-1725.
    • (2003) Mol. Microbiol , vol.48 , pp. 1711-1725
    • Bradshaw, J.S.1    Kuzminov, A.2
  • 11
    • 0029934099 scopus 로고    scopus 로고
    • Effect of mutY and mutM/ fpg-1 mutations on starvation-associated mutation in Escherichia coli: Implications for the role of 7,8-dihydro-8- oxoguanine
    • Bridges, B. A., M. Sekiguchi, and T. Tajiri. 1996. Effect of mutY and mutM/ fpg-1 mutations on starvation-associated mutation in Escherichia coli: implications for the role of 7,8-dihydro-8- oxoguanine. Mol. Gen. Genet. 251:352-357.
    • (1996) Mol. Gen. Genet , vol.251 , pp. 352-357
    • Bridges, B.A.1    Sekiguchi, M.2    Tajiri, T.3
  • 12
    • 33748767935 scopus 로고    scopus 로고
    • Hypoxanthine incorporation is nonmutagenic in Escherichia coli
    • Budke, B., and A. Kuzminov. 2006. Hypoxanthine incorporation is nonmutagenic in Escherichia coli. J. Bacteriol. 188:6553-6560.
    • (2006) J. Bacteriol , vol.188 , pp. 6553-6560
    • Budke, B.1    Kuzminov, A.2
  • 13
    • 0023708084 scopus 로고
    • - cloning vectors. I. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencing
    • - cloning vectors. I. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencing. Gene 68:139-149.
    • (1988) Gene , vol.68 , pp. 139-149
    • Chambers, S.P.1    Prior, S.E.2    Barstow, D.A.3    Minton, N.P.4
  • 14
    • 0035879027 scopus 로고    scopus 로고
    • Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii
    • Chung, J. H., J. H. Back, Y. I. Park, and Y. S. Han. 2001. Biochemical characterization of a novel hypoxanthine/xanthine dNTP pyrophosphatase from Methanococcus jannaschii. Nucleic Acids Res. 29:3099-3107.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3099-3107
    • Chung, J.H.1    Back, J.H.2    Park, Y.I.3    Han, Y.S.4
  • 15
    • 0036023039 scopus 로고    scopus 로고
    • Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli
    • Chung, J. H., H. Y. Park, J. H. Lee, and Y. Jang. 2002. Identification of the dITP- and XTP-hydrolyzing protein from Escherichia coli. J. Biochem. Mol. Biol. 35:403-408.
    • (2002) J. Biochem. Mol. Biol , vol.35 , pp. 403-408
    • Chung, J.H.1    Park, H.Y.2    Lee, J.H.3    Jang, Y.4
  • 16
    • 0035023305 scopus 로고    scopus 로고
    • Comparative gene expression profiles following UV exposure in wild-type and SOS-deficient Escherichia coli
    • Courcelle, J., A. Khodursky, B. Peter, P. O. Brown, and P. C. Hanawalt. 2001. Comparative gene expression profiles following UV exposure in wild-type and SOS-deficient Escherichia coli. Genetics 158:41-64.
    • (2001) Genetics , vol.158 , pp. 41-64
    • Courcelle, J.1    Khodursky, A.2    Peter, B.3    Brown, P.O.4    Hanawalt, P.C.5
  • 17
    • 0014591911 scopus 로고
    • Mutator gene studies in Escherichia coli
    • Cox, E. C., and C. Yanofsky. 1969. Mutator gene studies in Escherichia coli. J. Bacteriol. 100:390-397.
    • (1969) J. Bacteriol , vol.100 , pp. 390-397
    • Cox, E.C.1    Yanofsky, C.2
  • 18
    • 0345549815 scopus 로고
    • A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions
    • Cupples, C. G., and J. H. Miller. 1989. A set of lacZ mutations in Escherichia coli that allow rapid detection of each of the six base substitutions. Proc. Natl. Acad. Sci. USA 86:5345-5349.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5345-5349
    • Cupples, C.G.1    Miller, J.H.2
  • 19
    • 0018594692 scopus 로고
    • Deletions generated by the transposon Tn10 in the srl-recA region of the Escherichia coli K-12 chromosome
    • Czonka, L. N., and A. J. Clark. 1979. Deletions generated by the transposon Tn10 in the srl-recA region of the Escherichia coli K-12 chromosome. Genetics 93:321-343.
    • (1979) Genetics , vol.93 , pp. 321-343
    • Czonka, L.N.1    Clark, A.J.2
  • 20
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 21
    • 0025886466 scopus 로고
    • A constant rate of spontaneous mutation in DNA-based microbes
    • Drake, J. W. 1991. A constant rate of spontaneous mutation in DNA-based microbes. Proc. Natl. Acad. Sci. USA 88:7160-7164.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7160-7164
    • Drake, J.W.1
  • 22
    • 0032558424 scopus 로고    scopus 로고
    • Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8-dehydroguanosine triphosphate incorporation and extension by replicative and repair DNA polymerases
    • Einolf, H. J., N. Schnetz-Boutaud, and F. P. Guengerich. 1998. Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8-dehydroguanosine triphosphate incorporation and extension by replicative and repair DNA polymerases. Biochemistry 37:13300-13312.
    • (1998) Biochemistry , vol.37 , pp. 13300-13312
    • Einolf, H.J.1    Schnetz-Boutaud, N.2    Guengerich, F.P.3
  • 23
    • 0026711129 scopus 로고
    • Multiple mutant of Escherichia coli synthesizing virtually thymineless DNA during limited growth
    • El-Hajj, H. H., L. Wang, and B. Weiss. 1992. Multiple mutant of Escherichia coli synthesizing virtually thymineless DNA during limited growth. J. Bacteriol. 174:4450-4456.
    • (1992) J. Bacteriol , vol.174 , pp. 4450-4456
    • El-Hajj, H.H.1    Wang, L.2    Weiss, B.3
  • 25
    • 0024391958 scopus 로고
    • Methylene blue plus light mediates 8-hydroxyguanine formation in DNA
    • Floyd, R. A., M. S. West, K. L. Eneff, and J. E. Schneider. 1989. Methylene blue plus light mediates 8-hydroxyguanine formation in DNA. Arch. Biochem. Biophys. 273:106-111.
    • (1989) Arch. Biochem. Biophys , vol.273 , pp. 106-111
    • Floyd, R.A.1    West, M.S.2    Eneff, K.L.3    Schneider, J.E.4
  • 26
    • 0033390088 scopus 로고    scopus 로고
    • Mechanisms of stationary phase mutation: A decade of adaptive mutation
    • Foster, P. L. 1999. Mechanisms of stationary phase mutation: a decade of adaptive mutation. Annu. Rev. Genet. 33:57-88.
    • (1999) Annu. Rev. Genet , vol.33 , pp. 57-88
    • Foster, P.L.1
  • 27
    • 0037415388 scopus 로고    scopus 로고
    • Interactions among the Escherichia coli mutT, mutM, and mutY damage prevention pathways
    • Fowler, R. G., S. J. White, C. Koyama, S. C. Moore, R. L. Dunn, and R. M. Schaaper. 2003. Interactions among the Escherichia coli mutT, mutM, and mutY damage prevention pathways. DNA Repair 2:159-173.
    • (2003) DNA Repair , vol.2 , pp. 159-173
    • Fowler, R.G.1    White, S.J.2    Koyama, C.3    Moore, S.C.4    Dunn, R.L.5    Schaaper, R.M.6
  • 30
    • 0000204322 scopus 로고
    • Deoxyuridylate kinase activity and deoxyuridine triphosphatase in Escherichia coli
    • Greenberg, G. R., and R. L. Somerville. 1962. Deoxyuridylate kinase activity and deoxyuridine triphosphatase in Escherichia coli. Proc. Natl. Acad. Sci. USA 48:247-257.
    • (1962) Proc. Natl. Acad. Sci. USA , vol.48 , pp. 247-257
    • Greenberg, G.R.1    Somerville, R.L.2
  • 31
    • 0017886373 scopus 로고
    • Escherichia coli mutants deficient in deoxyuridine triphosphatase
    • Hochhauser, S. J., and B. Weiss. 1978. Escherichia coli mutants deficient in deoxyuridine triphosphatase. J. Bacteriol. 134:157-166.
    • (1978) J. Bacteriol , vol.134 , pp. 157-166
    • Hochhauser, S.J.1    Weiss, B.2
  • 32
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. 2003. Pathways of oxidative damage. Annu. Rev. Microbiol. 57:395-418.
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 33
    • 0025740545 scopus 로고
    • A combination of RNase H (rnh) and recBCD or sbcB mutations in Escherichia coli K12 adversely affects growth
    • Itaya, M., and R. J. Crouch. 1991. A combination of RNase H (rnh) and recBCD or sbcB mutations in Escherichia coli K12 adversely affects growth. Mol. Gen. Genet. 277:424-432.
    • (1991) Mol. Gen. Genet , vol.277 , pp. 424-432
    • Itaya, M.1    Crouch, R.J.2
  • 34
    • 0347286963 scopus 로고    scopus 로고
    • Suppression of spontaneous and hydrogen peroxide-induced mutations by a MutT-type nucleotide pool sanitization enzyme, the Escherichia coli Orf135 protein
    • Kamiya, H., E. Iida, N. Murata-Kamiya, Y. Yamamoto, T. Miki, and H. Harashima. 2003. Suppression of spontaneous and hydrogen peroxide-induced mutations by a MutT-type nucleotide pool sanitization enzyme, the Escherichia coli Orf135 protein. Genes Cells 8:941-950.
    • (2003) Genes Cells , vol.8 , pp. 941-950
    • Kamiya, H.1    Iida, E.2    Murata-Kamiya, N.3    Yamamoto, Y.4    Miki, T.5    Harashima, H.6
  • 36
    • 0019331557 scopus 로고
    • Hypoxanthine in deoxyribonucleic acid: Generation by heat-induced hydrolysis of adenine residues and release in free form by a deoxyribonucleic acid glycosylase from calf thymus
    • Karran, P., and T. Lindahl. 1980. Hypoxanthine in deoxyribonucleic acid: generation by heat-induced hydrolysis of adenine residues and release in free form by a deoxyribonucleic acid glycosylase from calf thymus. Biochemistry 19:6005-6011.
    • (1980) Biochemistry , vol.19 , pp. 6005-6011
    • Karran, P.1    Lindahl, T.2
  • 37
    • 0032500588 scopus 로고    scopus 로고
    • Potential of Escherichia coli GTP cyclohydrolase II for hydrolyzing 8-oxo-dGTP, a mutagenic substrate for DNA synthesis
    • Kobayashi, M., Y. Ohara-Nemoto, M. Kaneko, H. Hayakawa, M. Sekiguchi, and K. Yamamoto. 1998. Potential of Escherichia coli GTP cyclohydrolase II for hydrolyzing 8-oxo-dGTP, a mutagenic substrate for DNA synthesis. J. Biol. Chem. 273:26394-26399.
    • (1998) J. Biol. Chem , vol.273 , pp. 26394-26399
    • Kobayashi, M.1    Ohara-Nemoto, Y.2    Kaneko, M.3    Hayakawa, H.4    Sekiguchi, M.5    Yamamoto, K.6
  • 38
    • 0027253636 scopus 로고
    • Requirement of homologous recombination functions for viability of the Escherichia coli cells that lack RNase HI and exonuclease V activities
    • Kogoma, T., X. Hong, G. W. Cadwell, K. G. Barnard, and T. Asai. 1993. Requirement of homologous recombination functions for viability of the Escherichia coli cells that lack RNase HI and exonuclease V activities. Biochimie 75:89-99.
    • (1993) Biochimie , vol.75 , pp. 89-99
    • Kogoma, T.1    Hong, X.2    Cadwell, G.W.3    Barnard, K.G.4    Asai, T.5
  • 39
    • 0016813208 scopus 로고
    • Novel mutants of Escherichia coli that accumulate very small DNA replicative intermediates
    • Konrad, E. B., and I. R. Lehman. 1975. Novel mutants of Escherichia coli that accumulate very small DNA replicative intermediates. Proc. Natl. Acad. Sci. USA 72:2150-2154.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2150-2154
    • Konrad, E.B.1    Lehman, I.R.2
  • 40
    • 3142637981 scopus 로고
    • Enzymatic cleavage of deoxyguanosine triphosphate to deoxyguanosine and tripolyphosphate
    • Kornberg, S. R., I. R. Lehman, M. J. Bessman, E. S. Simms, and A. Kornberg. 1958. Enzymatic cleavage of deoxyguanosine triphosphate to deoxyguanosine and tripolyphosphate. J. Biol. Chem. 233:159-162.
    • (1958) J. Biol. Chem , vol.233 , pp. 159-162
    • Kornberg, S.R.1    Lehman, I.R.2    Bessman, M.J.3    Simms, E.S.4    Kornberg, A.5
  • 41
    • 0035422440 scopus 로고    scopus 로고
    • dim-2 encodes a DNA methyltransferase responsible for all known cytosine methylation in Neurospora
    • Kouzminova, E., and E. U. Selker. 2001. dim-2 encodes a DNA methyltransferase responsible for all known cytosine methylation in Neurospora. EMBO J. 20:4309-4323.
    • (2001) EMBO J , vol.20 , pp. 4309-4323
    • Kouzminova, E.1    Selker, E.U.2
  • 42
    • 1542616353 scopus 로고    scopus 로고
    • Chromosomal fragmentation in dUTPase-deficient mutants of Escherichia coli and its recombinational repair
    • Kouzminova, E. A., and A. Kuzminov. 2004. Chromosomal fragmentation in dUTPase-deficient mutants of Escherichia coli and its recombinational repair. Mol. Microbiol. 51:1279-1295.
    • (2004) Mol. Microbiol , vol.51 , pp. 1279-1295
    • Kouzminova, E.A.1    Kuzminov, A.2
  • 43
    • 28844477965 scopus 로고    scopus 로고
    • Fragmentation of replicating chromosomes triggered by uracil in DNA
    • Kouzminova, E. A., and A. Kuzminov. 2006. Fragmentation of replicating chromosomes triggered by uracil in DNA. J. Mol. Biol. 355:20-33.
    • (2006) J. Mol. Biol , vol.355 , pp. 20-33
    • Kouzminova, E.A.1    Kuzminov, A.2
  • 44
    • 9244256745 scopus 로고    scopus 로고
    • RecA-dependent mutants in E. coli reveal strategies to avoid replication fork failure
    • Kouzminova, E. A., E. Rotman, L. Macomber, J. Zhang, and A. Kuzminov. 2004. RecA-dependent mutants in E. coli reveal strategies to avoid replication fork failure. Proc. Natl. Acad. Sci. USA 101:16262-16267.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16262-16267
    • Kouzminova, E.A.1    Rotman, E.2    Macomber, L.3    Zhang, J.4    Kuzminov, A.5
  • 45
    • 0016371628 scopus 로고
    • In vivo studies of temperature-sensitive recB and recC mutants
    • Kushner, S. R. 1974. In vivo studies of temperature-sensitive recB and recC mutants. J. Bacteriol. 120:1213-1218.
    • (1974) J. Bacteriol , vol.120 , pp. 1213-1218
    • Kushner, S.R.1
  • 46
    • 0028998597 scopus 로고
    • Collapse and repair of replication forks in Escherichia coli
    • Kuzminov, A. 1995. Collapse and repair of replication forks in Escherichia coli. Mol. Microbiol. 16:373-384.
    • (1995) Mol. Microbiol , vol.16 , pp. 373-384
    • Kuzminov, A.1
  • 47
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ
    • Kuzminov, A. 1999. Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ. Microbiol. Mol. Biol. Rev. 63:751-813.
    • (1999) Microbiol. Mol. Biol. Rev , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 48
    • 0028176499 scopus 로고
    • χ-sites in combination with RecA protein increase the survival of linear DNA in E. coli by inactivating ExoV activity of RecBCD nuclease
    • Kuzminov, A., E. Schabtach, and F. W. Stahl. 1994. χ-sites in combination with RecA protein increase the survival of linear DNA in E. coli by inactivating ExoV activity of RecBCD nuclease. EMBO J. 13:2764-2776.
    • (1994) EMBO J , vol.13 , pp. 2764-2776
    • Kuzminov, A.1    Schabtach, E.2    Stahl, F.W.3
  • 49
    • 0031019463 scopus 로고    scopus 로고
    • Stability of linear DNA in recA mutant Escherichia coli cells reflects ongoing chromosomal DNA degradation
    • Kuzminov, A., and F. W. Stahl. 1997. Stability of linear DNA in recA mutant Escherichia coli cells reflects ongoing chromosomal DNA degradation. J. Bacteriol. 179:880-888.
    • (1997) J. Bacteriol , vol.179 , pp. 880-888
    • Kuzminov, A.1    Stahl, F.W.2
  • 50
    • 0000476915 scopus 로고
    • An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues
    • Lindahl, T. 1974. An N-glycosidase from Escherichia coli that releases free uracil from DNA containing deaminated cytosine residues. Proc. Natl. Acad. Sci. USA 71:3649-3653.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3649-3653
    • Lindahl, T.1
  • 51
    • 0017392934 scopus 로고
    • DNA N-glycosidases. Properties of uracil-DNA glycosidase from Escherichia coli
    • Lindahl, T., S. Ljungquist, W. Siegert, B. Nyberg, and B. Sperens. 1977. DNA N-glycosidases. Properties of uracil-DNA glycosidase from Escherichia coli. J. Biol. Chem. 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
  • 52
    • 0016257644 scopus 로고
    • Heat-induced deamination of cytosine residues in deoxyribonucleic acid
    • Lindahl, T., and B. Nyberg. 1974. Heat-induced deamination of cytosine residues in deoxyribonucleic acid. Biochemistry 13:3405-3410.
    • (1974) Biochemistry , vol.13 , pp. 3405-3410
    • Lindahl, T.1    Nyberg, B.2
  • 53
    • 0025810994 scopus 로고
    • Mechanism of specific LexA cleavage: Autodigestion and the role of RecA coprotease
    • Little, J. W. 1991. Mechanism of specific LexA cleavage: autodigestion and the role of RecA coprotease. Biochimie 73:411-421.
    • (1991) Biochimie , vol.73 , pp. 411-421
    • Little, J.W.1
  • 54
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • Maki, H., and M. Sekiguchi. 1992. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature 355:273-275.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 56
    • 0026684849 scopus 로고
    • Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA
    • Michaels, M. L., C. Cruz, A. P. Grollman, and J. H. Miller. 1992. Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA. Proc. Natl. Acad. Sci. USA 89:7022-7025.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7022-7025
    • Michaels, M.L.1    Cruz, C.2    Grollman, A.P.3    Miller, J.H.4
  • 57
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • Michaels, M. L., and J. H. Miller. 1992. The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J. Bacteriol. 174:6321-6325.
    • (1992) J. Bacteriol , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 58
  • 59
    • 0031025093 scopus 로고    scopus 로고
    • DNA double-strand breaks caused by replication arrest
    • Michel, B., S. D. Ehrlich, and M. Uzest. 1997. DNA double-strand breaks caused by replication arrest. EMBO J. 16:430-438.
    • (1997) EMBO J , vol.16 , pp. 430-438
    • Michel, B.1    Ehrlich, S.D.2    Uzest, M.3
  • 60
    • 0033909543 scopus 로고    scopus 로고
    • Resolution of Holliday junctions by RuvABC prevents dimer formation in rep mutants and UV-irradiated cells
    • Michel, B., G. D. Recchia, M. Penel-Colin, S. D. Ehrlich, and D. J. Sherratt. 2000. Resolution of Holliday junctions by RuvABC prevents dimer formation in rep mutants and UV-irradiated cells. Mol. Microbiol. 37:180-191.
    • (2000) Mol. Microbiol , vol.37 , pp. 180-191
    • Michel, B.1    Recchia, G.D.2    Penel-Colin, M.3    Ehrlich, S.D.4    Sherratt, D.J.5
  • 61
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in molecular genetics
    • Miller, J.H.1
  • 62
    • 0037398332 scopus 로고    scopus 로고
    • Chromosomal lesion suppression and removal in Escherichia coli via linear DNA degradation
    • Miranda, A., and A. Kuzminov. 2003. Chromosomal lesion suppression and removal in Escherichia coli via linear DNA degradation. Genetics 163:1255-1271.
    • (2003) Genetics , vol.163 , pp. 1255-1271
    • Miranda, A.1    Kuzminov, A.2
  • 63
    • 0028967533 scopus 로고
    • Sequence specificity for removal of uracil from U · A pairs and U · G mismatches by uracil-DNA glycosylase from Escherichia coli, and correlation with mutational hotspots
    • Nilsen, H., S. P. Yazdankhah, I. Eftedal, and H. E. Krokan. 1995. Sequence specificity for removal of uracil from U · A pairs and U · G mismatches by uracil-DNA glycosylase from Escherichia coli, and correlation with mutational hotspots. FEBS Lett. 362:205-209.
    • (1995) FEBS Lett , vol.362 , pp. 205-209
    • Nilsen, H.1    Yazdankhah, S.P.2    Eftedal, I.3    Krokan, H.E.4
  • 64
    • 0004370304 scopus 로고
    • Physical association of the 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites
    • O'Connor, T. R., and J. Laval. 1989. Physical association of the 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites. Proc. Natl. Acad. Sci. USA 86:5222-5226.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5222-5226
    • O'Connor, T.R.1    Laval, J.2
  • 65
    • 0035937181 scopus 로고    scopus 로고
    • Orf135 from Escherichia coli is a Nudix hydrolase specific for CTP, dCTP and 5-methyl-dCTP
    • O'Handley, S. F., C. A. Dunn, and M. J. Bessman. 2001. Orf135 from Escherichia coli is a Nudix hydrolase specific for CTP, dCTP and 5-methyl-dCTP. J. Biol. Chem. 276:5421-5426.
    • (2001) J. Biol. Chem , vol.276 , pp. 5421-5426
    • O'Handley, S.F.1    Dunn, C.A.2    Bessman, M.J.3
  • 66
    • 0024504224 scopus 로고
    • Mutations in uvrD induce the SOS response in Escherichia coli
    • Ossanna, N., and D. W. Mount. 1989. Mutations in uvrD induce the SOS response in Escherichia coli. J. Bacteriol. 171:303-307.
    • (1989) J. Bacteriol , vol.171 , pp. 303-307
    • Ossanna, N.1    Mount, D.W.2
  • 68
    • 0027983621 scopus 로고
    • 5-Hydroxypyrimidine deoxynucleoside triphosphates are more efficiently incoiporated into DNA by exonuclease-free Klenow fragment than 8-oxopurire deoxynucleoside triphosphates
    • Purmal, A. A., Y. W. Kow, and S. S. Wallace. 1994. 5-Hydroxypyrimidine deoxynucleoside triphosphates are more efficiently incoiporated into DNA by exonuclease-free Klenow fragment than 8-oxopurire deoxynucleoside triphosphates. Nucleic Acids Res. 22:3930-3935.
    • (1994) Nucleic Acids Res , vol.22 , pp. 3930-3935
    • Purmal, A.A.1    Kow, Y.W.2    Wallace, S.S.3
  • 69
    • 0025286303 scopus 로고
    • Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-encoding gene (dgt) of Escherichia coli
    • Quirk, S., S. K. Bhatnagar, and M. J. Bessman. 1990. Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-encoding gene (dgt) of Escherichia coli. Gene 89:13-18.
    • (1990) Gene , vol.89 , pp. 13-18
    • Quirk, S.1    Bhatnagar, S.K.2    Bessman, M.J.3
  • 70
    • 0034006621 scopus 로고    scopus 로고
    • Determining mutation rates in bacterial populations
    • Rosche, W. A., and P. L. Foster. 2000. Determining mutation rates in bacterial populations. Methods 20:4-17.
    • (2000) Methods , vol.20 , pp. 4-17
    • Rosche, W.A.1    Foster, P.L.2
  • 71
    • 0025953766 scopus 로고
    • Spontaneous mutation in the Escherichia coli lacI gene
    • Schaaper, R. M., and R. L. Dunn. 1991. Spontaneous mutation in the Escherichia coli lacI gene. Genetics 129:317-326.
    • (1991) Genetics , vol.129 , pp. 317-326
    • Schaaper, R.M.1    Dunn, R.L.2
  • 72
    • 0025096836 scopus 로고
    • Methylene blue plus light mediates 8-hydroxy 2′-deoxyguanosine formation in DNA preferentially over strand breakage
    • Schneider, J. E., S. Price, L. Maidt, J. M. Gutteridge, and R. A. Floyd. 1990. Methylene blue plus light mediates 8-hydroxy 2′-deoxyguanosine formation in DNA preferentially over strand breakage. Nucleic Acids Res. 18:631-635.
    • (1990) Nucleic Acids Res , vol.18 , pp. 631-635
    • Schneider, J.E.1    Price, S.2    Maidt, L.3    Gutteridge, J.M.4    Floyd, R.A.5
  • 73
    • 0028933674 scopus 로고
    • Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli
    • Tajiri, T., H. Maki, and M. Sekiguchi. 1995. Functional cooperation of MutT, MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli. Mutat. Res. 336:257-267.
    • (1995) Mutat. Res , vol.336 , pp. 257-267
    • Tajiri, T.1    Maki, H.2    Sekiguchi, M.3
  • 74
    • 0037013297 scopus 로고    scopus 로고
    • Assessing the metabolic function of the MutT 8-oxodeoxyguanosine triphosphatase in Escherichia coli by nucleotide pool analysis
    • Tassotto, M. L., and C. K. Mathews. 2002. Assessing the metabolic function of the MutT 8-oxodeoxyguanosine triphosphatase in Escherichia coli by nucleotide pool analysis. J. Biol. Chem. 277:15807-15812.
    • (2002) J. Biol. Chem , vol.277 , pp. 15807-15812
    • Tassotto, M.L.1    Mathews, C.K.2
  • 75
    • 0019921462 scopus 로고
    • Role of exonuclease III in the base excision repair of uracil-containing DNA
    • Taylor, A. F., and B. Weiss. 1982. Role of exonuclease III in the base excision repair of uracil-containing DNA. J. Bacteriol. 151:351-357.
    • (1982) J. Bacteriol , vol.151 , pp. 351-357
    • Taylor, A.F.1    Weiss, B.2
  • 76
    • 0017740439 scopus 로고
    • Excision repair of uracil incorporated in DNA as a result of a defect in dUTPase
    • Tye, B.-K., and I. R. Lehman. 1977. Excision repair of uracil incorporated in DNA as a result of a defect in dUTPase. J. Mol. Biol. 117:293-306.
    • (1977) J. Mol. Biol , vol.117 , pp. 293-306
    • Tye, B.-K.1    Lehman, I.R.2
  • 77
    • 0028786478 scopus 로고
    • Lethality of rep recB and rep recC double mutants of Escherichia coli
    • Uzest, M., S. D. Ehrlich, and B. Michel. 1995. Lethality of rep recB and rep recC double mutants of Escherichia coli. Mol. Microbiol. 17:1177-1188.
    • (1995) Mol. Microbiol , vol.17 , pp. 1177-1188
    • Uzest, M.1    Ehrlich, S.D.2    Michel, B.3
  • 78
    • 0027428503 scopus 로고
    • MutY repair is mutagenic in mutT -strains of Escherichia coli
    • Vidmar, J. J., and C. G. Cupples. 1993. MutY repair is mutagenic in mutT -strains of Escherichia coli. Can. J. Microbiol. 39:892-894.
    • (1993) Can. J. Microbiol , vol.39 , pp. 892-894
    • Vidmar, J.J.1    Cupples, C.G.2
  • 79
    • 0019475150 scopus 로고
    • Synthesis and metabolism of uracil-containing deoxyribonucleic acid in Escherichia coli
    • Warner, H. R., B. K. Duncan, C. Garrett, and J. Neuhard. 1981. Synthesis and metabolism of uracil-containing deoxyribonucleic acid in Escherichia coli. J. Bacteriol. 145:687-695.
    • (1981) J. Bacteriol , vol.145 , pp. 687-695
    • Warner, H.R.1    Duncan, B.K.2    Garrett, C.3    Neuhard, J.4
  • 80
    • 0014588869 scopus 로고
    • Characteristics of some multiply recombination-deficient strains of Escherichia coli
    • Willetts, N. S., and A. J. Clark. 1969. Characteristics of some multiply recombination-deficient strains of Escherichia coli. J. Bacteriol. 100:231-239.
    • (1969) J. Bacteriol , vol.100 , pp. 231-239
    • Willetts, N.S.1    Clark, A.J.2
  • 81
    • 0029743602 scopus 로고    scopus 로고
    • Conformation of plasmid DNA from Escherichia coli deficient in the repair systems protecting DNA from 8-oxyguanine lesions
    • Wójcik, A., E. Grzesiuk, B. Tudek, and C. Janion. 1996. Conformation of plasmid DNA from Escherichia coli deficient in the repair systems protecting DNA from 8-oxyguanine lesions. Biochimie 78:85-89.
    • (1996) Biochimie , vol.78 , pp. 85-89
    • Wójcik, A.1    Grzesiuk, E.2    Tudek, B.3    Janion, C.4
  • 82
    • 0037372874 scopus 로고    scopus 로고
    • The Escherichia coli methyl-directed mismatch repair system repairs base pairs containing oxidative lesions
    • Wyrzykowski, J., and M. R. Volkert. 2003. The Escherichia coli methyl-directed mismatch repair system repairs base pairs containing oxidative lesions. J. Bacteriol. 185:1701-1704.
    • (2003) J. Bacteriol , vol.185 , pp. 1701-1704
    • Wyrzykowski, J.1    Volkert, M.R.2
  • 83
    • 0013882288 scopus 로고
    • The unusual mutagenic specificity of an E. coli mutator gene
    • Yanofsky, C., E. C. Cox, and V. Horn. 1966. The unusual mutagenic specificity of an E. coli mutator gene. Proc. Natl. Acad. Sci. USA 55:274-281.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 274-281
    • Yanofsky, C.1    Cox, E.C.2    Horn, V.3
  • 84
    • 0028286268 scopus 로고
    • Purification and characterization of a novel deoxyinosine-specific enzyme, deoxyinosine 3′ endonuclease, from Escherichia coli
    • Yao, M., Z. Hatahet, R. J. Melamede, and Y. W. Kow. 1994. Purification and characterization of a novel deoxyinosine-specific enzyme, deoxyinosine 3′ endonuclease, from Escherichia coli. J. Biol. Chem. 269:16260-16268.
    • (1994) J. Biol. Chem , vol.269 , pp. 16260-16268
    • Yao, M.1    Hatahet, Z.2    Melamede, R.J.3    Kow, Y.W.4
  • 85
    • 1842338079 scopus 로고    scopus 로고
    • Further characterization of Escherichia coli endonuclease V. Mechanism of recognition for deoxyinosine, deoxyuridine, and base mismatches in DNA
    • Yao, M., and Y. W. Kow. 1997. Further characterization of Escherichia coli endonuclease V. Mechanism of recognition for deoxyinosine, deoxyuridine, and base mismatches in DNA. J. Biol. Chem. 272:30774-30779.
    • (1997) J. Biol. Chem , vol.272 , pp. 30774-30779
    • Yao, M.1    Kow, Y.W.2
  • 86
    • 0028845857 scopus 로고
    • Interaction of deoxyinosine 3′-endonuclease from Escherichia coli with DNA containing deoxyinosine
    • Yao, M., and Y. W. Kow. 1995. Interaction of deoxyinosine 3′-endonuclease from Escherichia coli with DNA containing deoxyinosine. J. Biol. Chem. 270:28609-28616.
    • (1995) J. Biol. Chem , vol.270 , pp. 28609-28616
    • Yao, M.1    Kow, Y.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.