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Volumn 38, Issue 17, 2010, Pages 5692-5705

A novel single-stranded DNA-specific 3′-5′ exonuclease, Thermus thermophilus exonuclease I, is involved in several DNA repair pathways

Author keywords

[No Author keywords available]

Indexed keywords

EXODEOXYRIBONUCLEASE I; EXONUCLEASE; HYDROGEN PEROXIDE; RECJ PROTEIN; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DNA; EXODEOXYRIBONUCLEASE; RECJ PROTEIN, BACTERIA;

EID: 77957231633     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq350     Document Type: Article
Times cited : (19)

References (72)
  • 4
    • 0035903140 scopus 로고    scopus 로고
    • Redundant exonuclease involvement in Escherichia coli methyl-directed mismatch repair
    • Viswanathan,M., Burdett,V., Baitinger,C., Modrich,P. and Lovett,S.T. (2001) Redundant exonuclease involvement in Escherichia coli methyl-directed mismatch repair. J. Biol. Chem., 276, 31053-31058.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31053-31058
    • Viswanathan, M.1    Burdett, V.2    Baitinger, C.3    Modrich, P.4    Lovett, S.T.5
  • 5
    • 0242362736 scopus 로고    scopus 로고
    • xni-deficient Escherichia coli are proficient for recombination and multiple pathways of repair
    • Lombardo,M.-J., Aponyi,I., Ray,M.P., Sandigursky,M., Franklin,W.A. and Rosenberg,S.M. (2003) xni-deficient Escherichia coli are proficient for recombination and multiple pathways of repair. DNA Repair, 2, 1175-1183.
    • (2003) DNA Repair , vol.2 , pp. 1175-1183
    • Lombardo, M.-J.1    Aponyi, I.2    Ray, M.P.3    Sandigursky, M.4    Franklin, W.A.5    Rosenberg, S.M.6
  • 7
    • 0020793619 scopus 로고
    • Induction of DNA strand breaks in normal human fibroblasts exposed to monochromatic ultraviolet and visible wavelengths in the 240-546 nm range
    • Rosenstein,B.S. and Ducore,J.M. (1983) Induction of DNA strand breaks in normal human fibroblasts exposed to monochromatic ultraviolet and visible wavelengths in the 240-546 nm range. Photochem. Photobiol., 38, 51-55.
    • (1983) Photochem. Photobiol. , vol.38 , pp. 51-55
    • Rosenstein, B.S.1    Ducore, J.M.2
  • 8
    • 0035695023 scopus 로고    scopus 로고
    • Recombination at double-strand breaks and DNA ends: conserved mechanisms from phage to humans
    • Cromie,G.A., Connelly,J.C. and Leach,D.R.F. (2001) Recombination at double-strand breaks and DNA ends: conserved mechanisms from phage to humans. Mol. Cell, 8, 1163-1174.
    • (2001) Mol. Cell , vol.8 , pp. 1163-1174
    • Cromie, G.A.1    Connelly, J.C.2    Leach, D.R.F.3
  • 11
    • 33746189409 scopus 로고    scopus 로고
    • Endonucleolytic function of MutLα in human mismatch repair
    • Kadyrov,F.A., Dzantiev,L., Constantin,N. and Modrich,P. (2006) Endonucleolytic function of MutLα in human mismatch repair. Cell, 126, 297-308.
    • (2006) Cell , vol.126 , pp. 297-308
    • Kadyrov, F.A.1    Dzantiev, L.2    Constantin, N.3    Modrich, P.4
  • 13
    • 33750083332 scopus 로고    scopus 로고
    • Mechanisms in eukaryotic mismatch repair
    • Modrich,P. (2006) Mechanisms in eukaryotic mismatch repair. J. Biol. Chem., 281, 30305-30309.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30305-30309
    • Modrich, P.1
  • 14
    • 0034641938 scopus 로고    scopus 로고
    • Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA
    • Obmolova,G., Ban,C., Hsieh,P. and Yang,W. (2000) Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature, 407, 703-710.
    • (2000) Nature , vol.407 , pp. 703-710
    • Obmolova, G.1    Ban, C.2    Hsieh, P.3    Yang, W.4
  • 15
    • 45549093251 scopus 로고    scopus 로고
    • Bound nucleotide controls the endonuclease activity of mismatch repair enzyme MutL
    • Fukui,K., Nishida,M., Nakagawa,N., Masui,R. and Kuramitsu,S. (2008) Bound nucleotide controls the endonuclease activity of mismatch repair enzyme MutL. J. Biol. Chem., 283, 12136-12145.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12136-12145
    • Fukui, K.1    Nishida, M.2    Nakagawa, N.3    Masui, R.4    Kuramitsu, S.5
  • 17
    • 0242380643 scopus 로고    scopus 로고
    • Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V
    • Moe,A., Ringvoll,J., Nordstrand,L.M., Eide,L., Bjoras,M., Seeberg,E., Rognes,T. and Klungland,A. (2003) Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V. Nucleic Acids Res., 31, 3893-3900.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3893-3900
    • Moe, A.1    Ringvoll, J.2    Nordstrand, L.M.3    Eide, L.4    Bjoras, M.5    Seeberg, E.6    Rognes, T.7    Klungland, A.8
  • 19
    • 1942488240 scopus 로고    scopus 로고
    • Thermus thermophilus MutS2, a MutS paralogue, possesses an endonuclease activity promoted by MutL
    • Fukui,K., Masui,R. and Kuramitsu,S. (2004) Thermus thermophilus MutS2, a MutS paralogue, possesses an endonuclease activity promoted by MutL. J. Biochem., 135, 375-384.
    • (2004) J. Biochem. , vol.135 , pp. 375-384
    • Fukui, K.1    Masui, R.2    Kuramitsu, S.3
  • 20
    • 48749122761 scopus 로고    scopus 로고
    • 6-methylguanine-DNA methyltransferase-like protein from Thermus thermophilus interacts with a nucleotide excision repair protein
    • 6-methylguanine-DNA methyltransferase-like protein from Thermus thermophilus interacts with a nucleotide excision repair protein. J. Biochem., 144, 267-277.
    • (2008) J. Biochem. , vol.144 , pp. 267-277
    • Morita, R.1    Nakagawa, N.2    Kuramitsu, S.3    Masui, R.4
  • 21
    • 0035890855 scopus 로고    scopus 로고
    • Overexpression, purification and characterization of RecJ protein from Thermus thermophilus HB8 and its core domain
    • Yamagata,A., Masui,R., Kakuta,Y., Kuramitsu,S. and Fukuyama,K. (2001) Overexpression, purification and characterization of RecJ protein from Thermus thermophilus HB8 and its core domain. Nucleic Acids Res., 29, 4617-4624.
    • (2001) Nucleic Acids Res , vol.29 , pp. 4617-4624
    • Yamagata, A.1    Masui, R.2    Kakuta, Y.3    Kuramitsu, S.4    Fukuyama, K.5
  • 22
    • 0031924593 scopus 로고    scopus 로고
    • Oligoribonuclease is encoded by a highly conserved gene in the 3′-5′ exonuclease superfamily
    • Zhang,X., Zhu,L. and Deutscher,M.P. (1998) Oligoribonuclease is encoded by a highly conserved gene in the 3′-5′ exonuclease superfamily. J. Bacteriol., 180, 2779-2781.
    • (1998) J. Bacteriol. , vol.180 , pp. 2779-2781
    • Zhang, X.1    Zhu, L.2    Deutscher, M.P.3
  • 23
    • 0031574363 scopus 로고    scopus 로고
    • The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains
    • Moser,M.J., Holley,W.R., Chatterjee,A. and Mian,I.S. (1997) The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains. Nucleic Acids Res., 25, 5110-5118.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 5110-5118
    • Moser, M.J.1    Holley, W.R.2    Chatterjee, A.3    Mian, I.S.4
  • 24
    • 0024474078 scopus 로고
    • A conserved 3′->5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases
    • Bernad,A., Blanco,L., Lazaro,J., Martin,G. and Salas,M. (1989) A conserved 3′->5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases. Cell, 59, 219-228.
    • (1989) Cell , vol.59 , pp. 219-228
    • Bernad, A.1    Blanco, L.2    Lazaro, J.3    Martin, G.4    Salas, M.5
  • 25
    • 0033664281 scopus 로고    scopus 로고
    • Structure of Escherichia coli exonuclease I suggests how processivity is achieved
    • Breyer,W.A. and Matthews,B.W. (2000) Structure of Escherichia coli exonuclease I suggests how processivity is achieved. Nat. Struct. Mol. Biol., 7, 1125-1128.
    • (2000) Nat. Struct. Mol. Biol. , vol.7 , pp. 1125-1128
    • Breyer, W.A.1    Matthews, B.W.2
  • 26
    • 38549126059 scopus 로고    scopus 로고
    • Structure of Escherichia coli exonuclease I in complex with thymidine 5′-monophosphate
    • Busam,R. (2008) Structure of Escherichia coli exonuclease I in complex with thymidine 5′-monophosphate. Acta Crystallogr. D Biol. Crystallogr., 64, 206-210.
    • (2008) Acta Crystallogr. D Biol. Crystallogr. , vol.64 , pp. 206-210
    • Busam, R.1
  • 27
    • 34248359835 scopus 로고    scopus 로고
    • Transcription activation mediated by a cyclic AMP receptor protein from Thermus thermophilus HB8
    • Shinkai,A., Kira,S., Nakagawa,N., Kashihara,A., Kuramitsu,S. and Yokoyama,S. (2007) Transcription activation mediated by a cyclic AMP receptor protein from Thermus thermophilus HB8. J. Bacteriol., 189, 3891-3901.
    • (2007) J. Bacteriol. , vol.189 , pp. 3891-3901
    • Shinkai, A.1    Kira, S.2    Nakagawa, N.3    Kashihara, A.4    Kuramitsu, S.5    Yokoyama, S.6
  • 28
    • 33846880929 scopus 로고    scopus 로고
    • Validation of universal conditions for duplex quantitative reverse transcription polymerase chain reaction assays
    • Ishii,T., Sootome,H., Shan,L. and Yamashita,K. (2007) Validation of universal conditions for duplex quantitative reverse transcription polymerase chain reaction assays. Anal. Biochem., 362, 201-212.
    • (2007) Anal. Biochem. , vol.362 , pp. 201-212
    • Ishii, T.1    Sootome, H.2    Shan, L.3    Yamashita, K.4
  • 29
    • 0035850879 scopus 로고    scopus 로고
    • Disruption of Thermus thermophilus genes by homologous recombination using a thermostable kanamycin-resistant marker
    • Hashimoto,Y., Yano,T., Kuramitsu,S. and Kagamiyama,H. (2001) Disruption of Thermus thermophilus genes by homologous recombination using a thermostable kanamycin-resistant marker. FEBS Lett., 506, 231-234.
    • (2001) FEBS Lett. , vol.506 , pp. 231-234
    • Hashimoto, Y.1    Yano, T.2    Kuramitsu, S.3    Kagamiyama, H.4
  • 30
    • 0032730861 scopus 로고    scopus 로고
    • Directed evolution of thermostable kanamycin-resistance gene: a convenient selection marker for Thermus thermophilus
    • Hoseki,J., Yano,T., Koyama,Y., Kuramitsu,S. and Kagamiyama,H. (1999) Directed evolution of thermostable kanamycin-resistance gene: a convenient selection marker for Thermus thermophilus. J. Biochem., 126, 951-956.
    • (1999) J. Biochem. , vol.126 , pp. 951-956
    • Hoseki, J.1    Yano, T.2    Koyama, Y.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 31
    • 67650136762 scopus 로고    scopus 로고
    • Degradation of ppGpp by nudix pyrophosphatase modulates the transition of growth phase in the bacterium Thermus thermophilus
    • Ooga,T., Ohashi,Y., Kuramitsu,S., Koyama,Y., Tomita,M., Soga,T. and Masui,R. (2009) Degradation of ppGpp by nudix pyrophosphatase modulates the transition of growth phase in the bacterium Thermus thermophilus. J. Biol. Chem., 284, 15549-15556.
    • (2009) J. Biol. Chem. , vol.284 , pp. 15549-15556
    • Ooga, T.1    Ohashi, Y.2    Kuramitsu, S.3    Koyama, Y.4    Tomita, M.5    Soga, T.6    Masui, R.7
  • 32
    • 0001641514 scopus 로고
    • Mutations of bacteria from virus sensitivity to virus resistance
    • Luria,S.E. and Delbruck,M. (1943) Mutations of bacteria from virus sensitivity to virus resistance. Genetics, 28, 491-511.
    • (1943) Genetics , vol.28 , pp. 491-511
    • Luria, S.E.1    Delbruck, M.2
  • 33
    • 44849110325 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins modified by nitric oxide-derived species
    • Salzano,A.M., D'Ambrosio,C. and Scaloni,A. (2008) Mass spectrometric characterization of proteins modified by nitric oxide-derived species. Meth. Enzymol., 440, 3-15.
    • (2008) Meth. Enzymol. , vol.440 , pp. 3-15
    • Salzano, A.M.1    D'Ambrosio, C.2    Scaloni, A.3
  • 34
    • 34548563856 scopus 로고    scopus 로고
    • Analysis of a nuclease activity of catalytic domain of Thermus thermophilus MutS2 by high-accuracy mass spectrometry
    • Fukui,K., Takahata,Y., Nakagawa,N., Kuramitsu,S. and Masui,R. (2007) Analysis of a nuclease activity of catalytic domain of Thermus thermophilus MutS2 by high-accuracy mass spectrometry. Nucleic Acids Res., 35, e100.
    • (2007) Nucleic Acids Res. , vol.35
    • Fukui, K.1    Takahata, Y.2    Nakagawa, N.3    Kuramitsu, S.4    Masui, R.5
  • 35
    • 58549101083 scopus 로고    scopus 로고
    • Orchestration of Haemophilus influenzae RecJ exonuclease by interaction with single-stranded DNA-binding protein
    • Sharma,R. and Rao,D.N. (2009) Orchestration of Haemophilus influenzae RecJ exonuclease by interaction with single-stranded DNA-binding protein. J. Mol. Biol., 385, 1375-1396.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1375-1396
    • Sharma, R.1    Rao, D.N.2
  • 36
    • 52049118325 scopus 로고    scopus 로고
    • Cooperative DNA binding and communication across the dimer interface in the TREX2 3′ -> 5′-exonuclease
    • Perrino,F.W., de Silva,U., Harvey,S., Pryor,E.E. Jr, Cole,D.W. and Hollis,T. (2008) Cooperative DNA binding and communication across the dimer interface in the TREX2 3′ -> 5′-exonuclease. J. Biol. Chem., 283, 21441-21452.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21441-21452
    • Perrino, F.W.1    de Silva, U.2    Harvey, S.3    Pryor E.E., Jr.4    Cole, D.W.5    Hollis, T.6
  • 37
    • 0033570183 scopus 로고    scopus 로고
    • Exonuclease X of Escherichia coli. A novel 3′-5′ DNase and DnaQ superfamily member involved in DNA repair
    • Viswanathan,M. and Lovett,S.T. (1999) Exonuclease X of Escherichia coli. A novel 3′-5′ DNase and DnaQ superfamily member involved in DNA repair. J. Biol. Chem., 274, 30094-30100.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30094-30100
    • Viswanathan, M.1    Lovett, S.T.2
  • 38
    • 0001063349 scopus 로고
    • The deoxyribonucleases of Escherichia coli
    • Lehman,I.R. and Nussbaum,A.L. (1964) The deoxyribonucleases of Escherichia coli. J. Biol. Chem., 239, 2628-2636.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2628-2636
    • Lehman, I.R.1    Nussbaum, A.L.2
  • 39
    • 0023689711 scopus 로고
    • A mutation in the 530 loop of Escherichia coli 16S ribosomal RNA causes resistance to streptomycin
    • Melancon,P., Lemieux,C. and Brakier-Gingras,L. (1988) A mutation in the 530 loop of Escherichia coli 16S ribosomal RNA causes resistance to streptomycin. Nucleic Acids Res., 16, 9631-9639.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9631-9639
    • Melancon, P.1    Lemieux, C.2    Brakier-Gingras, L.3
  • 40
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • Moazed,D. and Noller,H.F. (1987) Interaction of antibiotics with functional sites in 16S ribosomal RNA. Nature, 327, 389-394.
    • (1987) Nature , vol.327 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 41
    • 0019783890 scopus 로고
    • Double-strand breaks in DNA caused by repair of damage due to ultraviolet light
    • Bradley,M.O. (1981) Double-strand breaks in DNA caused by repair of damage due to ultraviolet light. J. Supramol. Struct. Cell. Biochem., 16, 337-343.
    • (1981) J. Supramol. Struct. Cell. Biochem. , vol.16 , pp. 337-343
    • Bradley, M.O.1
  • 42
    • 0022629164 scopus 로고
    • The role of the (6-4) photoproduct in ultraviolet light-induced transition mutations in E. coli
    • Franklin,W.A. and Haseltine,W.A. (1986) The role of the (6-4) photoproduct in ultraviolet light-induced transition mutations in E. coli. Mutat. Res., 165, 1-7.
    • (1986) Mutat. Res. , vol.165 , pp. 1-7
    • Franklin, W.A.1    Haseltine, W.A.2
  • 43
    • 0024584032 scopus 로고
    • Enzymatic analysis of isomeric trithymidylates containing ultraviolet light-induced cyclobutane pyrimidine dimers. II. Phosphorylation by phage T4 polynucleotide kinase
    • Weinfeld,M., Liuzzi,M. and Paterson,M.C. (1989) Enzymatic analysis of isomeric trithymidylates containing ultraviolet light-induced cyclobutane pyrimidine dimers. II. Phosphorylation by phage T4 polynucleotide kinase. J. Biol. Chem., 264, 6364-6370.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6364-6370
    • Weinfeld, M.1    Liuzzi, M.2    Paterson, M.C.3
  • 44
    • 0024439327 scopus 로고
    • Respective roles of pyrimidine dimer and pyrimidine (6-4) pyrimidone photoproducts in UV mutagenesis of simian virus 40 DNA in mammalian cells
    • Bourre,F., Benoit,A. and Sarasin,A. (1989) Respective roles of pyrimidine dimer and pyrimidine (6-4) pyrimidone photoproducts in UV mutagenesis of simian virus 40 DNA in mammalian cells. J. Virol., 63, 4520-4524.
    • (1989) J. Virol. , vol.63 , pp. 4520-4524
    • Bourre, F.1    Benoit, A.2    Sarasin, A.3
  • 45
    • 0016424156 scopus 로고
    • Enzymatic production of deoxyribonucleic acid double-strand breaks after ultraviolet irradiation of Escherichia coli K-12
    • Bonura,T. and Smith,K.C. (1975) Enzymatic production of deoxyribonucleic acid double-strand breaks after ultraviolet irradiation of Escherichia coli K-12. J. Bacteriol., 121, 511-517.
    • (1975) J. Bacteriol. , vol.121 , pp. 511-517
    • Bonura, T.1    Smith, K.C.2
  • 46
    • 31344469053 scopus 로고    scopus 로고
    • Evidence for mutagenesis by nitric oxide during nitrate metabolism in Escherichia coli
    • Weiss,B. (2006) Evidence for mutagenesis by nitric oxide during nitrate metabolism in Escherichia coli. J. Bacteriol., 188, 829-833.
    • (2006) J. Bacteriol. , vol.188 , pp. 829-833
    • Weiss, B.1
  • 47
    • 0036256934 scopus 로고    scopus 로고
    • Oxidative deamination by hydrogen peroxide in the presence of metals
    • Akagawa,M. and Suyama,K. (2002) Oxidative deamination by hydrogen peroxide in the presence of metals. Free Radic. Res., 36, 13-21.
    • (2002) Free Radic. Res. , vol.36 , pp. 13-21
    • Akagawa, M.1    Suyama, K.2
  • 48
    • 40349106220 scopus 로고    scopus 로고
    • Insights into different dependency of dNTP triphosphohydrolase on metal ion species from intracellular ion concentrations in Thermus thermophilus
    • Kondo,N., Nishikubo,T., Wakamatsu,T., Ishikawa,H., Nakagawa,N., Kuramitsu,S. and Masui,R. (2008) Insights into different dependency of dNTP triphosphohydrolase on metal ion species from intracellular ion concentrations in Thermus thermophilus. Extremophiles, 12, 217-223.
    • (2008) Extremophiles , vol.12 , pp. 217-223
    • Kondo, N.1    Nishikubo, T.2    Wakamatsu, T.3    Ishikawa, H.4    Nakagawa, N.5    Kuramitsu, S.6    Masui, R.7
  • 50
    • 17644407757 scopus 로고    scopus 로고
    • The human TREX2 3′ -> 5′-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis
    • Perrino,F.W., Harvey,S., McMillin,S. and Hollis,T. (2005) The human TREX2 3′ -> 5′-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis. J. Biol. Chem., 280, 15212-15218.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15212-15218
    • Perrino, F.W.1    Harvey, S.2    McMillin, S.3    Hollis, T.4
  • 51
    • 34249848019 scopus 로고    scopus 로고
    • The crystal structure of TREX1 explains the 3′ nucleotide specificity and reveals a polyproline II helix for protein partnering
    • de Silva,U., Choudhury,S., Bailey,S.L., Harvey,S., Perrino,F.W. and Hollis,T. (2007) The crystal structure of TREX1 explains the 3′ nucleotide specificity and reveals a polyproline II helix for protein partnering. J. Biol. Chem., 282, 10537-10543.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10537-10543
    • de Silva, U.1    Choudhury, S.2    Bailey, S.L.3    Harvey, S.4    Perrino, F.W.5    Hollis, T.6
  • 52
    • 65549101461 scopus 로고    scopus 로고
    • DNA binding induces active site conformational change in the human TREX2 3′-exonuclease
    • de Silva,U., Perrino,F.W. and Hollis,T. (2009) DNA binding induces active site conformational change in the human TREX2 3′-exonuclease. Nucleic Acids Res., 37, 2411-2417.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 2411-2417
    • de Silva, U.1    Perrino, F.W.2    Hollis, T.3
  • 53
    • 0000656815 scopus 로고
    • The deoxyribonucleases of Escherichia coli
    • Lehman,I.R. (1960) The deoxyribonucleases of Escherichia coli. J. Biol. Chem., 235, 1479-1487.
    • (1960) J. Biol. Chem. , vol.235 , pp. 1479-1487
    • Lehman, I.R.1
  • 54
    • 0033951831 scopus 로고    scopus 로고
    • AP lyases and dRPases: commonality of mechanism
    • Piersen,C.E., McCullough,A.K. and Lloyd,R.S. (2000) AP lyases and dRPases: commonality of mechanism. Mutat. Res., 459, 43-53.
    • (2000) Mutat. Res. , vol.459 , pp. 43-53
    • Piersen, C.E.1    McCullough, A.K.2    Lloyd, R.S.3
  • 55
    • 0028217623 scopus 로고
    • Escherichia coli single-stranded DNA binding protein stimulates the DNA deoxyribophosphodiesterase activity of exonuclease I
    • Sandigursky,M. and Franklin,W.A. (1994) Escherichia coli single-stranded DNA binding protein stimulates the DNA deoxyribophosphodiesterase activity of exonuclease I. Nucleic Acids Res., 22, 247-250.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 247-250
    • Sandigursky, M.1    Franklin, W.A.2
  • 56
    • 0026669836 scopus 로고
    • DNA deoxyribophosphodiesterase of Escherichia coli is associated with exonuclease I
    • Sandigursky,M. and Franklin,W.A. (1992) DNA deoxyribophosphodiesterase of Escherichia coli is associated with exonuclease I. Nucleic Acids Res., 20, 4699-4703.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4699-4703
    • Sandigursky, M.1    Franklin, W.A.2
  • 57
    • 13444301391 scopus 로고    scopus 로고
    • Contact with host cells induces a DNA repair system in pathogenic Neisseriae
    • Morelle,S., Carbonnelle,E., Matic,I. and Nassif,X. (2005) Contact with host cells induces a DNA repair system in pathogenic Neisseriae. Mol. Microbiol., 55, 853-861.
    • (2005) Mol. Microbiol. , vol.55 , pp. 853-861
    • Morelle, S.1    Carbonnelle, E.2    Matic, I.3    Nassif, X.4
  • 59
    • 0029929392 scopus 로고    scopus 로고
    • Protein-protein interactions between the Escherichia coli single-stranded DNA-binding protein and exonuclease I
    • Sandigursky,M., Mendez,F., Bases,R.E., Matsumoto,T. and Franklin,W.A. (1996) Protein-protein interactions between the Escherichia coli single-stranded DNA-binding protein and exonuclease I. Radiat. Res., 145, 619-623.
    • (1996) Radiat. Res. , vol.145 , pp. 619-623
    • Sandigursky, M.1    Mendez, F.2    Bases, R.E.3    Matsumoto, T.4    Franklin, W.A.5
  • 60
    • 33746522319 scopus 로고    scopus 로고
    • A distinct TthMutY bifunctional glycosylase that hydrolyzes not only adenine but also thymine opposite 8-oxoguanine in the hyperthermophilic bacterium. Thermus thermophilus
    • Back,J.H., Park,J.H., Chung,J.H., Kim,D.S.H.L. and Han,Y.S. (2006) A distinct TthMutY bifunctional glycosylase that hydrolyzes not only adenine but also thymine opposite 8-oxoguanine in the hyperthermophilic bacterium, Thermus thermophilus. DNA Repair, 5, 894-903.
    • (2006) DNA Repair , vol.5 , pp. 894-903
    • Back, J.H.1    Park, J.H.2    Chung, J.H.3    Kim, D.S.H.L.4    Han, Y.S.5
  • 63
    • 0035808729 scopus 로고    scopus 로고
    • Endonuclease V of Escherichia coli prevents mutations from nitrosative deamination during nitrate/nitrite respiration
    • Weiss,B. (2001) Endonuclease V of Escherichia coli prevents mutations from nitrosative deamination during nitrate/nitrite respiration. Mutat. Res., 461, 301-309.
    • (2001) Mutat. Res. , vol.461 , pp. 301-309
    • Weiss, B.1
  • 64
    • 0242380643 scopus 로고    scopus 로고
    • Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V
    • Moe,A., Ringvoll,J., Nordstrand,L.M., Eide,L., Bjoras,M., Seeberg,E., Rognes,T. and Klungland,A. (2003) Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V. Nucleic Acids Res., 31, 3893-3900.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3893-3900
    • Moe, A.1    Ringvoll, J.2    Nordstrand, L.M.3    Eide, L.4    Bjoras, M.5    Seeberg, E.6    Rognes, T.7    Klungland, A.8
  • 65
    • 33644619706 scopus 로고    scopus 로고
    • Prokaryotic nucleotide excision repair: the UvrABC system
    • Truglio,J.J., Croteau,D.L., Van Houten,B. and Kisker,C. (2006) Prokaryotic nucleotide excision repair: the UvrABC system. Chem. Rev., 106, 233-252.
    • (2006) Chem. Rev. , vol.106 , pp. 233-252
    • Truglio, J.J.1    Croteau, D.L.2    Van Houten, B.3    Kisker, C.4
  • 66
    • 0035902521 scopus 로고    scopus 로고
    • Participation of recombination proteins in rescue of arrested replication forks in UV-irradiated Escherichia coli need not involve recombination
    • Courcelle,J. and Hanawalt,P.C. (2001) Participation of recombination proteins in rescue of arrested replication forks in UV-irradiated Escherichia coli need not involve recombination. Proc. Natl Acad. Sci. USA, 98, 8196-8202.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8196-8202
    • Courcelle, J.1    Hanawalt, P.C.2
  • 67
  • 68
    • 14544272738 scopus 로고    scopus 로고
    • Effects of recJ, recQ, and recFOR mutations on recombination in nuclease-deficient recB recD double mutants of Escherichia coli
    • Ivancic-Bace,I., Salaj-Smic,E. and Brcic-Kostic,K. (2005) Effects of recJ, recQ, and recFOR mutations on recombination in nuclease-deficient recB recD double mutants of Escherichia coli. J. Bacteriol., 187, 1350-1356.
    • (2005) J. Bacteriol. , vol.187 , pp. 1350-1356
    • Ivancic-Bace, I.1    Salaj-Smic, E.2    Brcic-Kostic, K.3
  • 69
    • 73149087453 scopus 로고    scopus 로고
    • Transcription profile of Thermus thermophilus CRISPR systems after phage infection
    • Agari,Y., Sakamoto,K., Tamakoshi,M., Oshima,T., Kuramitsu,S. and Shinkai,A. (2010) Transcription profile of Thermus thermophilus CRISPR systems after phage infection. J. Mol. Biol., 395, 270-281.
    • (2010) J. Mol. Biol. , vol.395 , pp. 270-281
    • Agari, Y.1    Sakamoto, K.2    Tamakoshi, M.3    Oshima, T.4    Kuramitsu, S.5    Shinkai, A.6
  • 70
    • 39149142575 scopus 로고    scopus 로고
    • CRISPR-a widespread system that provides acquired resistance against phages in bacteria and archaea
    • Sorek,R., Kunin,V. and Hugenholtz,P. (2008) CRISPR-a widespread system that provides acquired resistance against phages in bacteria and archaea. Nat. Rev. Microbiol., 6, 181-186.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 181-186
    • Sorek, R.1    Kunin, V.2    Hugenholtz, P.3
  • 71
    • 60149089144 scopus 로고    scopus 로고
    • Regulatory RNAs in bacteria
    • Waters,L.S. and Storz,G. (2009) Regulatory RNAs in bacteria. Cell, 136, 615-628.
    • (2009) Cell , vol.136 , pp. 615-628
    • Waters, L.S.1    Storz, G.2
  • 72


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