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Volumn 12, Issue 6, 2004, Pages 288-295

Error-prone replication for better or worse

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; EXONUCLEASE; REPLICATION FACTOR C;

EID: 2542440567     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2004.04.004     Document Type: Review
Times cited : (107)

References (63)
  • 1
  • 2
    • 0035997344 scopus 로고    scopus 로고
    • Error-prone repair DNA polymerases in prokaryotes and eukaryotes
    • Goodman M.F. Error-prone repair DNA polymerases in prokaryotes and eukaryotes. Annu. Rev. Biochem. 71:2002;17-50
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 17-50
    • Goodman, M.F.1
  • 3
    • 0037172966 scopus 로고    scopus 로고
    • SOS-induced DNA polymerases enhance long-term survival and evolutionary fitness
    • Yeiser B., et al. SOS-induced DNA polymerases enhance long-term survival and evolutionary fitness. Proc. Natl. Acad. Sci. U. S. A. 99:2002;8737-8741
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8737-8741
    • Yeiser, B.1
  • 4
    • 0035941008 scopus 로고    scopus 로고
    • Two essential DNA polymerases at the bacterial replication fork
    • Dervyn E., et al. Two essential DNA polymerases at the bacterial replication fork. Science. 294:2001;1716-1719
    • (2001) Science , vol.294 , pp. 1716-1719
    • Dervyn, E.1
  • 5
    • 0035213509 scopus 로고    scopus 로고
    • Genetic identification of two distinct DNA polymerases, DnaE and PolC, that are essential for chromosomal DNA replication in Staphylococcus aureus
    • Inoue R., et al. Genetic identification of two distinct DNA polymerases, DnaE and PolC, that are essential for chromosomal DNA replication in Staphylococcus aureus. Mol. Genet. Genomics. 266:2001;564-571
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 564-571
    • Inoue, R.1
  • 6
    • 0035679232 scopus 로고    scopus 로고
    • Recombinational DNA repair of damaged replication forks in Escherichia coli: Questions
    • Cox M.M. Recombinational DNA repair of damaged replication forks in Escherichia coli: questions. Annu. Rev. Genet. 35:2001;53-82
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 53-82
    • Cox, M.M.1
  • 7
    • 17944380943 scopus 로고    scopus 로고
    • The Y-family of DNA polymerases
    • Ohmori H., et al. The Y-family of DNA polymerases. Mol. Cell. 8:2001;7-8
    • (2001) Mol. Cell , vol.8 , pp. 7-8
    • Ohmori, H.1
  • 8
    • 0034720286 scopus 로고    scopus 로고
    • Roles of E. coli DNA polymerases IV and V in lesion-targeted and untargeted mutagenesis
    • Tang M., et al. Roles of E. coli DNA polymerases IV and V in lesion-targeted and untargeted mutagenesis. Nature. 404:2000;1014-1018
    • (2000) Nature , vol.404 , pp. 1014-1018
    • Tang, M.1
  • 9
    • 0034669125 scopus 로고    scopus 로고
    • All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis
    • Napolitano R., et al. All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis. EMBO J. 19:2000;6259-6265
    • (2000) EMBO J. , vol.19 , pp. 6259-6265
    • Napolitano, R.1
  • 10
    • 0037072865 scopus 로고    scopus 로고
    • Fidelity of Escherichia coli DNA polymerase IV: Prefential generation of small deletion mutations by dNTP-stabilized misalignment
    • Kobayashi S., et al. Fidelity of Escherichia coli DNA polymerase IV: prefential generation of small deletion mutations by dNTP-stabilized misalignment. J. Biol. Chem. 277:2002;34198-34207
    • (2002) J. Biol. Chem. , vol.277 , pp. 34198-34207
    • Kobayashi, S.1
  • 11
    • 0242362731 scopus 로고    scopus 로고
    • Analysis of translesion replication across an abasic site by DNA polymerase IV of Escherichia coli
    • Maor-Shoshani A.M., et al. Analysis of translesion replication across an abasic site by DNA polymerase IV of Escherichia coli. DNA Repair (Amst.). 2:2003;1227-1238
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1227-1238
    • Maor-Shoshani, A.M.1
  • 12
    • 0022515733 scopus 로고
    • Role of RecA protein in untargeted UV mutagenesis of bacteriophage λ: Evidence for the requirement for the dinB gene
    • Brotcorne-Lannoye A., Maenhaut-Michel G. Role of RecA protein in untargeted UV mutagenesis of bacteriophage λ: Evidence for the requirement for the dinB gene. Proc. Natl. Acad. Sci. U. S. A. 83:1986;3904-3908
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 3904-3908
    • Brotcorne-Lannoye, A.1    Maenhaut-Michel, G.2
  • 13
    • 0034789619 scopus 로고    scopus 로고
    • Role of chromosomal and episomal dinB genes encoding DNA pol IV in targeted and untargeted mutagenesis in Escherichia coli
    • Kim S., et al. Role of chromosomal and episomal dinB genes encoding DNA pol IV in targeted and untargeted mutagenesis in Escherichia coli. Mol. Genet. Genomics. 266:2001;207-215
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 207-215
    • Kim, S.1
  • 14
    • 0037085366 scopus 로고    scopus 로고
    • Efficiency and Accuracy of SOS-induced DNA polymerases replicating benzo[a]pyrene-7,8-diol 9,10-epoxide a and G adducts
    • Shen X., et al. Efficiency and Accuracy of SOS-induced DNA polymerases replicating benzo[a]pyrene-7, 8-diol 9, 10-epoxide A and G adducts. J. Biol. Chem. 277:2002;5265-5274
    • (2002) J. Biol. Chem. , vol.277 , pp. 5265-5274
    • Shen, X.1
  • 15
    • 0036012786 scopus 로고    scopus 로고
    • Genetics of mutagenesis in E. coli: Various combinations of translesion polymerases (Pol II, IV and V) deal with lesion/sequence context diversity
    • Wagner J., et al. Genetics of mutagenesis in E. coli: various combinations of translesion polymerases (Pol II, IV and V) deal with lesion/sequence context diversity. DNA Repair (Amst.). 1:2002;159-167
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 159-167
    • Wagner, J.1
  • 16
    • 0033529763 scopus 로고    scopus 로고
    • 2C is an error-prone DNA polymerase, Escherichia coli pol V
    • 2C is an error-prone DNA polymerase, Escherichia coli pol V. Proc. Natl. Acad. Sci. U. S. A. 96:1999;8919-8924
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8919-8924
    • Tang, M.1
  • 17
    • 0033527533 scopus 로고    scopus 로고
    • The mutagenic protein UmuC is a DNA polymerase activated by UmuD′, RecA, and SSB and is specialized for translesion replication
    • Reuven N.B., et al. The mutagenic protein UmuC is a DNA polymerase activated by UmuD′, RecA, and SSB and is specialized for translesion replication. J. Biol. Chem. 274:1999;31763-31766
    • (1999) J. Biol. Chem. , vol.274 , pp. 31763-31766
    • Reuven, N.B.1
  • 18
    • 0032544079 scopus 로고    scopus 로고
    • 2′C mutagenic complex and RecA protein
    • 2′C mutagenic complex and RecA protein. Proc. Natl. Acad. Sci. U. S. A. 95:1998;9755-9760
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9755-9760
    • Tang, M.1
  • 19
    • 0035905817 scopus 로고    scopus 로고
    • A model for SOS-lesion targeted mutations in E. coli involving pol V, RecA, SSB and β sliding clamp
    • Pham P., et al. A model for SOS-lesion targeted mutations in E. coli involving pol V, RecA, SSB and β sliding clamp. Nature. 409:2001;366-370
    • (2001) Nature , vol.409 , pp. 366-370
    • Pham, P.1
  • 20
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ
    • Kuzminov A. Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ Microbiol. Mol. Biol. Rev. 63:1999;751-813
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 21
    • 0024583633 scopus 로고
    • New recA mutations that dissociate the various reca protein activities in Escherichia coli provide evidence for an additional role for reca protein in UV mutagenesis
    • Dutreix M., et al. New recA mutations that dissociate the various reca protein activities in Escherichia coli provide evidence for an additional role for reca protein in UV mutagenesis. J. Bacteriol. 171:1989;2415-2423
    • (1989) J. Bacteriol. , vol.171 , pp. 2415-2423
    • Dutreix, M.1
  • 22
    • 0025314791 scopus 로고
    • RecA protein of Escherichia coli has a third essential role in SOS mutator activity
    • Sweasy J.B., et al. RecA protein of Escherichia coli has a third essential role in SOS mutator activity. J. Bacteriol. 172:1990;3030-3036
    • (1990) J. Bacteriol. , vol.172 , pp. 3030-3036
    • Sweasy, J.B.1
  • 23
    • 0037143704 scopus 로고    scopus 로고
    • Two distinct modes of RecA action are required for DNA polymerase V-catalyzed tranlesion synthesis
    • Pham P., et al. Two distinct modes of RecA action are required for DNA polymerase V-catalyzed tranlesion synthesis. Proc. Natl. Acad. Sci. U. S. A. 99:2002;11061-11066
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11061-11066
    • Pham, P.1
  • 24
    • 0025909497 scopus 로고
    • A RecA protein mutant deficient in its interaction with the UmuDC complex
    • Bailone A., et al. A RecA protein mutant deficient in its interaction with the UmuDC complex. Biochimie. 73:1991;479-484
    • (1991) Biochimie , vol.73 , pp. 479-484
    • Bailone, A.1
  • 25
    • 0030849316 scopus 로고    scopus 로고
    • - recombination by the mutagenesis complex UmuD′C
    • - recombination by the mutagenesis complex UmuD′C. J. Mol. Biol. 270:1997;201-211
    • (1997) J. Mol. Biol. , vol.270 , pp. 201-211
    • Boudsocq, F.1
  • 26
    • 0035902496 scopus 로고    scopus 로고
    • Interaction of the β sliding clamp with MutS, ligase, and DNA polymerase I
    • Lopez de Saro, F.J. and O'Donnell, M. (2001) Interaction of the β sliding clamp with MutS, ligase, and DNA polymerase I. Proc. Natl. Acad. Sci. U. S. A. 98, 8376-8380.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8376-8380
    • Lopez De Saro, F.J.1    O'Donnell, M.2
  • 27
    • 0033777562 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • Warbrick E. The puzzle of PCNA's many partners. Bioessays. 22:2000;997-1006
    • (2000) Bioessays , vol.22 , pp. 997-1006
    • Warbrick, E.1
  • 28
    • 0348134870 scopus 로고    scopus 로고
    • Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair
    • Lopez de Saro, F.J., et al. (2003) Competitive processivity-clamp usage by DNA polymerases during DNA replication and repair. EMBO J. 22, 6408-6418.
    • (2003) EMBO J , vol.22 , pp. 6408-6418
    • Lopez De Saro, F.J.1
  • 29
    • 0036171550 scopus 로고    scopus 로고
    • The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo
    • Lenne-Samuel N., et al. The processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivo. EMBO Rep. 3:2002;45-49
    • (2002) EMBO Rep. , vol.3 , pp. 45-49
    • Lenne-Samuel, N.1
  • 30
    • 0242389787 scopus 로고    scopus 로고
    • Structural basis for recruitment of translesion DNA polymerase IV/DinB to the beta-clamp
    • Bunting K.A., et al. Structural basis for recruitment of translesion DNA polymerase IV/DinB to the beta-clamp. EMBO J. 22:2003;5883-5892
    • (2003) EMBO J. , vol.22 , pp. 5883-5892
    • Bunting, K.A.1
  • 31
    • 0032535038 scopus 로고    scopus 로고
    • Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: In vitro degradation and identification of residues required for proteolysis
    • Gonzalez M., et al. Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis. Genes Dev. 12:1998;3889-3899
    • (1998) Genes Dev. , vol.12 , pp. 3889-3899
    • Gonzalez, M.1
  • 32
    • 0345687188 scopus 로고    scopus 로고
    • Distinct peptide signals in the UmuD and UmuD′ subunits of UmuD/D′ mediate tethering and substrate processing by the ClpXP protease
    • Neher S.B., et al. Distinct peptide signals in the UmuD and UmuD′ subunits of UmuD/D′ mediate tethering and substrate processing by the ClpXP protease. Proc. Natl. Acad. Sci. U. S. A. 100:2003;13219-13224
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13219-13224
    • Neher, S.B.1
  • 33
    • 0346101767 scopus 로고    scopus 로고
    • Escherichia coli DNA polymerase V subunit exchange: A post-SOS mechanism to curtail error-prone DNA synthesis
    • Shen X., et al. Escherichia coli DNA polymerase V subunit exchange: a post-SOS mechanism to curtail error-prone DNA synthesis. J. Biol. Chem. 278:2003;52546-52550
    • (2003) J. Biol. Chem. , vol.278 , pp. 52546-52550
    • Shen, X.1
  • 34
    • 0024244830 scopus 로고
    • Purification and characterization of an inducible Escherichia coli DNA polymerase capable of insertion and bypass at Abasic lesions in DNA
    • Bonner C.A., et al. Purification and characterization of an inducible Escherichia coli DNA polymerase capable of insertion and bypass at Abasic lesions in DNA. J. Biol. Chem. 263:1988;18946-18952
    • (1988) J. Biol. Chem. , vol.263 , pp. 18946-18952
    • Bonner, C.A.1
  • 35
    • 0030887046 scopus 로고    scopus 로고
    • The Escherichia coli polB locus is identical to dinA, the structural gene for DNA polymerase II: Characterization of Pol II purified from a polB mutant
    • Qiu Z., Goodman M.F. The Escherichia coli polB locus is identical to dinA, the structural gene for DNA polymerase II: characterization of Pol II purified from a polB mutant. J. Biol. Chem. 272:1997;8611-8617
    • (1997) J. Biol. Chem. , vol.272 , pp. 8611-8617
    • Qiu, Z.1    Goodman, M.F.2
  • 36
    • 0025815515 scopus 로고
    • Levels of chromasomally encoded Umu proteins and requirements for in vivo UmuD cleavage
    • Woodgate R., Ennis D.G. Levels of chromasomally encoded Umu proteins and requirements for in vivo UmuD cleavage. Mol. Gen. Genet. 229:1991;10-16
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 10-16
    • Woodgate, R.1    Ennis, D.G.2
  • 38
    • 0035265678 scopus 로고    scopus 로고
    • SOS mutator DNA polymerase IV functions in adaptive mutation and not adaptive amplification
    • McKenzie G.J., et al. SOS mutator DNA polymerase IV functions in adaptive mutation and not adaptive amplification. Mol. Cell. 7:2001;571-579
    • (2001) Mol. Cell , vol.7 , pp. 571-579
    • McKenzie, G.J.1
  • 39
    • 0029097479 scopus 로고
    • Proofreading-defective DNA polymerase II increases adaptive mutation in Escherichia coli
    • Foster P.L., et al. Proofreading-defective DNA polymerase II increases adaptive mutation in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 92:1995;7951-7955
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 7951-7955
    • Foster, P.L.1
  • 40
    • 0033613335 scopus 로고    scopus 로고
    • Enzymes of evolutionary change
    • Radman M. Enzymes of evolutionary change. Nature. 401:1999;866-869
    • (1999) Nature , vol.401 , pp. 866-869
    • Radman, M.1
  • 41
    • 0023925456 scopus 로고
    • DNA polymerase III holoenzyme of Escherichia coli
    • McHenry C.S. DNA polymerase III holoenzyme of Escherichia coli. Annu. Rev. Biochem. 57:1988;519-550
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 519-550
    • McHenry, C.S.1
  • 42
    • 0034666303 scopus 로고    scopus 로고
    • The DNA replication machine of a gram-positive organism
    • Bruck I., O'Donnell M. The DNA replication machine of a gram-positive organism. J. Biol. Chem. 275:2000;28971-28983
    • (2000) J. Biol. Chem. , vol.275 , pp. 28971-28983
    • Bruck, I.1    O'Donnell, M.2
  • 43
    • 0242666381 scopus 로고    scopus 로고
    • The essential C family DnaE polymerase is error-prone and efficient at lesion bypass
    • Bruck I., et al. The essential C family DnaE polymerase is error-prone and efficient at lesion bypass. J. Biol. Chem. 278:2003;44361-44368
    • (2003) J. Biol. Chem. , vol.278 , pp. 44361-44368
    • Bruck, I.1
  • 44
    • 0037453719 scopus 로고    scopus 로고
    • DnaE2 polymerase contributes to in vivo survival and the emergence of drug resistance in Mycobacterium tuberculosis
    • Boshoff H.I.M., et al. DnaE2 polymerase contributes to in vivo survival and the emergence of drug resistance in Mycobacterium tuberculosis. Cell. 113:2003;183-193
    • (2003) Cell , vol.113 , pp. 183-193
    • Boshoff, H.I.M.1
  • 45
    • 0036267340 scopus 로고    scopus 로고
    • Definition of the mycobacterial SOS box and use to identify LexA-regulated genes in Mycobacterium tuberculosis
    • Davis E.O., et al. Definition of the mycobacterial SOS box and use to identify LexA-regulated genes in Mycobacterium tuberculosis. J. Bacteriol. 184:2002;3287-3295
    • (2002) J. Bacteriol. , vol.184 , pp. 3287-3295
    • Davis, E.O.1
  • 46
    • 0035949599 scopus 로고    scopus 로고
    • A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems
    • Dalrymple B.P., et al. A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems. Proc. Natl. Acad. Sci. U. S. A. 98:2001;11627-11632
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11627-11632
    • Dalrymple, B.P.1
  • 47
    • 0347717893 scopus 로고    scopus 로고
    • Involvement of DnaE, the second replicative DNA polymerase from Bacillus subtilis, in DNA mutagenesis
    • Le Chatelier E., et al. Involvement of DnaE, the second replicative DNA polymerase from Bacillus subtilis, in DNA mutagenesis. J. Biol. Chem. 279:2004;1757-1767
    • (2004) J. Biol. Chem. , vol.279 , pp. 1757-1767
    • Le Chatelier, E.1
  • 48
    • 0038374522 scopus 로고    scopus 로고
    • Split dnaE genes encoding multiple novel inteins in Trichodesmium erythraeum
    • Liu X., Yang J. Split dnaE genes encoding multiple novel inteins in Trichodesmium erythraeum. J. Biol. Chem. 278:2003;26315-26318
    • (2003) J. Biol. Chem. , vol.278 , pp. 26315-26318
    • Liu, X.1    Yang, J.2
  • 49
    • 0032483013 scopus 로고    scopus 로고
    • Protein trans-splicing by a split intein encoded in a split DnaE gene of Synechocytis sp. PCC6803
    • Wu H., et al. Protein trans-splicing by a split intein encoded in a split DnaE gene of Synechocytis sp. PCC6803. Proc. Natl. Acad. Sci. U. S. A. 95:1998;9226-9231
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9226-9231
    • Wu, H.1
  • 50
    • 0037178275 scopus 로고    scopus 로고
    • Damage-repair error-prone polymerases of eubacteria: Association with mobile genetic elements
    • Permina E.A., et al. Damage-repair error-prone polymerases of eubacteria: association with mobile genetic elements. Gene. 293:2002;133-140
    • (2002) Gene , vol.293 , pp. 133-140
    • Permina, E.A.1
  • 51
    • 0035890599 scopus 로고    scopus 로고
    • Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): And archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic pol η
    • Boudsocq F., et al. Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): and archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic pol η Nucleic Acids Res. 29:2001;4607-4616
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4607-4616
    • Boudsocq, F.1
  • 52
    • 0034762679 scopus 로고    scopus 로고
    • Crystal structure of a DinB family error-prone DNA polymerase from Sulfolubus solfataricus
    • Silvian L.F., et al. Crystal structure of a DinB family error-prone DNA polymerase from Sulfolubus solfataricus. Nat. Struct. Biol. 8:2001;984-989
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 984-989
    • Silvian, L.F.1
  • 53
    • 0037205402 scopus 로고    scopus 로고
    • Low fidelity DNA synthesis by a Y family DNA polymerase due to misalignment in the active site
    • Kokoska R.J., et al. Low fidelity DNA synthesis by a Y family DNA polymerase due to misalignment in the active site. J. Biol. Chem. 277:2002;19633-19638
    • (2002) J. Biol. Chem. , vol.277 , pp. 19633-19638
    • Kokoska, R.J.1
  • 54
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • Ling H., et al. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell. 107:2001;91-102
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1
  • 55
    • 0034857266 scopus 로고    scopus 로고
    • Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classical polymerase catalytic domain
    • Zhou B.-L., et al. Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classical polymerase catalytic domain. Mol. Cell. 8:2001;427-437
    • (2001) Mol. Cell , vol.8 , pp. 427-437
    • Zhou, B.-L.1
  • 56
    • 0035861667 scopus 로고    scopus 로고
    • Synthetic activity of Sso DNA polymerase Y1, an archaeal DinB-like DNA polymerase, is stimulated by processivity factors proliferating cell nuclear antigen and replication factor C
    • Gruz P., et al. Synthetic activity of Sso DNA polymerase Y1, an archaeal DinB-like DNA polymerase, is stimulated by processivity factors proliferating cell nuclear antigen and replication factor C. J. Biol. Chem. 276:2001;47394-47401
    • (2001) J. Biol. Chem. , vol.276 , pp. 47394-47401
    • Gruz, P.1
  • 57
    • 0242317682 scopus 로고    scopus 로고
    • An error-prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses a 'steric gate' residue for discrimination against ribonucleotides
    • DeLucia A.M., et al. An error-prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses a 'steric gate' residue for discrimination against ribonucleotides. Nucleic Acids Res. 31:2003;4129-4137
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4129-4137
    • Delucia, A.M.1
  • 58
    • 0037368828 scopus 로고    scopus 로고
    • Erroneous incorporation of oxidized DNA precursors by Y-family DNA polymerases
    • Shimizu M., et al. Erroneous incorporation of oxidized DNA precursors by Y-family DNA polymerases. EMBO Rep. 4:2003;269-273
    • (2003) EMBO Rep. , vol.4 , pp. 269-273
    • Shimizu, M.1
  • 59
    • 0034677948 scopus 로고    scopus 로고
    • Fidelity of human DNA polymerase eta
    • Johnson R.E., et al. Fidelity of human DNA polymerase eta. J. Biol. Chem. 275:2000;7447-7450
    • (2000) J. Biol. Chem. , vol.275 , pp. 7447-7450
    • Johnson, R.E.1
  • 60
    • 0033578040 scopus 로고    scopus 로고
    • The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η
    • Masutani C., et al. The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η Nature. 399:1999;700-704
    • (1999) Nature , vol.399 , pp. 700-704
    • Masutani, C.1
  • 61
    • 0042881002 scopus 로고    scopus 로고
    • Sequence context-dependent replication of DNA templates containing UV-induced lesions by human DNA polymerase iota
    • Vaisman A., et al. Sequence context-dependent replication of DNA templates containing UV-induced lesions by human DNA polymerase iota. DNA Repair (Amst.). 2:2003;991-1006
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 991-1006
    • Vaisman, A.1
  • 63
    • 0035023305 scopus 로고    scopus 로고
    • Comparative gene expression profiles following UV exposure in wild-type and SOS deficient Escherichia coli
    • Courcelle J.A., et al. Comparative gene expression profiles following UV exposure in wild-type and SOS deficient Escherichia coli. Genetics. 158:2001;41-64
    • (2001) Genetics , vol.158 , pp. 41-64
    • Courcelle, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.