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Volumn 424, Issue 1-2, 1999, Pages 221-236

DNA polymerase mutagenic bypass and proofreading of endogenous DNA lesions

Author keywords

Alkylation mutagenesis; DNA polymerase; Error discrimination; HSV thymidine kinase; Proofreading exonuclease; Translesion synthesis

Indexed keywords

DNA POLYMERASE; ETHYLNITROSOUREA; EXONUCLEASE; METHYLNITROSOUREA; THYMIDINE KINASE;

EID: 0033535426     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0027-5107(99)00021-4     Document Type: Article
Times cited : (22)

References (58)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature. 362:1993;709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 0025980239 scopus 로고
    • 6-methylguanine-DNA-methyltransferase
    • 6-methylguanine-DNA-methyltransferase. J. Bacteriol. 173:1991;2068-2076.
    • (1991) J. Bacteriol. , vol.173 , pp. 2068-2076
    • Rebeck, G.W.1    Samson, L.2
  • 3
    • 0027477075 scopus 로고
    • In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells
    • Xiao W., Samson L. In vivo evidence for endogenous DNA alkylation damage as a source of spontaneous mutation in eukaryotic cells. Proc. Natl. Acad. Sci. USA. 90:1993;2117-2121.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2117-2121
    • Xiao, W.1    Samson, L.2
  • 4
    • 0025864553 scopus 로고
    • Cellular role of yeast Apn 1 apurinic endonuclease/3′ diesterase: Repair of oxidative and alkylation DNA damage and control of spontaneous mutation
    • Ramotar D., Popoff S.C., Gralla E.B., Demple B. Cellular role of yeast Apn 1 apurinic endonuclease/3′ diesterase: repair of oxidative and alkylation DNA damage and control of spontaneous mutation. Mol. Cell. Biol. 11:1991;4537-4544.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4537-4544
    • Ramotar, D.1    Popoff, S.C.2    Gralla, E.B.3    Demple, B.4
  • 5
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • Maki H., Sekiguchi M. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis. Nature. 355:1992;273-275.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 6
    • 0028206048 scopus 로고
    • Function and structure relationships in DNA polymerases
    • Joyce C.M., Steitz T.A. Function and structure relationships in DNA polymerases. Annu. Rev. Biochem. 63:1994;777-822.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 777-822
    • Joyce, C.M.1    Steitz, T.A.2
  • 7
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublie S., Tabor S., Long A.M., Richardson C.C., Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature. 391:1998;251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 8
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structure of human DNA polymerase β complexed with DNA: Implications for catalytic mechanism, processivity and fidelity
    • Pelletier H., Sawaya M.R., Wolfle W., Kraut J. Crystal structure of human DNA polymerase β complexed with DNA: implications for catalytic mechanism, processivity and fidelity. Biochemistry. 35:1996;12742-12761.
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfle, W.3    Kraut, J.4
  • 9
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69
    • Wang J., Sattar A.K.M.A., Wang C.C., Karam J.D., Konigsberg W.H., Steitz T.A. Crystal structure of a pol α family replication DNA polymerase from bacteriophage RB69. Cell. 89:1997;1087-1099.
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1    Sattar, A.K.M.A.2    Wang, C.C.3    Karam, J.D.4    Konigsberg, W.H.5    Steitz, T.A.6
  • 10
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • Steitz T.A. A mechanism for all polymerases. Nature. 391:1998;231-232.
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 11
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
    • Kiefer J.R., Mao C., Braman J.C., Beese L.S. Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Nature. 391:1998;304-307.
    • (1998) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 12
    • 0023770718 scopus 로고
    • Kinetic mechanism whereby DNA polymerase I (Klenow) replicates DNA with high fidelity
    • Kuchta R.D., Benkovic P., Benkovic S.J. Kinetic mechanism whereby DNA polymerase I (Klenow) replicates DNA with high fidelity. Biochemistry. 27:1988;6716-6725.
    • (1988) Biochemistry , vol.27 , pp. 6716-6725
    • Kuchta, R.D.1    Benkovic, P.2    Benkovic, S.J.3
  • 13
    • 0000984220 scopus 로고
    • Mechanistic aspects of DNA polymerases: Escherichia coli DNA polymerase I (Klenow fragment) as a paradigm
    • Carroll S.S., Benkovic S.J. Mechanistic aspects of DNA polymerases: Escherichia coli DNA polymerase I (Klenow fragment) as a paradigm. Chem. Rev. 90:1990;1291-1307.
    • (1990) Chem. Rev. , vol.90 , pp. 1291-1307
    • Carroll, S.S.1    Benkovic, S.J.2
  • 14
    • 0027220197 scopus 로고
    • Conformational coupling in DNA replication fidelity
    • Johnson K.A. Conformational coupling in DNA replication fidelity. Annu. Rev. Biochem. 62:1993;685-713.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 685-713
    • Johnson, K.A.1
  • 15
    • 0025783442 scopus 로고
    • Fidelity mechanisms in DNA replication
    • Echols H., Goodman M.F. Fidelity mechanisms in DNA replication. Annu. Rev. Biochem. 60:1991;477-511.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 477-511
    • Echols, H.1    Goodman, M.F.2
  • 17
    • 0023696960 scopus 로고
    • Recent studies of the fidelity of DNA synthesis
    • Kunkel T.A., Bebenek K. Recent studies of the fidelity of DNA synthesis. Biochem. Biophys. Acta. 951:1988;1-15.
    • (1988) Biochem. Biophys. Acta , vol.951 , pp. 1-15
    • Kunkel, T.A.1    Bebenek, K.2
  • 19
    • 0030986238 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen promotes DNA synthesis past template lesions by mammalian DNA polymerase δ
    • Mozzherin D.J., Shibutani S., Tan C.-K., Downey K.M., Fisher P.A. Proliferating cell nuclear antigen promotes DNA synthesis past template lesions by mammalian DNA polymerase δ Proc. Natl. Acad. Sci. USA. 94:1997;6126-6131.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6126-6131
    • Mozzherin, D.J.1    Shibutani, S.2    Tan, C.-K.3    Downey, K.M.4    Fisher, P.A.5
  • 20
    • 0022399410 scopus 로고
    • Mechanisms of carcinogenesis induced by alkylating agents
    • Saffhill R., Margison G., O'Connor P. Mechanisms of carcinogenesis induced by alkylating agents. Biochim. Biophys. Acta. 823:1985;111-145.
    • (1985) Biochim. Biophys. Acta , vol.823 , pp. 111-145
    • Saffhill, R.1    Margison, G.2    O'Connor, P.3
  • 21
    • 0028151464 scopus 로고
    • DNA damages processed by base excision repair: Biological consequences
    • Wallace S.S. DNA damages processed by base excision repair: biological consequences. Int. J. Radiat. Biol. 66:1994;579-589.
    • (1994) Int. J. Radiat. Biol. , vol.66 , pp. 579-589
    • Wallace, S.S.1
  • 22
    • 0021811720 scopus 로고
    • In vitro miscoding of alkylthymines with DNA and RNA polymerases
    • Saffhill R. In vitro miscoding of alkylthymines with DNA and RNA polymerases. Chem. Biol. Interact. 53:1985;121-130.
    • (1985) Chem. Biol. Interact. , vol.53 , pp. 121-130
    • Saffhill, R.1
  • 25
    • 0028990982 scopus 로고
    • 6-methylguanine-induced replication blocks
    • 6-methylguanine-induced replication blocks. Carcinogenesis. 16:1995;1775-1782.
    • (1995) Carcinogenesis , vol.16 , pp. 1775-1782
    • Voigt, J.M.1    Topal, M.D.2
  • 26
    • 0029661257 scopus 로고    scopus 로고
    • 6-methylguanine by human DNA polymerase β in vitro
    • 6-methylguanine by human DNA polymerase β in vitro. J. Biol. Chem. 271:1996;28391-28398.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28391-28398
    • Singh, J.1    Su, L.2    Snow, E.T.3
  • 28
    • 0030738503 scopus 로고    scopus 로고
    • Development and use of an in vitro HSV-tk forward mutation assay to study eukaryotic DNA polymerase processing of DNA alkyl lesions
    • Eckert K.A., Hile S.E., Vargo P.L. Development and use of an in vitro HSV-tk forward mutation assay to study eukaryotic DNA polymerase processing of DNA alkyl lesions. Nucleic Acids Res. 25:1997;1450-1457.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1450-1457
    • Eckert, K.A.1    Hile, S.E.2    Vargo, P.L.3
  • 29
    • 0021099440 scopus 로고
    • Depurination-induced infidelity of deoxyribonucleic acid synthesis with purified deoxyribonucleic acid replication proteins in vitro
    • Kunkel T.A., Schaaper R.M., Loeb L.A. Depurination-induced infidelity of deoxyribonucleic acid synthesis with purified deoxyribonucleic acid replication proteins in vitro. Biochemistry. 22:1983;2378-2384.
    • (1983) Biochemistry , vol.22 , pp. 2378-2384
    • Kunkel, T.A.1    Schaaper, R.M.2    Loeb, L.A.3
  • 30
    • 0027983133 scopus 로고
    • Oxygen radical induced mutagenesis is DNA polymerase specific
    • Feig D.I., Loeb L.A. Oxygen radical induced mutagenesis is DNA polymerase specific. J. Mol. Biol. 235:1994;33-41.
    • (1994) J. Mol. Biol. , vol.235 , pp. 33-41
    • Feig, D.I.1    Loeb, L.A.2
  • 31
    • 0024214186 scopus 로고
    • Molecular analysis of mutations induced in human cells by N-ethyl-N-nitrosourea
    • Eckert K.A., Ingle C.A., Klinedinst D.K., Drinkwater N.R. Molecular analysis of mutations induced in human cells by N-ethyl-N-nitrosourea. Mol. Carcinog. 1:1988;50-56.
    • (1988) Mol. Carcinog. , vol.1 , pp. 50-56
    • Eckert, K.A.1    Ingle, C.A.2    Klinedinst, D.K.3    Drinkwater, N.R.4
  • 32
    • 0024367969 scopus 로고
    • N-Ethyl-N-nitrosourea induces A:T to C:G transversion mutations as well as transition mutations in SOS-induced Escherichia coli
    • Eckert K.A., Ingle C.A., Drinkwater N.R. N-Ethyl-N-nitrosourea induces A:T to C:G transversion mutations as well as transition mutations in SOS-induced Escherichia coli. Carcinogenesis. 10:1989;2261-2267.
    • (1989) Carcinogenesis , vol.10 , pp. 2261-2267
    • Eckert, K.A.1    Ingle, C.A.2    Drinkwater, N.R.3
  • 33
    • 0025831694 scopus 로고
    • Site-specific mutagenesis: Retrospective and prospective
    • Singer B., Essigmann J.M. Site-specific mutagenesis: retrospective and prospective. Carcinogenesis. 12:1991;949-955.
    • (1991) Carcinogenesis , vol.12 , pp. 949-955
    • Singer, B.1    Essigmann, J.M.2
  • 34
    • 0026019625 scopus 로고
    • Structural basis for the 3′→5′ exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
    • Beese L.S., Steitz T.A. Structural basis for the 3′→5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. EMBO J. 10:1991;25-33.
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 35
    • 0026085471 scopus 로고
    • The 3′→5′ exonuclease of DNA polymerase I of Escherichia coli: Contribution of each amino acid at the active site to the reaction
    • Derbyshire V., Grindley N.D.F., Joyce C.M. The 3′→5′ exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. EMBO J. 10:1991;17-24.
    • (1991) EMBO J. , vol.10 , pp. 17-24
    • Derbyshire, V.1    Grindley, N.D.F.2    Joyce, C.M.3
  • 37
    • 0023275843 scopus 로고
    • RecA-dependent and recA-independent N-Ethyl-N-nitrosourea mutagenesis at a plasmid-encoded herpes simplex virus thymidine kinase gene in Escherichia coli
    • Eckert K.A., Drinkwater N.R. recA-dependent and recA-independent N-Ethyl-N-nitrosourea mutagenesis at a plasmid-encoded herpes simplex virus thymidine kinase gene in Escherichia coli. Mutat. Res. 178:1987;1-10.
    • (1987) Mutat. Res. , vol.178 , pp. 1-10
    • Eckert, K.A.1    Drinkwater, N.R.2
  • 38
    • 0032562169 scopus 로고    scopus 로고
    • Mutator form of polymerase β with amino acid substitution at tyrosine 265 in the hinge region displays an increase in both base substitution and frameshift errors
    • Opresko P.L., Sweasy J.B., Eckert K.A. Mutator form of polymerase β with amino acid substitution at tyrosine 265 in the hinge region displays an increase in both base substitution and frameshift errors. Biochemistry. 37:1998;2111-2119.
    • (1998) Biochemistry , vol.37 , pp. 2111-2119
    • Opresko, P.L.1    Sweasy, J.B.2    Eckert, K.A.3
  • 39
    • 0002602003 scopus 로고
    • The fidelity of polymerases used in the PCR
    • in: M.J. McPherson, P. Quirke, G.R. Taylor (Eds.) Oxford Univ. Press, New York
    • K.A. Eckert, T.A. Kunkel, The fidelity of polymerases used in the PCR, in: M.J. McPherson, P. Quirke, G.R. Taylor (Eds.), PCR: A Practical Approach, Oxford Univ. Press, New York, 1991, pp. 225-244.
    • (1991) PCR: A Practical Approach , pp. 225-244
    • Eckert, K.A.1    Kunkel, T.A.2
  • 40
    • 0019877448 scopus 로고
    • On the fidelity of DNA replication. Effect of the next nucleotide on proofreading
    • Kunkel T.A., Schaaper R.M., Beckman R.A., Loeb L.A. On the fidelity of DNA replication. Effect of the next nucleotide on proofreading. J. Biol. Chem. 256:1981;9883-9889.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9883-9889
    • Kunkel, T.A.1    Schaaper, R.M.2    Beckman, R.A.3    Loeb, L.A.4
  • 41
    • 0000348649 scopus 로고
    • The difference between spontaneous and base-analogue induced mutations of phage T4
    • Freese E. The difference between spontaneous and base-analogue induced mutations of phage T4. Proc. Natl. Acad. Sci. USA. 45:1959;622-633.
    • (1959) Proc. Natl. Acad. Sci. USA , vol.45 , pp. 622-633
    • Freese, E.1
  • 42
    • 0031426032 scopus 로고    scopus 로고
    • 6-alkylguanine-DNA-methyltransferase deficient cells
    • 6-alkylguanine-DNA-methyltransferase deficient cells. Carcinogenesis. 18:1997;1561-1567.
    • (1997) Carcinogenesis , vol.18 , pp. 1561-1567
    • Sedgwick, B.1
  • 44
    • 0026357568 scopus 로고
    • 6-methylguanine paired with cytosine or thymine in defined oligonucleotide sequences
    • 6-methylguanine paired with cytosine or thymine in defined oligonucleotide sequences. Biochemistry. 30:1991;11595-11599.
    • (1991) Biochemistry , vol.30 , pp. 11595-11599
    • Dosanjh, M.K.1    Galeros, G.2    Goodman, M.F.3    Singer, B.4
  • 45
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani S., Takeshita M., Grollman A.P. Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature. 349:1991;431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 46
    • 0028341311 scopus 로고
    • Major oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil, exhibit sequence context-dependent mispairing in vitro
    • Purmal A.A., Kow Y.W., Wallace S.S. Major oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil, exhibit sequence context-dependent mispairing in vitro. Nucleic Acids Res. 22:1994;72-78.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 72-78
    • Purmal, A.A.1    Kow, Y.W.2    Wallace, S.S.3
  • 47
    • 0028266940 scopus 로고
    • DNA replication fidelity with 8-oxodeoxyguanosine triphosphate
    • Pavlov Y.I., Minnick D.T., Izuta S., Kunkel T.A. DNA replication fidelity with 8-oxodeoxyguanosine triphosphate. Biochemistry. 33:1994;4695-4701.
    • (1994) Biochemistry , vol.33 , pp. 4695-4701
    • Pavlov, Y.I.1    Minnick, D.T.2    Izuta, S.3    Kunkel, T.A.4
  • 48
    • 0028566564 scopus 로고
    • The fidelity of the human leading and lagging strand DNA replication apparatus with 8-oxodeoxyguanosine triphosphate
    • Minnick D.T., Pavlov Y.I., Kunkel T.A. The fidelity of the human leading and lagging strand DNA replication apparatus with 8-oxodeoxyguanosine triphosphate. Nucleic Acids Res. 22:1994;5658-5664.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5658-5664
    • Minnick, D.T.1    Pavlov, Y.I.2    Kunkel, T.A.3
  • 49
    • 0032488631 scopus 로고    scopus 로고
    • Uracil glycol deoxynucleoside triphosphate is a better substrate for DNA polymerase I Klenow fragment that thymine glycol deoxynucleoside triphosphate
    • Purmal A.A., Bond J.P., Lyons B.A., Kow Y.W., Wallace S.S. Uracil glycol deoxynucleoside triphosphate is a better substrate for DNA polymerase I Klenow fragment that thymine glycol deoxynucleoside triphosphate. Biochemistry. 37:1998;330-338.
    • (1998) Biochemistry , vol.37 , pp. 330-338
    • Purmal, A.A.1    Bond, J.P.2    Lyons, B.A.3    Kow, Y.W.4    Wallace, S.S.5
  • 51
    • 0031038053 scopus 로고    scopus 로고
    • Abasic translesion synthesis by DNA polymerase β violates the 'A-rule'
    • Efrati E., Tocco G., Eritja R., Wilson S., Goodman M. Abasic translesion synthesis by DNA polymerase β violates the 'A-rule'. J. Biol. Chem. 272:1997;2559-2569.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2559-2569
    • Efrati, E.1    Tocco, G.2    Eritja, R.3    Wilson, S.4    Goodman, M.5
  • 53
    • 0027231782 scopus 로고
    • Structure of DNA polymerase I Klenow fragment bound to duplex DNA
    • Beese L.S., Derbyshire V., Steitz T.A. Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Science. 260:1993;352-355.
    • (1993) Science , vol.260 , pp. 352-355
    • Beese, L.S.1    Derbyshire, V.2    Steitz, T.A.3
  • 54
    • 0029744345 scopus 로고    scopus 로고
    • Mechanism of translesion DNA synthesis by DNA polymerase II: Comparison to DNA polymerases I and III core
    • Paz-Elizur T., Takeshita M., Goodman M., O'Donnell M., Livneh Z. Mechanism of translesion DNA synthesis by DNA polymerase II: comparison to DNA polymerases I and III core. J. Biol. Chem. 271:1996;24662-24669.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24662-24669
    • Paz-Elizur, T.1    Takeshita, M.2    Goodman, M.3    O'Donnell, M.4    Livneh, Z.5
  • 57
    • 0027983621 scopus 로고
    • 5-Hydroxypyrimidine deoxynucleoside triphosphates are more efficiently incorporated into DNA by exonuclease-free Klenow fragment than 8-oxopurine deoxynucleoside triphosphates
    • Purmal A.A., Kow Y.W., Wallace S.S. 5-Hydroxypyrimidine deoxynucleoside triphosphates are more efficiently incorporated into DNA by exonuclease-free Klenow fragment than 8-oxopurine deoxynucleoside triphosphates. Nucleic Acids Res. 22:1994;3930-3935.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3930-3935
    • Purmal, A.A.1    Kow, Y.W.2    Wallace, S.S.3
  • 58
    • 0032480954 scopus 로고    scopus 로고
    • Alkylation-induced frameshift mutagenesis during in vitro DNA synthesis by DNA polymerases α and β
    • Eckert K.A., Hile S.E. Alkylation-induced frameshift mutagenesis during in vitro DNA synthesis by DNA polymerases α and β Mutation Research. 422:1998;255-269.
    • (1998) Mutation Research , vol.422 , pp. 255-269
    • Eckert, K.A.1    Hile, S.E.2


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