메뉴 건너뛰기




Volumn 44, Issue 46, 2005, Pages 15387-15395

Mechanism for N-acetyl-2-aminofluorene-induced frameshift mutagenesis by Escherichia coli DNA polymerase I (Klenow fragment)

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; BIOSYNTHESIS; CARCINOGENS; DNA; DNA SEQUENCES; ESCHERICHIA COLI; MUTAGENESIS; NITROGEN COMPOUNDS;

EID: 27944479681     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051437s     Document Type: Article
Times cited : (15)

References (37)
  • 1
    • 0028911858 scopus 로고
    • Effect of aminofluorene and (acetylamino)fluorene adducts on the DNA replication mediated by Escherichia coli polymerases I (Klenow fragment) and III
    • Doisy, R., and Tang, M. S. (1995) Effect of aminofluorene and (acetylamino)fluorene adducts on the DNA replication mediated by Escherichia coli polymerases I (Klenow fragment) and III, Biochemistry 34, 4358-4368.
    • (1995) Biochemistry , vol.34 , pp. 4358-4368
    • Doisy, R.1    Tang, M.S.2
  • 2
    • 0032168923 scopus 로고    scopus 로고
    • Mutagenic specificity of (acetylamino)fluorene-derived DNA adducts in mammalian cells
    • Shibutani, S., Suzuki, N., and Grollman, A. P. (1998) Mutagenic specificity of (acetylamino)fluorene-derived DNA adducts in mammalian cells, Biochemistry 37, 12034-12041.
    • (1998) Biochemistry , vol.37 , pp. 12034-12041
    • Shibutani, S.1    Suzuki, N.2    Grollman, A.P.3
  • 3
    • 0021873379 scopus 로고
    • DNA binding and mutation spectra of the carcinogen N-2-aminofluorene in Escherichia coli. A correlation between the conformation of the premutagenic lesion and the mutation specificity
    • Bichara, M., and Fuchs, R. P. P. (1985) DNA binding and mutation spectra of the carcinogen N-2-aminofluorene in Escherichia coli. A correlation between the conformation of the premutagenic lesion and the mutation specificity, J. Mol. Biol 183, 341-351.
    • (1985) J. Mol. Biol. , vol.183 , pp. 341-351
    • Bichara, M.1    Fuchs, R.P.P.2
  • 4
    • 84886640242 scopus 로고
    • Carcinogen-induced mutation spectrum in wild-type, uvrA and umuC strains of Escherichia coli. Strain specificity and mutation-prone sequences
    • Koffel-Schwartz, N., Verdier, J. M., Bichara, M., Freund, A. M., Daune, M. P., and Fuchs, R. P. (1984) Carcinogen-induced mutation spectrum in wild-type, uvrA and umuC strains of Escherichia coli. Strain specificity and mutation-prone sequences, J. Mol. Biol. 177, 33-51.
    • (1984) J. Mol. Biol. , vol.177 , pp. 33-51
    • Koffel-Schwartz, N.1    Verdier, J.M.2    Bichara, M.3    Freund, A.M.4    Daune, M.P.5    Fuchs, R.P.6
  • 5
    • 0028031199 scopus 로고
    • Mutagenesis at a site-specifically modified NarI sequence by acetylated and deacetylated aminofluorene adducts
    • Tebbs, R. S., and Romano, L. J. (1994) Mutagenesis at a site-specifically modified NarI sequence by acetylated and deacetylated aminofluorene adducts, Biochemistry 33, 8998-9006.
    • (1994) Biochemistry , vol.33 , pp. 8998-9006
    • Tebbs, R.S.1    Romano, L.J.2
  • 7
    • 0027935994 scopus 로고
    • Genetic toxicity of 2-acetylaminofluorene, 2-aminofluorene and some of their metabolites and model metabolites
    • Heflich, R. H., and Neft, R. E. (1994) Genetic toxicity of 2-acetylaminofluorene, 2-aminofluorene and some of their metabolites and model metabolites, Mutat. Res. 318, 73-114.
    • (1994) Mutat. Res. , vol.318 , pp. 73-114
    • Heflich, R.H.1    Neft, R.E.2
  • 8
    • 0029053782 scopus 로고
    • N-2-aminofluorene and N-2-acetylaminofluorene adducts: The local sequence context of an adduct and its chemical structure determine its replication properties
    • Belguise-Valladier, P., and Fuchs, R. P. (1995) N-2-aminofluorene and N-2-acetylaminofluorene adducts: the local sequence context of an adduct and its chemical structure determine its replication properties, J Mol. Biol. 249, 903-913.
    • (1995) J. Mol. Biol. , vol.249 , pp. 903-913
    • Belguise-Valladier, P.1    Fuchs, R.P.2
  • 9
    • 0027457947 scopus 로고
    • Structural characterization of an N-acetyl-2-aminofluorene (AAF) modified DNA oligomer by NMR, energy minimization, and molecular dynamics
    • O'Handley, S. F., Sanford, D. G., Xu, R., Lester, C. C., Hingerty, B. E., Broyde, S., and Krugh, T. R. (1993) Structural characterization of an N-acetyl-2-aminofluorene (AAF) modified DNA oligomer by NMR, energy minimization, and molecular dynamics, Biochemistry 32, 2481-2497.
    • (1993) Biochemistry , vol.32 , pp. 2481-2497
    • O'Handley, S.F.1    Sanford, D.G.2    Xu, R.3    Lester, C.C.4    Hingerty, B.E.5    Broyde, S.6    Krugh, T.R.7
  • 10
    • 0031800438 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structures of covalent aromatic amine-DNA adducts and their mutagenic relevance
    • Patel, D. J., Mao, B., Gu, Z., Hingerty, B. E., Gorin, A., Basu, A. K., and Broyde, S. (1998) Nuclear magnetic resonance solution structures of covalent aromatic amine-DNA adducts and their mutagenic relevance, Chem. Res. Toxicol. 11, 391-407.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 391-407
    • Patel, D.J.1    Mao, B.2    Gu, Z.3    Hingerty, B.E.4    Gorin, A.5    Basu, A.K.6    Broyde, S.7
  • 11
    • 0025887465 scopus 로고
    • Strong sequence-dependent polymorphism in adduct-induced DNA structure: Analysis of single N-2-acetylaminofluorene residues bound within the NarI mutation hot spot
    • Belguise-Valladier, P., and Fuchs, R. P. (1991) Strong sequence-dependent polymorphism in adduct-induced DNA structure: analysis of single N-2-acetylaminofluorene residues bound within the NarI mutation hot spot, Biochemistry 30, 10091-10100.
    • (1991) Biochemistry , vol.30 , pp. 10091-10100
    • Belguise-Valladier, P.1    Fuchs, R.P.2
  • 12
    • 0024828173 scopus 로고
    • Strong structural effect of the position of a single acetylaminofluorene adduct within a mutation hot spot
    • Koehl, P., Valladier, P., Lefevre, J. F., and Fuchs, R. P. (1989) Strong structural effect of the position of a single acetylaminofluorene adduct within a mutation hot spot, Nucleic Acids Res. 17, 9531-9541.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 9531-9541
    • Koehl, P.1    Valladier, P.2    Lefevre, J.F.3    Fuchs, R.P.4
  • 13
    • 0032512437 scopus 로고    scopus 로고
    • Rate of incision of N-acetyl-2-aminofluorene and N-2-aminofluorene adducts by UvrABC nuclease is adduct- and sequence-specific: Comparison of the rates of UvrABC nuclease incision and protein-DNA complex formation
    • Mekhovich, O., Tang, M., and Romano, L. J. (1998) Rate of incision of N-acetyl-2-aminofluorene and N-2-aminofluorene adducts by UvrABC nuclease is adduct- and sequence-specific: comparison of the rates of UvrABC nuclease incision and protein-DNA complex formation, Biochemistry 37, 571-579.
    • (1998) Biochemistry , vol.37 , pp. 571-579
    • Mekhovich, O.1    Tang, M.2    Romano, L.J.3
  • 14
    • 0033525079 scopus 로고    scopus 로고
    • Interaction of Escherichia coli DNA polymerase I (Klenow fragment) with primer-templates containing N-acetyl-2-aminofluorene or N-2-aminofluorene adducts in the active site
    • Dzantiev, L., and Romano, L. J. (1999) Interaction of Escherichia coli DNA polymerase I (Klenow fragment) with primer-templates containing N-acetyl-2-aminofluorene or N-2-aminofluorene adducts in the active site, J. Biol. Chem. 274, 3279-3284.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3279-3284
    • Dzantiev, L.1    Romano, L.J.2
  • 15
    • 0034595307 scopus 로고    scopus 로고
    • Differential effects of N-acetyl-2-aminofluorene and N-2-aminofluorene adducts on the conformational change in the structure of DNA polymerase I (Klenow fragment)
    • Dzantiev, L., and Romano, L. J. (2000) Differential effects of N-acetyl-2-aminofluorene and N-2-aminofluorene adducts on the conformational change in the structure of DNA polymerase I (Klenow fragment), Biochemistry 39, 5139-5145.
    • (2000) Biochemistry , vol.39 , pp. 5139-5145
    • Dzantiev, L.1    Romano, L.J.2
  • 16
    • 9244229513 scopus 로고    scopus 로고
    • Crystal structures of 2-acetylaminofluorene and 2-aminofluorene in complex with T7 DNA polymerase reveal mechanisms of mutagenesis
    • Dutta, S., Li, Y., Johnson, D., Dzantiev, L., Richardson, C. C., Romano, L. J., and Ellenberger, T. (2004) Crystal structures of 2-acetylaminofluorene and 2-aminofluorene in complex with T7 DNA polymerase reveal mechanisms of mutagenesis, Proc. Natl. Acad. Sci. U.S.A. 101, 16186-16191.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16186-16191
    • Dutta, S.1    Li, Y.2    Johnson, D.3    Dzantiev, L.4    Richardson, C.C.5    Romano, L.J.6    Ellenberger, T.7
  • 17
    • 0035902484 scopus 로고    scopus 로고
    • Mechanism of DNA polymerase II-mediated frameshift mutagenesis
    • Becherel, O. J., and Fuchs, R. P. (2001) Mechanism of DNA polymerase II-mediated frameshift mutagenesis, Proc. Natl. Acad. Sci. U.S.A. 98, 8566-8571.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8566-8571
    • Becherel, O.J.1    Fuchs, R.P.2
  • 18
    • 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., Janel-Bintz, R., Wagner, J., and Fuchs, R. P. (2000) All three SOS-inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis, EMBO J. 19, 6259-6265.
    • (2000) EMBO J. , vol.19 , pp. 6259-6265
    • Napolitano, R.1    Janel-Bintz, R.2    Wagner, J.3    Fuchs, R.P.4
  • 19
    • 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., and Joyce, C. M. (1991) 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, 17-24.
    • (1991) EMBO J. , vol.10 , pp. 17-24
    • Derbyshire, V.1    Grindley, N.D.2    Joyce, C.M.3
  • 20
    • 0028827318 scopus 로고
    • Purification of Escherichia coli DNA polymerase I and Klenow fragment
    • Joyce, C. M., and Derbyshire, V. (1995) Purification of Escherichia coli DNA polymerase I and Klenow fragment, Methods Enzymol. 262, 3-13.
    • (1995) Methods Enzymol. , vol.262 , pp. 3-13
    • Joyce, C.M.1    Derbyshire, V.2
  • 21
    • 0016018693 scopus 로고
    • DNA polymerase I from Escherichia coli
    • Setlow, P. (1974) DNA polymerase I from Escherichia coli, Methods Enzymol. 29, 3-12.
    • (1974) Methods Enzymol. , vol.29 , pp. 3-12
    • Setlow, P.1
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0027755201 scopus 로고
    • Solid-phase synthesis of oligonucleotides containing site-specific N-(2′-deoxyguanosin-8-yl)-2-(acetylamino)fluorene adducts using 9-fluorenylmethoxy-carbonyl as the base-protecting group
    • Zhou, Y., and Romano, L. J. (1993) Solid-phase synthesis of oligonucleotides containing site-specific N-(2′-deoxyguanosin-8-yl)-2- (acetylamino)fluorene adducts using 9-fluorenylmethoxy-carbonyl as the base-protecting group, Biochemistry 32, 14043-14052.
    • (1993) Biochemistry , vol.32 , pp. 14043-14052
    • Zhou, Y.1    Romano, L.J.2
  • 25
    • 0028817759 scopus 로고
    • A method for the purification of oligonucleotides containing strong intra- Or intermolecular interactions by reversed-phase high-performance liquid chromatography
    • Arghavani, M. B., and Romano, L. J. (1995) A method for the purification of oligonucleotides containing strong intra- or intermolecular interactions by reversed-phase high-performance liquid chromatography, Anal.Biochem 231, 201-9.
    • (1995) Anal. Biochem. , vol.231 , pp. 201-209
    • Arghavani, M.B.1    Romano, L.J.2
  • 26
    • 0028947982 scopus 로고
    • Deoxynucleoside triphosphate and pyrophosphate binding sites in the catalytically competent ternary complex for the polymerase reaction catalyzed by DNA polymerase I (Klenow fragment)
    • Astatke, M., Grindley, N. D., and Joyce, C. M. (1995) Deoxynucleoside triphosphate and pyrophosphate binding sites in the catalytically competent ternary complex for the polymerase reaction catalyzed by DNA polymerase I (Klenow fragment), J. Biol. Chem. 270, 1945-1954.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1945-1954
    • Astatke, M.1    Grindley, N.D.2    Joyce, C.M.3
  • 27
    • 0028039973 scopus 로고
    • Use of single-turnover kinetics to study bulky adduct bypass by T7 DNA polymerase
    • Lindsley, J. E., and Fuchs, R. P. (1994) Use of single-turnover kinetics to study bulky adduct bypass by T7 DNA polymerase, Biochemistry 33, 764-772.
    • (1994) Biochemistry , vol.33 , pp. 764-772
    • Lindsley, J.E.1    Fuchs, R.P.2
  • 28
    • 0033533495 scopus 로고    scopus 로고
    • Primer length dependence of binding of DNA polymerase I Klenow fragment to template-primer complexes containing site-specific bulky lesions
    • Rechkoblit, O., Amin, S., and Geacintov, N. E. (1999) Primer length dependence of binding of DNA polymerase I Klenow fragment to template-primer complexes containing site-specific bulky lesions, Biochemistry 38, 11834-11843.
    • (1999) Biochemistry , vol.38 , pp. 11834-11843
    • Rechkoblit, O.1    Amin, S.2    Geacintov, N.E.3
  • 29
    • 0034681153 scopus 로고    scopus 로고
    • A conformational change in E. coli DNA polymerase I (Klenow fragment) is induced in the presence of a dNTP complementary to the template base in the active site
    • Dzantiev, L., and Romano, L. J. (2000) A conformational change in E. coli DNA polymerase I (Klenow fragment) is induced in the presence of a dNTP complementary to the template base in the active site, Biochemistry 39, 356-361.
    • (2000) Biochemistry , vol.39 , pp. 356-361
    • Dzantiev, L.1    Romano, L.J.2
  • 30
    • 0025033234 scopus 로고
    • Position of a single acetylaminofluorene adduct within a mutational hot spot is critical for the related mutagenic event
    • Burnouf, D., Koehl, P., and Fuchs, R. P. (1990) Position of a single acetylaminofluorene adduct within a mutational hot spot is critical for the related mutagenic event, Basic Life Sci. 52, 277-287.
    • (1990) Basic Life Sci. , vol.52 , pp. 277-287
    • Burnouf, D.1    Koehl, P.2    Fuchs, R.P.3
  • 31
    • 0026055005 scopus 로고
    • Polymorphism in N-2-acetylaminofluorene induced DNA structure as revealed by DNase I footprinting
    • Veaute, X., and Fuchs, R. P. (1991) Polymorphism in N-2- acetylaminofluorene induced DNA structure as revealed by DNase I footprinting, Nucleic Acids Res. 19, 5603-5606.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5603-5606
    • Veaute, X.1    Fuchs, R.P.2
  • 32
    • 0022838294 scopus 로고
    • Energy minimized structures of carcinogen-DNA adducts: 2-acetylaminofluorene and 2-aminofluorene
    • Hingerty, B. E., and Broyde, S. (1986) Energy minimized structures of carcinogen-DNA adducts: 2-acetylaminofluorene and 2-aminofluorene, J. Biomol. Struct. Dyn. 4, 365-372.
    • (1986) J. Biomol. Struct. Dyn. , vol.4 , pp. 365-372
    • Hingerty, B.E.1    Broyde, S.2
  • 34
    • 0028033727 scopus 로고
    • Structural characterization of two interchangeable conformations of a 2-aminofluorene-modified DNA oligomer by NMR and energy minimization
    • Eckel, L. M., and Krugh, T. R. (1994) Structural characterization of two interchangeable conformations of a 2-aminofluorene-modified DNA oligomer by NMR and energy minimization, Biochemistry 33, 13611-13624.
    • (1994) Biochemistry , vol.33 , pp. 13611-13624
    • Eckel, L.M.1    Krugh, T.R.2
  • 35
    • 9644276853 scopus 로고    scopus 로고
    • Observing translesion synthesis of an aromatic amine DNA adduct by a high-fidelity DNA polymerase
    • Hsu, G. W., Kiefer, J. R., Burnouf, D., Becherel, O. J., Fuchs, R. P., and Beese, L. S. (2004) Observing translesion synthesis of an aromatic amine DNA adduct by a high-fidelity DNA polymerase, J. Biol. Chem. 279, 50280-50285.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50280-50285
    • Hsu, G.W.1    Kiefer, J.R.2    Burnouf, D.3    Becherel, O.J.4    Fuchs, R.P.5    Beese, L.S.6
  • 37
    • 0037196077 scopus 로고    scopus 로고
    • Two-step error-prone bypass of the (+)- and (-)-trans-anti-BPDE-N(2)-dG adducts by human DNA polymerases eta and kappa
    • Zhang, Y., Wu, X., Guo, D., Rechkoblit, O., Geacintov, N. E., and Wang, Z. (2002) Two-step error-prone bypass of the (+)- and (-)-trans-anti-BPDE-N(2)- dG adducts by human DNA polymerases eta and kappa, Mutat. Res. 510, 23-35.
    • (2002) Mutat. Res. , vol.510 , pp. 23-35
    • Zhang, Y.1    Wu, X.2    Guo, D.3    Rechkoblit, O.4    Geacintov, N.E.5    Wang, Z.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.