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Volumn 51, Issue 16, 2012, Pages 3485-3496

Kinetic basis for the differing response to an oxidative lesion by a replicative and a lesion bypass DNA polymerase from Sulfolobus solfataricus

Author keywords

[No Author keywords available]

Indexed keywords

BASE PAIRS; DNA LESIONS; DNA POLYMERASE; DNA REPLICATIONS; DNA SUBSTRATES; EXONUCLEASE ACTIVITY; GENOMIC MUTATION; HIGH TEMPERATURE; HYPERTHERMOPHILES; HYPERTHERMOPHILIC; LESION BYPASS; LESION SITE; OXIDATIVE DAMAGE; POLYMERASE ACTIVITIES; PRE-STEADY STATE; REPLICATION FORK; SULFOLOBUS SOLFATARICUS; SWITCHING MECHANISM;

EID: 84860189814     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300246r     Document Type: Article
Times cited : (25)

References (58)
  • 1
    • 0031469841 scopus 로고    scopus 로고
    • Analysis of a form of oxidative DNA damage, 8-hydroxy-2′- deoxyguanosine, as a marker of cellular oxidative stress during carcinogenesis
    • Kasai, H. (1997) Analysis of a form of oxidative DNA damage, 8-hydroxy-2′-deoxyguanosine, as a marker of cellular oxidative stress during carcinogenesis Mutat. Res. 387, 147-163
    • (1997) Mutat. Res. , vol.387 , pp. 147-163
    • Kasai, H.1
  • 2
    • 0344154463 scopus 로고    scopus 로고
    • Oxidative damage to DNA: Formation, measurement and biochemical features
    • Cadet, J., Douki, T., Gasparutto, D., and Ravanat, J. L. (2003) Oxidative damage to DNA: Formation, measurement and biochemical features Mutat. Res. 531, 5-23
    • (2003) Mutat. Res. , vol.531 , pp. 5-23
    • Cadet, J.1    Douki, T.2    Gasparutto, D.3    Ravanat, J.L.4
  • 3
    • 0025891866 scopus 로고
    • NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex. 8-Oxo-7H-dG(syn)•dA(anti) alignment at lesion site
    • Kouchakdjian, M., Bodepudi, V., Shibutani, S., Eisenberg, M., Johnson, F., Grollman, A. P., and Patel, D. J. (1991) NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex. 8-Oxo-7H-dG(syn)•dA(anti) alignment at lesion site Biochemistry 30, 1403-1412
    • (1991) Biochemistry , vol.30 , pp. 1403-1412
    • Kouchakdjian, M.1    Bodepudi, V.2    Shibutani, S.3    Eisenberg, M.4    Johnson, F.5    Grollman, A.P.6    Patel, D.J.7
  • 5
    • 33947170923 scopus 로고    scopus 로고
    • Single-turnover kinetic analysis of the mutagenic potential of 8-oxo-7,8-dihydro-2′-deoxyguanosine during gap-filling synthesis catalyzed by human DNA polymerases λ and β
    • Brown, J. A., Duym, W. W., Fowler, J. D., and Suo, Z. (2007) Single-turnover kinetic analysis of the mutagenic potential of 8-oxo-7,8-dihydro-2′-deoxyguanosine during gap-filling synthesis catalyzed by human DNA polymerases λ and β J. Mol. Biol. 367, 1258-1269
    • (2007) J. Mol. Biol. , vol.367 , pp. 1258-1269
    • Brown, J.A.1    Duym, W.W.2    Fowler, J.D.3    Suo, Z.4
  • 7
    • 0030918969 scopus 로고    scopus 로고
    • Analysis of nucleotide insertion and extension at 8-oxo-7,8- dihydroguanine by replicative T7 polymerase exo- and human immunodeficiency virus-1 reverse transcriptase using steady-state and pre-steady-state kinetics
    • Furge, L. L. and Guengerich, F. P. (1997) Analysis of nucleotide insertion and extension at 8-oxo-7,8-dihydroguanine by replicative T7 polymerase exo- and human immunodeficiency virus-1 reverse transcriptase using steady-state and pre-steady-state kinetics Biochemistry 36, 6475-6487
    • (1997) Biochemistry , vol.36 , pp. 6475-6487
    • Furge, L.L.1    Guengerich, F.P.2
  • 8
    • 0032558424 scopus 로고    scopus 로고
    • Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8-dihydroguanosine triphosphate incorporation and extension by replicative and repair DNA polymerases
    • Einolf, H. J., Schnetz-Boutaud, N., and Guengerich, F. P. (1998) Steady-state and pre-steady-state kinetic analysis of 8-oxo-7,8-dihydroguanosine 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
  • 9
    • 4544273926 scopus 로고    scopus 로고
    • Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase
    • Hsu, G. W., Ober, M., Carell, T., and Beese, L. S. (2004) Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase Nature 431, 217-221
    • (2004) Nature , vol.431 , pp. 217-221
    • Hsu, G.W.1    Ober, M.2    Carell, T.3    Beese, L.S.4
  • 10
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani, S., Takeshita, M., and Grollman, A. P. (1991) Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG Nature 349, 431-434
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 11
    • 0029780554 scopus 로고    scopus 로고
    • Steady-state and pre-steady-state kinetic analysis of dNTP insertion opposite 8-oxo-7,8-dihydroguanine by Escherichia coli polymerases i exo- and II exo
    • Lowe, L. G. and Guengerich, F. P. (1996) Steady-state and pre-steady-state kinetic analysis of dNTP insertion opposite 8-oxo-7,8-dihydroguanine by Escherichia coli polymerases I exo- and II exo Biochemistry 35, 9840-9849
    • (1996) Biochemistry , vol.35 , pp. 9840-9849
    • Lowe, L.G.1    Guengerich, F.P.2
  • 12
    • 0037227566 scopus 로고    scopus 로고
    • Structure of DNA polymerase β with the mutagenic DNA lesion 8-oxodeoxyguanine reveals structural insights into its coding potential
    • Krahn, J. M., Beard, W. A., Miller, H., Grollman, A. P., and Wilson, S. H. (2003) Structure of DNA polymerase β with the mutagenic DNA lesion 8-oxodeoxyguanine reveals structural insights into its coding potential Structure 11, 121-127
    • (2003) Structure , vol.11 , pp. 121-127
    • Krahn, J.M.1    Beard, W.A.2    Miller, H.3    Grollman, A.P.4    Wilson, S.H.5
  • 13
    • 14844364365 scopus 로고    scopus 로고
    • Mechanism of efficient and accurate nucleotide incorporation opposite 7,8-dihydro-8-oxoguanine by Saccharomyces cerevisiae DNA polymerase η
    • Carlson, K. D. and Washington, M. T. (2005) Mechanism of efficient and accurate nucleotide incorporation opposite 7,8-dihydro-8-oxoguanine by Saccharomyces cerevisiae DNA polymerase η Mol. Cell. Biol. 25, 2169-2176
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2169-2176
    • Carlson, K.D.1    Washington, M.T.2
  • 14
    • 77949270833 scopus 로고    scopus 로고
    • Mechanism of error-free and semitargeted mutagenic bypass of an aromatic amine lesion by Y-family polymerase Dpo4
    • Rechkoblit, O., Kolbanovskiy, A., Malinina, L., Geacintov, N. E., Broyde, S., and Patel, D. J. (2010) Mechanism of error-free and semitargeted mutagenic bypass of an aromatic amine lesion by Y-family polymerase Dpo4 Nat. Struct. Mol. Biol. 17, 379-388
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 379-388
    • Rechkoblit, O.1    Kolbanovskiy, A.2    Malinina, L.3    Geacintov, N.E.4    Broyde, S.5    Patel, D.J.6
  • 15
    • 33644866040 scopus 로고    scopus 로고
    • Efficient and high fidelity incorporation of dCTP opposite 7,8-dihydro-8-oxodeoxyguanosine by Sulfolobus solfataricus DNA polymerase Dpo4
    • Zang, H., Irimia, A., Choi, J. Y., Angel, K. C., Loukachevitch, L. V., Egli, M., and Guengerich, F. P. (2006) Efficient and high fidelity incorporation of dCTP opposite 7,8-dihydro-8-oxodeoxyguanosine by Sulfolobus solfataricus DNA polymerase Dpo4 J. Biol. Chem. 281, 2358-2372
    • (2006) J. Biol. Chem. , vol.281 , pp. 2358-2372
    • Zang, H.1    Irimia, A.2    Choi, J.Y.3    Angel, K.C.4    Loukachevitch, L.V.5    Egli, M.6    Guengerich, F.P.7
  • 16
    • 35748946285 scopus 로고    scopus 로고
    • Human DNA polymerase λ is a proficient extender of primer ends paired to 7,8-dihydro-8-oxoguanine
    • Picher, A. J. and Blanco, L. (2007) Human DNA polymerase λ is a proficient extender of primer ends paired to 7,8-dihydro-8-oxoguanine DNA Repair 6, 1749-1756
    • (2007) DNA Repair , vol.6 , pp. 1749-1756
    • Picher, A.J.1    Blanco, L.2
  • 17
    • 78549267771 scopus 로고    scopus 로고
    • DNA polymerase structure-based insight on the mutagenic properties of 8-oxoguanine
    • Beard, W. A., Batra, V. K., and Wilson, S. H. (2010) DNA polymerase structure-based insight on the mutagenic properties of 8-oxoguanine Mutat. Res. 703, 18-23
    • (2010) Mutat. Res. , vol.703 , pp. 18-23
    • Beard, W.A.1    Batra, V.K.2    Wilson, S.H.3
  • 18
    • 4644259458 scopus 로고    scopus 로고
    • Structural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase
    • Brieba, L. G., Eichman, B. F., Kokoska, R. J., Doublie, S., Kunkel, T. A., and Ellenberger, T. (2004) Structural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase EMBO J. 23, 3452-3461
    • (2004) EMBO J. , vol.23 , pp. 3452-3461
    • Brieba, L.G.1    Eichman, B.F.2    Kokoska, R.J.3    Doublie, S.4    Kunkel, T.A.5    Ellenberger, T.6
  • 19
    • 27644597370 scopus 로고    scopus 로고
    • A lysine residue in the fingers subdomain of T7 DNA polymerase modulates the miscoding potential of 8-oxo-7,8-dihydroguanosine
    • Brieba, L. G., Kokoska, R. J., Bebenek, K., Kunkel, T. A., and Ellenberger, T. (2005) A lysine residue in the fingers subdomain of T7 DNA polymerase modulates the miscoding potential of 8-oxo-7,8-dihydroguanosine Structure 13, 1653-1659
    • (2005) Structure , vol.13 , pp. 1653-1659
    • Brieba, L.G.1    Kokoska, R.J.2    Bebenek, K.3    Kunkel, T.A.4    Ellenberger, T.5
  • 21
    • 65149093314 scopus 로고    scopus 로고
    • Impact of conformational heterogeneity of OxoG lesions and their pairing partners on bypass fidelity by y family polymerases
    • Rechkoblit, O., Malinina, L., Cheng, Y., Geacintov, N. E., Broyde, S., and Patel, D. J. (2009) Impact of conformational heterogeneity of OxoG lesions and their pairing partners on bypass fidelity by Y family polymerases Structure 17, 725-736
    • (2009) Structure , vol.17 , pp. 725-736
    • Rechkoblit, O.1    Malinina, L.2    Cheng, Y.3    Geacintov, N.E.4    Broyde, S.5    Patel, D.J.6
  • 22
    • 34547136494 scopus 로고    scopus 로고
    • Hydrogen bonding of 7,8-dihydro-8-oxodeoxyguanosine with a charged residue in the little finger domain determines miscoding events in Sulfolobus solfataricus DNA polymerase Dpo4
    • Eoff, R. L., Irimia, A., Angel, K. C., Egli, M., and Guengerich, F. P. (2007) Hydrogen bonding of 7,8-dihydro-8-oxodeoxyguanosine with a charged residue in the little finger domain determines miscoding events in Sulfolobus solfataricus DNA polymerase Dpo4 J. Biol. Chem. 282, 19831-19843
    • (2007) J. Biol. Chem. , vol.282 , pp. 19831-19843
    • Eoff, R.L.1    Irimia, A.2    Angel, K.C.3    Egli, M.4    Guengerich, F.P.5
  • 23
    • 34249870372 scopus 로고    scopus 로고
    • 8-Oxo-guanine bypass by human DNA polymerases in the presence of auxiliary proteins
    • Maga, G., Villani, G., Crespan, E., Wimmer, U., Ferrari, E., Bertocci, B., and Hubscher, U. (2007) 8-Oxo-guanine bypass by human DNA polymerases in the presence of auxiliary proteins Nature 447, 606-608
    • (2007) Nature , vol.447 , pp. 606-608
    • Maga, G.1    Villani, G.2    Crespan, E.3    Wimmer, U.4    Ferrari, E.5    Bertocci, B.6    Hubscher, U.7
  • 25
    • 0037085734 scopus 로고    scopus 로고
    • Heat-induced formation of reactive oxygen species and 8-oxoguanine, a biomarker of damage to DNA
    • Bruskov, V. I., Malakhova, L. V., Masalimov, Z. K., and Chernikov, A. V. (2002) Heat-induced formation of reactive oxygen species and 8-oxoguanine, a biomarker of damage to DNA Nucleic Acids Res. 30, 1354-1363
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1354-1363
    • Bruskov, V.I.1    Malakhova, L.V.2    Masalimov, Z.K.3    Chernikov, A.V.4
  • 27
    • 80052406753 scopus 로고    scopus 로고
    • Roles of the four DNA polymerases of the crenarchaeon Sulfolobus solfataricus and accessory proteins in DNA replication
    • Choi, J. Y., Eoff, R. L., Pence, M. G., Wang, J., Martin, M. V., Kim, E. J., Folkmann, L. M., and Guengerich, F. P. (2011) Roles of the four DNA polymerases of the crenarchaeon Sulfolobus solfataricus and accessory proteins in DNA replication J. Biol. Chem. 286, 31180-31193
    • (2011) J. Biol. Chem. , vol.286 , pp. 31180-31193
    • Choi, J.Y.1    Eoff, R.L.2    Pence, M.G.3    Wang, J.4    Martin, M.V.5    Kim, E.J.6    Folkmann, L.M.7    Guengerich, F.P.8
  • 28
    • 34247181139 scopus 로고    scopus 로고
    • Mechanism of abasic lesion bypass catalyzed by a Y-family DNA polymerase
    • Fiala, K. A., Hypes, C. D., and Suo, Z. (2007) Mechanism of abasic lesion bypass catalyzed by a Y-family DNA polymerase J. Biol. Chem. 282, 8188-8198
    • (2007) J. Biol. Chem. , vol.282 , pp. 8188-8198
    • Fiala, K.A.1    Hypes, C.D.2    Suo, Z.3
  • 29
    • 47249163382 scopus 로고    scopus 로고
    • Mechanism of double-base lesion bypass catalyzed by a Y-family DNA polymerase
    • Brown, J. A., Newmister, S. A., Fiala, K. A., and Suo, Z. (2008) Mechanism of double-base lesion bypass catalyzed by a Y-family DNA polymerase Nucleic Acids Res. 36, 3867-3878
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3867-3878
    • Brown, J.A.1    Newmister, S.A.2    Fiala, K.A.3    Suo, Z.4
  • 30
    • 77953618270 scopus 로고    scopus 로고
    • Structural insight into dynamic bypass of the major cisplatin-DNA adduct by Y-family polymerase Dpo4
    • Wong, J. H., Brown, J. A., Suo, Z., Blum, P., Nohmi, T., and Ling, H. (2010) Structural insight into dynamic bypass of the major cisplatin-DNA adduct by Y-family polymerase Dpo4 EMBO J. 29, 2059-2069
    • (2010) EMBO J. , vol.29 , pp. 2059-2069
    • Wong, J.H.1    Brown, J.A.2    Suo, Z.3    Blum, P.4    Nohmi, T.5    Ling, H.6
  • 31
    • 65249138294 scopus 로고    scopus 로고
    • Mechanistic studies of the bypass of a bulky single-base lesion catalyzed by a Y-family DNA polymerase
    • Sherrer, S. M., Brown, J. A., Pack, L. R., Jasti, V. P., Fowler, J. D., Basu, A. K., and Suo, Z. (2009) Mechanistic studies of the bypass of a bulky single-base lesion catalyzed by a Y-family DNA polymerase J. Biol. Chem. 284, 6379-6388
    • (2009) J. Biol. Chem. , vol.284 , pp. 6379-6388
    • Sherrer, S.M.1    Brown, J.A.2    Pack, L.R.3    Jasti, V.P.4    Fowler, J.D.5    Basu, A.K.6    Suo, Z.7
  • 32
    • 1242307762 scopus 로고    scopus 로고
    • Mechanism of DNA polymerization catalyzed by Sulfolobus solfataricus P2 DNA polymerase IV
    • Fiala, K. A. and Suo, Z. (2004) Mechanism of DNA polymerization catalyzed by Sulfolobus solfataricus P2 DNA polymerase IV Biochemistry 43, 2116-2125
    • (2004) Biochemistry , vol.43 , pp. 2116-2125
    • Fiala, K.A.1    Suo, Z.2
  • 33
    • 1242285442 scopus 로고    scopus 로고
    • Pre-steady-state kinetic studies of the fidelity of Sulfolobus solfataricus P2 DNA polymerase IV
    • Fiala, K. A. and Suo, Z. (2004) Pre-steady-state kinetic studies of the fidelity of Sulfolobus solfataricus P2 DNA polymerase IV Biochemistry 43, 2106-2115
    • (2004) Biochemistry , vol.43 , pp. 2106-2115
    • Fiala, K.A.1    Suo, Z.2
  • 34
    • 68249105256 scopus 로고    scopus 로고
    • Elucidating the kinetic mechanism of DNA polymerization catalyzed by Sulfolobus solfataricus P2 DNA polymerase B1
    • Brown, J. A. and Suo, Z. (2009) Elucidating the kinetic mechanism of DNA polymerization catalyzed by Sulfolobus solfataricus P2 DNA polymerase B1 Biochemistry 48, 7502-7511
    • (2009) Biochemistry , vol.48 , pp. 7502-7511
    • Brown, J.A.1    Suo, Z.2
  • 35
    • 68249097023 scopus 로고    scopus 로고
    • Polymerization fidelity of a replicative DNA polymerase from the hyperthermophilic archaeon Sulfolobus solfataricus P2
    • Zhang, L., Brown, J. A., Newmister, S. A., and Suo, Z. (2009) Polymerization fidelity of a replicative DNA polymerase from the hyperthermophilic archaeon Sulfolobus solfataricus P2 Biochemistry 48, 7492-7501
    • (2009) Biochemistry , vol.48 , pp. 7492-7501
    • Zhang, L.1    Brown, J.A.2    Newmister, S.A.3    Suo, Z.4
  • 36
    • 41849102779 scopus 로고    scopus 로고
    • Mechanistic consequences of temperature on DNA polymerization catalyzed by a Y-family DNA polymerase
    • Fiala, K. A., Sherrer, S. M., Brown, J. A., and Suo, Z. (2008) Mechanistic consequences of temperature on DNA polymerization catalyzed by a Y-family DNA polymerase Nucleic Acids Res. 36, 1990-2001
    • (2008) Nucleic Acids Res. , vol.36 , pp. 1990-2001
    • Fiala, K.A.1    Sherrer, S.M.2    Brown, J.A.3    Suo, Z.4
  • 37
    • 0242317687 scopus 로고    scopus 로고
    • Processing of DNA lesions by archaeal DNA polymerases from Sulfolobus solfataricus
    • Gruz, P., Shimizu, M., Pisani, F. M., De Felice, M., Kanke, Y., and Nohmi, T. (2003) Processing of DNA lesions by archaeal DNA polymerases from Sulfolobus solfataricus Nucleic Acids Res. 31, 4024-4030
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4024-4030
    • Gruz, P.1    Shimizu, M.2    Pisani, F.M.3    De Felice, M.4    Kanke, Y.5    Nohmi, T.6
  • 38
    • 69249088166 scopus 로고    scopus 로고
    • Interaction of human DNA polymerase α and DNA polymerase i from Bacillus stearothermophilus with hypoxanthine and 8-oxoguanine nucleotides
    • Patro, J. N., Urban, M., and Kuchta, R. D. (2009) Interaction of human DNA polymerase α and DNA polymerase I from Bacillus stearothermophilus with hypoxanthine and 8-oxoguanine nucleotides Biochemistry 48, 8271-8278
    • (2009) Biochemistry , vol.48 , pp. 8271-8278
    • Patro, J.N.1    Urban, M.2    Kuchta, R.D.3
  • 39
    • 77949532175 scopus 로고    scopus 로고
    • Kinetics of mismatch formation opposite lesions by the replicative DNA polymerase from bacteriophage RB69
    • Hogg, M., Rudnicki, J., Midkiff, J., Reha-Krantz, L., Doublie, S., and Wallace, S. S. (2010) Kinetics of mismatch formation opposite lesions by the replicative DNA polymerase from bacteriophage RB69 Biochemistry 49, 2317-2325
    • (2010) Biochemistry , vol.49 , pp. 2317-2325
    • Hogg, M.1    Rudnicki, J.2    Midkiff, J.3    Reha-Krantz, L.4    Doublie, S.5    Wallace, S.S.6
  • 40
    • 34548570175 scopus 로고    scopus 로고
    • A highly conserved tyrosine residue of family B DNA polymerases contributes to dictate translesion synthesis past 8-oxo-7,8-dihydro-2′- deoxyguanosine
    • de Vega, M. and Salas, M. (2007) A highly conserved tyrosine residue of family B DNA polymerases contributes to dictate translesion synthesis past 8-oxo-7,8-dihydro-2′-deoxyguanosine Nucleic Acids Res. 35, 5096-5107
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5096-5107
    • De Vega, M.1    Salas, M.2
  • 41
    • 0032703301 scopus 로고    scopus 로고
    • Replication of damaged DNA: Molecular defect in xeroderma pigmentosum variant cells
    • Cordonnier, A. M. and Fuchs, R. P. (1999) Replication of damaged DNA: Molecular defect in xeroderma pigmentosum variant cells Mutat. Res. 435, 111-119
    • (1999) Mutat. Res. , vol.435 , pp. 111-119
    • Cordonnier, A.M.1    Fuchs, R.P.2
  • 42
    • 33845638804 scopus 로고    scopus 로고
    • Mechanism of Template-independent Nucleotide Incorporation Catalyzed by a Template-dependent DNA Polymerase
    • Fiala, K. A., Brown, J. A., Ling, H., Kshetry, A. K., Zhang, J., Taylor, J. S., Yang, W., and Suo, Z. (2007) Mechanism of Template-independent Nucleotide Incorporation Catalyzed by a Template-dependent DNA Polymerase J. Mol. Biol. 365, 590-602
    • (2007) J. Mol. Biol. , vol.365 , pp. 590-602
    • Fiala, K.A.1    Brown, J.A.2    Ling, H.3    Kshetry, A.K.4    Zhang, J.5    Taylor, J.S.6    Yang, W.7    Suo, Z.8
  • 43
    • 0034940811 scopus 로고    scopus 로고
    • Genetic fidelity under harsh conditions: Analysis of spontaneous mutation in the thermoacidophilic archaeon Sulfolobus acidocaldarius
    • Grogan, D. W., Carver, G. T., and Drake, J. W. (2001) Genetic fidelity under harsh conditions: Analysis of spontaneous mutation in the thermoacidophilic archaeon Sulfolobus acidocaldarius Proc. Natl. Acad. Sci. U.S.A. 98, 7928-7933
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 7928-7933
    • Grogan, D.W.1    Carver, G.T.2    Drake, J.W.3
  • 44
    • 27144542782 scopus 로고    scopus 로고
    • Fidelity of Dpo4: Effect of metal ions, nucleotide selection and pyrophosphorolysis
    • Vaisman, A., Ling, H., Woodgate, R., and Yang, W. (2005) Fidelity of Dpo4: Effect of metal ions, nucleotide selection and pyrophosphorolysis EMBO J. 24, 2957-2967
    • (2005) EMBO J. , vol.24 , pp. 2957-2967
    • Vaisman, A.1    Ling, H.2    Woodgate, R.3    Yang, W.4
  • 45
    • 0035830851 scopus 로고    scopus 로고
    • Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase δ. Steady-state and pre-steady-state kinetic analysis
    • Einolf, H. J. and Guengerich, F. P. (2001) Fidelity of nucleotide insertion at 8-oxo-7,8-dihydroguanine by mammalian DNA polymerase δ. Steady-state and pre-steady-state kinetic analysis J. Biol. Chem. 276, 3764-3771
    • (2001) J. Biol. Chem. , vol.276 , pp. 3764-3771
    • Einolf, H.J.1    Guengerich, F.P.2
  • 46
    • 0031034183 scopus 로고    scopus 로고
    • Mechanism of bypass synthesis through an abasic site analog by DNA polymerase i
    • Paz-Elizur, T., Takeshita, M., and Livneh, Z. (1997) Mechanism of bypass synthesis through an abasic site analog by DNA polymerase I Biochemistry 36, 1766-1773
    • (1997) Biochemistry , vol.36 , pp. 1766-1773
    • Paz-Elizur, T.1    Takeshita, M.2    Livneh, Z.3
  • 47
    • 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., and Livneh, Z. (1996) Mechanism of translesion DNA synthesis by DNA polymerase II. Comparison to DNA polymerases I and III core J. Biol. Chem. 271, 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
  • 48
    • 66349132334 scopus 로고    scopus 로고
    • Proofreading exonuclease activity of human DNA polymerase δ and its effects on lesion-bypass DNA synthesis
    • Fazlieva, R., Spittle, C. S., Morrissey, D., Hayashi, H., Yan, H., and Matsumoto, Y. (2009) Proofreading exonuclease activity of human DNA polymerase δ and its effects on lesion-bypass DNA synthesis Nucleic Acids Res. 37, 2854-2866
    • (2009) Nucleic Acids Res. , vol.37 , pp. 2854-2866
    • Fazlieva, R.1    Spittle, C.S.2    Morrissey, D.3    Hayashi, H.4    Yan, H.5    Matsumoto, Y.6
  • 49
    • 0035968340 scopus 로고    scopus 로고
    • The 3′ → 5′ exonuclease of T4 DNA polymerase removes premutagenic alkyl mispairs and contributes to futile cycling at O6-methylguanine lesions
    • Khare, V. and Eckert, K. A. (2001) The 3′ → 5′ exonuclease of T4 DNA polymerase removes premutagenic alkyl mispairs and contributes to futile cycling at O6-methylguanine lesions J. Biol. Chem. 276, 24286-24292
    • (2001) J. Biol. Chem. , vol.276 , pp. 24286-24292
    • Khare, V.1    Eckert, K.A.2
  • 50
    • 2342484512 scopus 로고    scopus 로고
    • Lesion (in)tolerance reveals insights into DNA replication fidelity
    • Freisinger, E., Grollman, A. P., Miller, H., and Kisker, C. (2004) Lesion (in)tolerance reveals insights into DNA replication fidelity EMBO J. 23, 1494-1505
    • (2004) EMBO J. , vol.23 , pp. 1494-1505
    • Freisinger, E.1    Grollman, A.P.2    Miller, H.3    Kisker, C.4
  • 51
    • 77952407219 scopus 로고    scopus 로고
    • Substitution of Ala for Tyr567 in RB69 DNA polymerase allows dAMP to be inserted opposite 7,8-dihydro-8-oxoguanine
    • Beckman, J., Wang, M., Blaha, G., Wang, J., and Konigsberg, W. H. (2010) Substitution of Ala for Tyr567 in RB69 DNA polymerase allows dAMP to be inserted opposite 7,8-dihydro-8-oxoguanine Biochemistry 49, 4116-4125
    • (2010) Biochemistry , vol.49 , pp. 4116-4125
    • Beckman, J.1    Wang, M.2    Blaha, G.3    Wang, J.4    Konigsberg, W.H.5
  • 52
    • 35548972018 scopus 로고    scopus 로고
    • The DNA polymerase γ Y955C disease variant associated with PEO and parkinsonism mediates the incorporation and translesion synthesis opposite 7,8-dihydro-8-oxo-2′-deoxyguanosine
    • Graziewicz, M. A., Bienstock, R. J., and Copeland, W. C. (2007) The DNA polymerase γ Y955C disease variant associated with PEO and parkinsonism mediates the incorporation and translesion synthesis opposite 7,8-dihydro-8-oxo-2′-deoxyguanosine Hum. Mol. Genet. 16, 2729-2739
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2729-2739
    • Graziewicz, M.A.1    Bienstock, R.J.2    Copeland, W.C.3
  • 53
    • 0025898648 scopus 로고
    • A general structure for DNA-dependent DNA polymerases
    • Blanco, L., Bernad, A., Blasco, M. A., and Salas, M. (1991) A general structure for DNA-dependent DNA polymerases Gene 100, 27-38
    • (1991) Gene , vol.100 , pp. 27-38
    • Blanco, L.1    Bernad, A.2    Blasco, M.A.3    Salas, M.4
  • 54
    • 7944222972 scopus 로고    scopus 로고
    • Insights into DNA replication: The crystal structure of DNA polymerase B1 from the archaeon Sulfolobus solfataricus
    • Savino, C., Federici, L., Johnson, K. A., Vallone, B., Nastopoulos, V., Rossi, M., Pisani, F. M., and Tsernoglou, D. (2004) Insights into DNA replication: the crystal structure of DNA polymerase B1 from the archaeon Sulfolobus solfataricus Structure 12, 2001-2008
    • (2004) Structure , vol.12 , pp. 2001-2008
    • Savino, C.1    Federici, L.2    Johnson, K.A.3    Vallone, B.4    Nastopoulos, V.5    Rossi, M.6    Pisani, F.M.7    Tsernoglou, D.8
  • 55
    • 84859765696 scopus 로고    scopus 로고
    • A DNA Lesion Alters the Global Conformational Dynamics of a Y-Family DNA Polymerase during Catalysis
    • Maxwell, B. A., Xu, C., and Suo, Z. (2012) A DNA Lesion Alters the Global Conformational Dynamics of a Y-Family DNA Polymerase during Catalysis J. Biol. Chem. 287, 13040-13047
    • (2012) J. Biol. Chem. , vol.287 , pp. 13040-13047
    • Maxwell, B.A.1    Xu, C.2    Suo, Z.3
  • 56
    • 0037115955 scopus 로고    scopus 로고
    • How DNA lesions are turned into mutations within cells?
    • Pages, V. and Fuchs, R. P. (2002) How DNA lesions are turned into mutations within cells? Oncogene 21, 8957-8966
    • (2002) Oncogene , vol.21 , pp. 8957-8966
    • Pages, V.1    Fuchs, R.P.2
  • 57
    • 0037251411 scopus 로고    scopus 로고
    • A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus
    • Dionne, I., Nookala, R. K., Jackson, S. P., Doherty, A. J., and Bell, S. D. (2003) A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus solfataricus Mol. Cell 11, 275-282
    • (2003) Mol. Cell , vol.11 , pp. 275-282
    • Dionne, I.1    Nookala, R.K.2    Jackson, S.P.3    Doherty, A.J.4    Bell, S.D.5
  • 58
    • 58449104506 scopus 로고    scopus 로고
    • Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA
    • Xing, G., Kirouac, K., Shin, Y. J., Bell, S. D., and Ling, H. (2009) Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA Mol. Microbiol. 71, 678-691
    • (2009) Mol. Microbiol. , vol.71 , pp. 678-691
    • Xing, G.1    Kirouac, K.2    Shin, Y.J.3    Bell, S.D.4    Ling, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.