메뉴 건너뛰기




Volumn 52, Issue 25, 2013, Pages 4422-4432

Structural changes in the hydrophobic hinge region adversely affect the activity and fidelity of the I260Q mutator DNA polymerase β

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; DOUBLE STRANDED DNA; MODELING STUDIES; ORDERED WATER; SIDE-CHAINS; STRUCTURAL CHANGE; STRUCTURAL VARIATIONS; TERNARY COMPLEX;

EID: 84879513246     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301368f     Document Type: Article
Times cited : (13)

References (54)
  • 1
    • 58549094699 scopus 로고    scopus 로고
    • Distribution and roles of X-family DNA polymerases in eukaryotes
    • Uchiyama, Y., Takeuchi, R., Kodera, H., and Sakaguchi, K. (2009) Distribution and roles of X-family DNA polymerases in eukaryotes Biochimie 91, 165-170
    • (2009) Biochimie , vol.91 , pp. 165-170
    • Uchiyama, Y.1    Takeuchi, R.2    Kodera, H.3    Sakaguchi, K.4
  • 2
    • 58949084649 scopus 로고    scopus 로고
    • Base excision repair of oxidative DNA damage and association with cancer and aging
    • Maynard, S., Schurman, S. H., Harboe, C., Souza-Pinto, N. C., and Borh, V. A. (2009) Base excision repair of oxidative DNA damage and association with cancer and aging Carcinogenesis 30, 2-10
    • (2009) Carcinogenesis , vol.30 , pp. 2-10
    • Maynard, S.1    Schurman, S.H.2    Harboe, C.3    Souza-Pinto, N.C.4    Borh, V.A.5
  • 3
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Matsumoto, Y. and Kim, K. (1995) Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair Science 269, 699-702
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 4
    • 0032100860 scopus 로고    scopus 로고
    • Mammalian base excision repair and DNA polymerase β
    • Wilson, S. (1998) Mammalian base excision repair and DNA polymerase β Mutat. Res. 407, 203-215
    • (1998) Mutat. Res. , vol.407 , pp. 203-215
    • Wilson, S.1
  • 5
    • 0027179827 scopus 로고
    • Short Gap-filling Synthesis by DNA Polymerase β Is Processive
    • Singhal, R. K. and Wilson, S. H. (1993) Short Gap-filling Synthesis by DNA Polymerase β Is Processive J. Biol. Chem. 268, 15906-15911
    • (1993) J. Biol. Chem. , vol.268 , pp. 15906-15911
    • Singhal, R.K.1    Wilson, S.H.2
  • 6
    • 0028338562 scopus 로고
    • Studies of Gapped DNA Substrate Binding by Mammalian DNA Polymerase β
    • Prasad, R., Beard, W. A., and Wilson, S. H. (1994) Studies of Gapped DNA Substrate Binding by Mammalian DNA Polymerase β J. Biol. Chem. 269, 18096-18101
    • (1994) J. Biol. Chem. , vol.269 , pp. 18096-18101
    • Prasad, R.1    Beard, W.A.2    Wilson, S.H.3
  • 7
    • 0032539979 scopus 로고    scopus 로고
    • Different DNA polymerases are involved in short- and long-patch base excision repair in mammalian cells
    • Fortini, P., Pascucci, B., Parlanti, E., Sobol, R. W., Wilson, S. H., and Dogliotti, E. (1998) Different DNA polymerases are involved in short- and long-patch base excision repair in mammalian cells Biochemistry 37, 3575-3580
    • (1998) Biochemistry , vol.37 , pp. 3575-3580
    • Fortini, P.1    Pascucci, B.2    Parlanti, E.3    Sobol, R.W.4    Wilson, S.H.5    Dogliotti, E.6
  • 8
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1)
    • Klungland, A. and Lindhal, T. (1997) Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1) EMBO J. 16, 3341-3348
    • (1997) EMBO J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindhal, T.2
  • 9
    • 0035936560 scopus 로고    scopus 로고
    • DNA synthesis and dRPase activity of polymerase β are both essential for single-nucleotide patch base excision repair in mammalian cell extracts
    • Podlutsky, A. J., Dianova, I. I., Wilson, S. H., Bohr, V. A., and Dianov, G. L. (2001) DNA synthesis and dRPase activity of polymerase β; are both essential for single-nucleotide patch base excision repair in mammalian cell extracts Biochemistry 40, 809-813
    • (2001) Biochemistry , vol.40 , pp. 809-813
    • Podlutsky, A.J.1    Dianova, I.I.2    Wilson, S.H.3    Bohr, V.A.4    Dianov, G.L.5
  • 10
    • 13944279514 scopus 로고    scopus 로고
    • Is There a Link between DNA Polymerase β and Cancer?
    • Starcevic, D., Dalal, S., and Sweasy, J. B. (2004) Is There a Link Between DNA Polymerase β and Cancer? Cell Cycle 3, 998-1001
    • (2004) Cell Cycle , vol.3 , pp. 998-1001
    • Starcevic, D.1    Dalal, S.2    Sweasy, J.B.3
  • 11
    • 0028881713 scopus 로고
    • Polymerase Structures and Functions: Variations on a Theme?
    • Joyce, C. M. and Steitz, T. A. (1995) Polymerase Structures and Functions: Variations on a Theme? J. Bacteriol. 177, 6321-6329
    • (1995) J. Bacteriol. , vol.177 , pp. 6321-6329
    • Joyce, C.M.1    Steitz, T.A.2
  • 12
    • 0039792280 scopus 로고    scopus 로고
    • Getting a grip: Polymerases and their substrate complexes
    • Jaeger, J. and Pata, J. D. (1999) Getting a grip: Polymerases and their substrate complexes Curr. Opin. Struct. Biol. 9, 21-28
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 21-28
    • Jaeger, J.1    Pata, J.D.2
  • 13
    • 0028606031 scopus 로고
    • A Unified Polymerase Mechanism for Nonhomologous DNA and RNA Polymerases
    • Steitz, T. A., Smerdon, S. J., Jaeger, J., and Joyce, C. M. (1994) A Unified Polymerase Mechanism for Nonhomologous DNA and RNA Polymerases Science 266, 2022-2025
    • (1994) Science , vol.266 , pp. 2022-2025
    • Steitz, T.A.1    Smerdon, S.J.2    Jaeger, J.3    Joyce, C.M.4
  • 14
    • 0029836483 scopus 로고    scopus 로고
    • Characterization of the Metal Ion Binding Helix-Hairpin-Helix Motifs in Human DNA Polymerase β by X-ray Structural Analysis
    • Pelletier, H. and Sawaya, M. R. (1996) Characterization of the Metal Ion Binding Helix-Hairpin-Helix Motifs in Human DNA Polymerase β by X-ray Structural Analysis Biochemistry 35, 12778-12787
    • (1996) Biochemistry , vol.35 , pp. 12778-12787
    • Pelletier, H.1    Sawaya, M.R.2
  • 15
    • 0030891201 scopus 로고    scopus 로고
    • DNA polymerase β in abasic site repair: A structurally conserved helix-hairpin-helix motif in lesion detection by base excision repair enzymes
    • Mullen, G. P. and Wilson, S. H. (1997) DNA polymerase β in abasic site repair: A structurally conserved helix-hairpin-helix motif in lesion detection by base excision repair enzymes Biochemistry 36, 4713-4717
    • (1997) Biochemistry , vol.36 , pp. 4713-4717
    • Mullen, G.P.1    Wilson, S.H.2
  • 16
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: Evidence for an induced fit mechanism
    • Sawaya, M. R., Prasad, R., Wilson, S. H., Kraut, J., and Pelletier, H. (1997) Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: Evidence for an induced fit mechanism Biochemistry 36, 11205-11215
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 17
    • 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. and Steitz, T. A. (1991) Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism EMBO J. 10, 25-33
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 18
    • 0030010766 scopus 로고    scopus 로고
    • DNA polymerase β: Pre-steady-state kinetic analysis and roles of arginine-283 in catalysis and fidelity
    • Werneburg, B. G., Ahn, J., Zhong, X., Hondal, R. J., Kraynov, V. S., and Tsai, M. D. (1996) DNA polymerase β: Pre-steady-state kinetic analysis and roles of arginine-283 in catalysis and fidelity Biochemistry 35, 7041-7050
    • (1996) Biochemistry , vol.35 , pp. 7041-7050
    • Werneburg, B.G.1    Ahn, J.2    Zhong, X.3    Hondal, R.J.4    Kraynov, V.S.5    Tsai, M.D.6
  • 19
    • 0034719142 scopus 로고    scopus 로고
    • DNA Polymerase β: Contributions of Template-Positioning and dNTP Triphosphate-Binding Residues to Catalysis and Fidelity
    • Kraynov, V. S., Showalter, A. K., Liu, J., Zhong, X., and Tsai, M. D. (2000) DNA Polymerase β: Contributions of Template-Positioning and dNTP Triphosphate-Binding Residues to Catalysis and Fidelity Biochemistry 39, 16008-16015
    • (2000) Biochemistry , vol.39 , pp. 16008-16015
    • Kraynov, V.S.1    Showalter, A.K.2    Liu, J.3    Zhong, X.4    Tsai, M.D.5
  • 20
    • 0032562169 scopus 로고    scopus 로고
    • The Mutator Form of Polymerase β with Amino Acid Substitution at Tyrosine 265 in the Hinge Region Displays an Increase in both Base Substitution and Frame Shift Errors
    • Opresko, P. L., Sweasy, J. B., and Eckert, K. A. (1998) The Mutator Form of Polymerase β with Amino Acid Substitution at Tyrosine 265 in the Hinge Region Displays an Increase in both Base Substitution and Frame Shift Errors Biochemistry 37, 2111-2119
    • (1998) Biochemistry , vol.37 , pp. 2111-2119
    • Opresko, P.L.1    Sweasy, J.B.2    Eckert, K.A.3
  • 21
    • 0033551096 scopus 로고    scopus 로고
    • Involvement of Phenylalanine 272 of DNA Polymerase β in Discriminating between Correct and Incorrect Deoxynucleoside Triphosphates
    • Li, S.-X., Vaccaro, J. A., and Sweasy, J. B. (1999) Involvement of Phenylalanine 272 of DNA Polymerase β in Discriminating between Correct and Incorrect Deoxynucleoside Triphosphates Biochemistry 38, 4800-4808
    • (1999) Biochemistry , vol.38 , pp. 4800-4808
    • Li, S.-X.1    Vaccaro, J.A.2    Sweasy, J.B.3
  • 22
    • 0035949644 scopus 로고    scopus 로고
    • A DNA polymerase β mutator mutant with reduced nucleotide discrimination and increase protein stability
    • Shah, A. M., Conn, D. A., Li, S. X., Capaldi, A., Jager, J., and Sweasy, J. B. (2001) A DNA polymerase β mutator mutant with reduced nucleotide discrimination and increase protein stability Biochemistry 40, 11372-11381
    • (2001) Biochemistry , vol.40 , pp. 11372-11381
    • Shah, A.M.1    Conn, D.A.2    Li, S.X.3    Capaldi, A.4    Jager, J.5    Sweasy, J.B.6
  • 23
    • 28544444617 scopus 로고    scopus 로고
    • Prostate-Cancer-Associated I260M Variant of DNA Polymerase β Is a Sequence-Specific Mutator
    • Dalal, S., Hile, S., Eckert, K. A., Sun, K.-w., Starcevic, D., and Sweasy, J. B. (2005) Prostate-Cancer-Associated I260M Variant of DNA Polymerase β Is a Sequence-Specific Mutator Biochemistry 44, 15664-15673
    • (2005) Biochemistry , vol.44 , pp. 15664-15673
    • Dalal, S.1    Hile, S.2    Eckert, K.A.3    Sun, K.-W.4    Starcevic, D.5    Sweasy, J.B.6
  • 24
    • 23344450425 scopus 로고    scopus 로고
    • The Hydrophobic Hinge Region of Rat DNA Polymerase β Is Critical for Substrate Binding Pocket Geometry
    • Starcevic, D., Dalal, S., Jaeger, J., and Sweasy, J. B. (2005) The Hydrophobic Hinge Region of Rat DNA Polymerase β Is Critical for Substrate Binding Pocket Geometry J. Biol. Chem. 280, 28388-28393
    • (2005) J. Biol. Chem. , vol.280 , pp. 28388-28393
    • Starcevic, D.1    Dalal, S.2    Jaeger, J.3    Sweasy, J.B.4
  • 25
    • 56249121875 scopus 로고    scopus 로고
    • The I260Q Variant of DNA Polymerase β Extends Mispaired Primer Termini Due to Its Decreased Affinity for Deoxynucleotide Triphosphate Substrates
    • Dalal, S., Starcevic, D., Jaeger, J., and Sweasy, J. B. (2008) The I260Q Variant of DNA Polymerase β Extends Mispaired Primer Termini Due to Its Decreased Affinity for Deoxynucleotide Triphosphate Substrates Biochemistry 47, 12118-12125
    • (2008) Biochemistry , vol.47 , pp. 12118-12125
    • Dalal, S.1    Starcevic, D.2    Jaeger, J.3    Sweasy, J.B.4
  • 26
    • 51849149950 scopus 로고    scopus 로고
    • Mismatched and Matched dNTP Incorporation by DNA Polymerase β Proceed via Analogous Kinetic Pathways
    • Roettger, M. P., Bakhtina, M., and Tsai, M.-D. (2008) Mismatched and Matched dNTP Incorporation by DNA Polymerase β Proceed via Analogous Kinetic Pathways Biochemistry 47, 9718-9727
    • (2008) Biochemistry , vol.47 , pp. 9718-9727
    • Roettger, M.P.1    Bakhtina, M.2    Tsai, M.-D.3
  • 27
    • 0347052870 scopus 로고    scopus 로고
    • The D246V mutant of DNA polymerase β misincorporates nucleotides: Evidence for a role for the flexible loop in DNA positioning within the active site
    • Dalal, S., Kosa, J. L., and Sweasy, J. B. (2004) The D246V mutant of DNA polymerase β misincorporates nucleotides: Evidence for a role for the flexible loop in DNA positioning within the active site J. Biol. Chem. 279, 577-584
    • (2004) J. Biol. Chem. , vol.279 , pp. 577-584
    • Dalal, S.1    Kosa, J.L.2    Sweasy, J.B.3
  • 29
    • 0032748078 scopus 로고    scopus 로고
    • Functional mutation of DNA polymerase β found in human gastric cancer: Inability of the base excision repair in vitro
    • Iwanaga, A., Ouchida, M., Miyazaki, K., Hori, K., and Mukai, T. (1999) Functional mutation of DNA polymerase β found in human gastric cancer: Inability of the base excision repair in vitro Mutat. Res. 435, 121-128
    • (1999) Mutat. Res. , vol.435 , pp. 121-128
    • Iwanaga, A.1    Ouchida, M.2    Miyazaki, K.3    Hori, K.4    Mukai, T.5
  • 30
    • 34547195827 scopus 로고    scopus 로고
    • The E295K DNA Polymerase β Gastric Cancer-Associated Variant Interferes with Base Excision Repair and Induces Cellular Transformation
    • Lang, T., Dalal, S., Chikova, A., DiMaio, D., and Sweasy, J. B. (2007) The E295K DNA Polymerase β Gastric Cancer-Associated Variant Interferes with Base Excision Repair and Induces Cellular Transformation Mol. Cell. Biol. 27, 5587-5596
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5587-5596
    • Lang, T.1    Dalal, S.2    Chikova, A.3    Dimaio, D.4    Sweasy, J.B.5
  • 31
    • 79952743209 scopus 로고    scopus 로고
    • Systematic Biochemical Analysis of Somatic Missense Mutations in DNA Polymerase β Found in Prostate Cancer Reveal Alteration of Enzymatic Function
    • An, C. L., Chen, D., and Makridakis, N. M. (2011) Systematic Biochemical Analysis of Somatic Missense Mutations in DNA Polymerase β Found in Prostate Cancer Reveal Alteration of Enzymatic Function Hum. Mutat. 32, 415-423
    • (2011) Hum. Mutat. , vol.32 , pp. 415-423
    • An, C.L.1    Chen, D.2    Makridakis, N.M.3
  • 32
    • 44349090420 scopus 로고    scopus 로고
    • Mismatched dNTP incorporation by DNA polymerase β does not proceed via globally different conformational pathways
    • Tang, K.-H., Nieburh, M., Tung, C.-S., Chan, H.-c., Chou, C.-C., and Tsai, M. D. (2008) Mismatched dNTP incorporation by DNA polymerase β does not proceed via globally different conformational pathways Nucleic Acids Res. 36, 2948-2957
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2948-2957
    • Tang, K.-H.1    Nieburh, M.2    Tung, C.-S.3    Chan, H.-C.4    Chou, C.-C.5    Tsai, M.D.6
  • 33
    • 14844346283 scopus 로고    scopus 로고
    • Hinge Residue Ile260 of DNA Polymerase β is Important for Enzyme Activity and Fidelity
    • Starcevic, D., Dalal, S., and Sweasy, J. B. (2005) Hinge Residue Ile260 of DNA Polymerase β is Important for Enzyme Activity and Fidelity Biochemistry 44, 3775-3784
    • (2005) Biochemistry , vol.44 , pp. 3775-3784
    • Starcevic, D.1    Dalal, S.2    Sweasy, J.B.3
  • 34
    • 0028049441 scopus 로고
    • Structure of Ternary Complexes of Rat DNA Polymerase β, a DNA Template-Primer, and ddCTP
    • Pelletier, H., Sawaya, M. R., Kumar, A., Wilson, S. H., and Kraut, H. (1994) Structure of Ternary Complexes of Rat DNA Polymerase β, a DNA Template-Primer, and ddCTP Science 264, 1891-1903
    • (1994) Science , vol.264 , pp. 1891-1903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, H.5
  • 35
    • 34250626890 scopus 로고    scopus 로고
    • Loop II of DNA polymerase β is important for polymerization activity and fidelity
    • Lin, G. C., Jaeger, J., and Sweasy, J. B. (2007) Loop II of DNA polymerase β is important for polymerization activity and fidelity Nucleic Acids Res. 35, 2924-2935
    • (2007) Nucleic Acids Res. , vol.35 , pp. 2924-2935
    • Lin, G.C.1    Jaeger, J.2    Sweasy, J.B.3
  • 36
    • 0033525093 scopus 로고    scopus 로고
    • 3′-Azido-3′-deoxythymidine-resistant Mutants of DNA Polymerase β Identified by in Vivo Selection
    • Kosa, J. L. and Sweasy, J. B. (1999) 3′-Azido-3′- deoxythymidine-resistant Mutants of DNA Polymerase β Identified by in Vivo Selection J. Biol. Chem. 274, 3851-3858
    • (1999) J. Biol. Chem. , vol.274 , pp. 3851-3858
    • Kosa, J.L.1    Sweasy, J.B.2
  • 37
    • 0001464258 scopus 로고
    • Construction of a plasmid that overproduces the large proteolytic fragment (Klenow fragment) of DNA polymerase i of Escherichia coli
    • Joyce, C. M. and Grindley, N. D. (1983) Construction of a plasmid that overproduces the large proteolytic fragment (Klenow fragment) of DNA polymerase I of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 80, 1830-1834
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 1830-1834
    • Joyce, C.M.1    Grindley, N.D.2
  • 38
    • 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., 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.F.2    Joyce, C.M.3
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt, G. (1996) Use of non-crystallographic symmetry in protein structure refinement Acta Crystallogr. D52, 842-857
    • (1996) Acta Crystallogr. , vol.52 , pp. 842-857
    • Kleywegt, G.1
  • 46
    • 0012293235 scopus 로고    scopus 로고
    • DeLano Scientific, San Carlos, CA.
    • DeLano, W. L. (2001) PyMol, DeLano Scientific, San Carlos, CA.
    • (2001) PyMol
    • Delano, W.L.1
  • 47
    • 39149130715 scopus 로고    scopus 로고
    • The Leu22Pro tumor-associated variant of DNA polymerase β is dRP lyase deficient
    • Dalal, S., Chikova, A., Jaeger, J., and Sweasy, J. B. (2008) The Leu22Pro tumor-associated variant of DNA polymerase β; is dRP lyase deficient Nucleic Acids Res. 36, 411-422
    • (2008) Nucleic Acids Res. , vol.36 , pp. 411-422
    • Dalal, S.1    Chikova, A.2    Jaeger, J.3    Sweasy, J.B.4
  • 48
    • 0028136070 scopus 로고
    • Crystal Structure of Rat DNA Polymerase β: Evidence for a Common Polymerase Mechanism
    • Sawaya, M. R., Pelletier, H., Kumar, A., Wilson, S. H., and Kraut, J. (1994) Crystal Structure of Rat DNA Polymerase β: Evidence for a Common Polymerase Mechanism Science 264, 1930-1935
    • (1994) Science , vol.264 , pp. 1930-1935
    • Sawaya, M.R.1    Pelletier, H.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 50
  • 51
    • 0029817866 scopus 로고    scopus 로고
    • Crystal Structures of Human DNA Polymerase β Complexed with DNA: Implications for Catalytic Mechanism, Processivity, and Fidelity
    • Pelletier, H., Sawaya, M. R., Wolfle, W., Wilson, S. H., and Kraut, J. (1996) Crystal Structures of Human DNA Polymerase β Complexed with DNA: Implications for Catalytic Mechanism, Processivity, and Fidelity Biochemistry 35, 12742-12761
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfle, W.3    Wilson, S.H.4    Kraut, J.5
  • 52
    • 33745211646 scopus 로고    scopus 로고
    • Activities and mechanism of DNA polymerase β
    • Beard, W. A., Prasad, R., and Wilson, S. H. (2006) Activities and mechanism of DNA polymerase β Methods Enzymol. 408, 91-107
    • (2006) Methods Enzymol. , vol.408 , pp. 91-107
    • Beard, W.A.1    Prasad, R.2    Wilson, S.H.3
  • 53
    • 17544370107 scopus 로고    scopus 로고
    • Enzyme-DNA Interactions Required for Efficient Nucleotide Incorporation and Discrimination in Human DNA Polymerase β
    • Beard, W. A., Osheroff, W. P., Prasad, R., Sawaya, M. R., Jaju, M., Wood, T. G., Kraut, J., Kunkel, T. A., and Wilson, S. H. (1996) Enzyme-DNA Interactions Required for Efficient Nucleotide Incorporation and Discrimination in Human DNA Polymerase β J. Biol. Chem. 271, 12141-12144
    • (1996) J. Biol. Chem. , vol.271 , pp. 12141-12144
    • Beard, W.A.1    Osheroff, W.P.2    Prasad, R.3    Sawaya, M.R.4    Jaju, M.5    Wood, T.G.6    Kraut, J.7    Kunkel, T.A.8    Wilson, S.H.9
  • 54
    • 0021872030 scopus 로고
    • The Mutational Specificity of DNA Polymerase-β during in Vitro DNA Synthesis
    • Kunkel, T. A. (1985) The Mutational Specificity of DNA Polymerase-β during in Vitro DNA Synthesis J. Biol. Chem. 260, 5787-5796
    • (1985) J. Biol. Chem. , vol.260 , pp. 5787
    • Kunkel, T.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.