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Volumn 408, Issue , 2006, Pages 91-107

Activities and Mechanism of DNA Polymerase β

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA DIRECTED DNA POLYMERASE BETA; LYASE; NUCLEOTIDYLTRANSFERASE;

EID: 33745211646     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(06)08007-4     Document Type: Review
Times cited : (55)

References (44)
  • 1
    • 0023839680 scopus 로고
    • Expression of human DNA polymerase β in Escherichia coli and characterization of the recombinant enzyme
    • Abbotts J., Sen Gupta D.N., Zmudzka B., Widen S.G., Notario V., and Wilson S.H. Expression of human DNA polymerase β in Escherichia coli and characterization of the recombinant enzyme. Biochemistry 27 (1988) 901-909
    • (1988) Biochemistry , vol.27 , pp. 901-909
    • Abbotts, J.1    Sen Gupta, D.N.2    Zmudzka, B.3    Widen, S.G.4    Notario, V.5    Wilson, S.H.6
  • 2
    • 0028803178 scopus 로고
    • Purification and domain-mapping of mammalian DNA polymerase β
    • Beard W.A., and Wilson S.H. Purification and domain-mapping of mammalian DNA polymerase β. Methods Enzymol. 262 (1995) 98-107
    • (1995) Methods Enzymol. , vol.262 , pp. 98-107
    • Beard, W.A.1    Wilson, S.H.2
  • 4
    • 0037566670 scopus 로고    scopus 로고
    • Structural insights into the origins of DNA polymerase fidelity
    • Beard W.A., and Wilson S.H. Structural insights into the origins of DNA polymerase fidelity. Structure 11 (2003) 489-496
    • (2003) Structure , vol.11 , pp. 489-496
    • Beard, W.A.1    Wilson, S.H.2
  • 5
    • 3843122085 scopus 로고    scopus 로고
    • Influence of DNA structure on DNA polymerase β active site function: Extension of mutagenic DNA intermediates
    • Beard W.A., Shock D.D., and Wilson S.H. Influence of DNA structure on DNA polymerase β active site function: Extension of mutagenic DNA intermediates. J. Biol. Chem. 279 (2004) 31921-31929
    • (2004) J. Biol. Chem. , vol.279 , pp. 31921-31929
    • Beard, W.A.1    Shock, D.D.2    Wilson, S.H.3
  • 6
    • 0037032998 scopus 로고    scopus 로고
    • Efficiency of correct nucleotide insertion governs DNA polymerase fidelity
    • Beard W.A., Shock D.D., Vande Berg B.J., and Wilson S.H. Efficiency of correct nucleotide insertion governs DNA polymerase fidelity. J. Biol. Chem. 277 (2002) 47393-47398
    • (2002) J. Biol. Chem. , vol.277 , pp. 47393-47398
    • Beard, W.A.1    Shock, D.D.2    Vande Berg, B.J.3    Wilson, S.H.4
  • 7
    • 0031985891 scopus 로고    scopus 로고
    • Impairment of proliferating cell nuclear antigen-dependent apurinic/apyrimidinic site repair on linear DNA
    • Biade S., Sobol R.W., Wilson S.H., and Matsumoto Y. Impairment of proliferating cell nuclear antigen-dependent apurinic/apyrimidinic site repair on linear DNA. J. Biol. Chem. 273 (1998) 898-902
    • (1998) J. Biol. Chem. , vol.273 , pp. 898-902
    • Biade, S.1    Sobol, R.W.2    Wilson, S.H.3    Matsumoto, Y.4
  • 10
    • 0034615978 scopus 로고    scopus 로고
    • Mapping of the 5′-2-deoxyribose-5-phosphate lyase active site in DNA polymerase β by mass spectrometry
    • Deterding L.J., Prasad R., Mullen G.P., Wilson S.H., and Tomer K.B. Mapping of the 5′-2-deoxyribose-5-phosphate lyase active site in DNA polymerase β by mass spectrometry. J. Biol. Chem. 275 (2000) 10463-10471
    • (2000) J. Biol. Chem. , vol.275 , pp. 10463-10471
    • Deterding, L.J.1    Prasad, R.2    Mullen, G.P.3    Wilson, S.H.4    Tomer, K.B.5
  • 11
    • 0242299709 scopus 로고    scopus 로고
    • Monitoring base excision repair by in vitro assays
    • Dianov G.L. Monitoring base excision repair by in vitro assays. Toxicology 193 (2003) 35-41
    • (2003) Toxicology , vol.193 , pp. 35-41
    • Dianov, G.L.1
  • 12
    • 0033600570 scopus 로고    scopus 로고
    • Replication protein A stimulates proliferating cell nuclear antigen-dependent repair of abasic sites in DNA by human cell extracts
    • Dianov G.L., Jensen B.R., Kenny M.K., and Bohr V.A. Replication protein A stimulates proliferating cell nuclear antigen-dependent repair of abasic sites in DNA by human cell extracts. Biochemistry 38 (1999) 11021-11025
    • (1999) Biochemistry , vol.38 , pp. 11021-11025
    • Dianov, G.L.1    Jensen, B.R.2    Kenny, M.K.3    Bohr, V.A.4
  • 13
    • 0032493309 scopus 로고    scopus 로고
    • Deoxyribose phosphate excision by the N-terminal domain of the polymerase β: The mechanism revisited
    • Feng J.-A., Crasto C.J., and Matsumoto Y. Deoxyribose phosphate excision by the N-terminal domain of the polymerase β: The mechanism revisited. Biochemistry 37 (1998) 9605-9611
    • (1998) Biochemistry , vol.37 , pp. 9605-9611
    • Feng, J.-A.1    Crasto, C.J.2    Matsumoto, Y.3
  • 14
    • 0032539979 scopus 로고    scopus 로고
    • Different DNA polymerases are involved in the 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. Different DNA polymerases are involved in the short- and long-patch base excision repair in mammalian cells. Biochemistry 37 (1998) 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
  • 16
    • 0025771210 scopus 로고
    • Ribozyme-catalyzed and nonenzymatic reactions of phosphate diesters: Rate effects upon substitution of sulfur for a nonbridging phosphoryl oxygen atom
    • Herschlag D., Piccirilli J.A., and Cech T.R. Ribozyme-catalyzed and nonenzymatic reactions of phosphate diesters: Rate effects upon substitution of sulfur for a nonbridging phosphoryl oxygen atom. Biochemistry 30 (1991) 4844-4854
    • (1991) Biochemistry , vol.30 , pp. 4844-4854
    • Herschlag, D.1    Piccirilli, J.A.2    Cech, T.R.3
  • 17
    • 0034695632 scopus 로고    scopus 로고
    • Protection against methylation-induced cytotoxicity by DNA polymerase β-dependent long patch base excision repair
    • Horton J.K., Prasad R., Hou E., and Wilson S.H. Protection against methylation-induced cytotoxicity by DNA polymerase β-dependent long patch base excision repair. J. Biol. Chem. 275 (2000) 2211-2218
    • (2000) J. Biol. Chem. , vol.275 , pp. 2211-2218
    • Horton, J.K.1    Prasad, R.2    Hou, E.3    Wilson, S.H.4
  • 18
    • 0642315208 scopus 로고
    • Transient-state kinetic analysis of enzyme reaction pathways
    • Sigman D.S. (Ed), Academic Press, New York
    • Johnson K.A. Transient-state kinetic analysis of enzyme reaction pathways. In: Sigman D.S. (Ed). "The Enzymes: Mechanisms of Catalysis" Vol. XX (1992), Academic Press, New York 1-61
    • (1992) "The Enzymes: Mechanisms of Catalysis" , vol.XX , pp. 1-61
    • Johnson, K.A.1
  • 19
    • 8544278025 scopus 로고    scopus 로고
    • DNA polymerase fidelity: Kinetics, structure, and checkpoints
    • Joyce C.M., and Benkovic S.J. DNA polymerase fidelity: Kinetics, structure, and checkpoints. Biochemistry 43 (2004) 14317-14324
    • (2004) Biochemistry , vol.43 , pp. 14317-14324
    • Joyce, C.M.1    Benkovic, S.J.2
  • 21
    • 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 Lindahl T. Second pathway for completion of human DNA base excision-repair: Reconstitution with purified proteins and requirement for DNase IV (FEN1). EMBO J. 16 (1997) 3341-3348
    • (1997) EMBO J. , vol.16 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 22
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair
    • Matsumoto Y., and Kim K. Excision of deoxyribose phosphate residues by DNA polymerase β during DNA repair. Science 269 (1995) 699-702
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, K.2
  • 23
    • 0033597779 scopus 로고    scopus 로고
    • Base substitution specificity of DNA polymerase β depends on interactions in the DNA minor groove
    • Osheroff W.P., Beard W.A., Wilson S.H., and Kunkel T.A. Base substitution specificity of DNA polymerase β depends on interactions in the DNA minor groove. J. Biol. Chem. 274 (1999) 20749-20752
    • (1999) J. Biol. Chem. , vol.274 , pp. 20749-20752
    • Osheroff, W.P.1    Beard, W.A.2    Wilson, S.H.3    Kunkel, T.A.4
  • 24
    • 0344527720 scopus 로고    scopus 로고
    • The fidelity of DNA polymerase β during distributive and processive DNA synthesis
    • Osheroff W.P., Jung H.K., Beard W.A., Wilson S.H., and Kunkel T.A. The fidelity of DNA polymerase β during distributive and processive DNA synthesis. J. Biol. Chem. 274 (1999) 3642-3650
    • (1999) J. Biol. Chem. , vol.274 , pp. 3642-3650
    • Osheroff, W.P.1    Jung, H.K.2    Beard, W.A.3    Wilson, S.H.4    Kunkel, T.A.5
  • 25
    • 0034142142 scopus 로고    scopus 로고
    • Molecular cloning and high-level expression of human polymerase β cDNA and comparison of the purified recombinant human and rat enzymes
    • Patterson T.A., Little W., Cheng X., Widen S.G., Kumar A., Beard W.A., and Wilson S.H. Molecular cloning and high-level expression of human polymerase β cDNA and comparison of the purified recombinant human and rat enzymes. Protein Expr. Purif. 18 (2000) 100-110
    • (2000) Protein Expr. Purif. , vol.18 , pp. 100-110
    • Patterson, T.A.1    Little, W.2    Cheng, X.3    Widen, S.G.4    Kumar, A.5    Beard, W.A.6    Wilson, S.H.7
  • 26
    • 0029892846 scopus 로고    scopus 로고
    • Evidence for an imino intermediate in the DNA polymerase β deoxyribose phosphate excision reaction
    • Piersen C.E., Prasad R., Wilson S.H., and Lloyd R.S. Evidence for an imino intermediate in the DNA polymerase β deoxyribose phosphate excision reaction. J. Biol. Chem. 271 (1996) 17811-17815
    • (1996) J. Biol. Chem. , vol.271 , pp. 17811-17815
    • Piersen, C.E.1    Prasad, R.2    Wilson, S.H.3    Lloyd, R.S.4
  • 28
    • 0028338562 scopus 로고
    • Studies of gapped DNA substrate binding by mammalian DNA polymerase β: Dependence on 5′-phosphate group
    • Prasad R., Beard W.A., and Wilson S.H. Studies of gapped DNA substrate binding by mammalian DNA polymerase β: Dependence on 5′-phosphate group. J. Biol. Chem. 269 (1994) 18096-18101
    • (1994) J. Biol. Chem. , vol.269 , pp. 18096-18101
    • Prasad, R.1    Beard, W.A.2    Wilson, S.H.3
  • 29
    • 0032510962 scopus 로고    scopus 로고
    • Human DNA polymerase β deoxyribose phosphate lyase: Substrate specificity and catalytic mechanism
    • Prasad R., Beard W.A., Strauss P.R., and Wilson S.H. Human DNA polymerase β deoxyribose phosphate lyase: Substrate specificity and catalytic mechanism. J. Biol. Chem. 273 (1998) 15263-15270
    • (1998) J. Biol. Chem. , vol.273 , pp. 15263-15270
    • Prasad, R.1    Beard, W.A.2    Strauss, P.R.3    Wilson, S.H.4
  • 30
    • 0034635403 scopus 로고    scopus 로고
    • FEN1 stimulation of DNA polymerase β mediates an excision step in mammalian long patch base excision repair
    • Prasad R., Dianov G.L., Bohr V.A., and Wilson S.H. FEN1 stimulation of DNA polymerase β mediates an excision step in mammalian long patch base excision repair. J. Biol. Chem. 275 (2000) 4460-4466
    • (2000) J. Biol. Chem. , vol.275 , pp. 4460-4466
    • Prasad, R.1    Dianov, G.L.2    Bohr, V.A.3    Wilson, S.H.4
  • 31
    • 0035980003 scopus 로고    scopus 로고
    • DNA polymerase β-mediated long patch base excision repair: Poly(ADP-ribose) polymerase-1 stimulates strand displacement DNA synthesis
    • Prasad R., Lavrik O.I., Kim S.J., Kedar P., Yang X.P., Vande Berg B.J., and Wilson S.H. DNA polymerase β-mediated long patch base excision repair: Poly(ADP-ribose) polymerase-1 stimulates strand displacement DNA synthesis. J. Biol. Chem. 276 (2001) 32411-32414
    • (2001) J. Biol. Chem. , vol.276 , pp. 32411-32414
    • Prasad, R.1    Lavrik, O.I.2    Kim, S.J.3    Kedar, P.4    Yang, X.P.5    Vande Berg, B.J.6    Wilson, S.H.7
  • 32
    • 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 P., Wilson S.H., Kraut J., and Pelletier H. Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: Evidence for an induced fit mechanism. Biochemistry 36 (1997) 11205-11215
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, P.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 33
    • 0028966181 scopus 로고
    • DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract
    • Singhal R.K., Prasad R., and Wilson S.H. DNA polymerase β conducts the gap-filling step in uracil-initiated base excision repair in a bovine testis nuclear extract. J. Biol. Chem. 270 (1995) 949-957
    • (1995) J. Biol. Chem. , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.H.3
  • 34
    • 0027179827 scopus 로고
    • Short gap-filling synthesis by DNA polymerase β is processive
    • Singhal R.K., and Wilson S.H. Short gap-filling synthesis by DNA polymerase β is processive. J. Biol. Chem. 268 (1993) 15906-15911
    • (1993) J. Biol. Chem. , vol.268 , pp. 15906-15911
    • Singhal, R.K.1    Wilson, S.H.2
  • 35
    • 0028933306 scopus 로고
    • Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase
    • Slupphaug G., Eftedal I., Kavli B., Bharati S., Helle N.M., Haug T., Levine D.W., and Krokan H.E. Properties of a recombinant human uracil-DNA glycosylase from the UNG gene and evidence that UNG encodes the major uracil-DNA glycosylase. Biochemistry 34 (1995) 128-138
    • (1995) Biochemistry , vol.34 , pp. 128-138
    • Slupphaug, G.1    Eftedal, I.2    Kavli, B.3    Bharati, S.4    Helle, N.M.5    Haug, T.6    Levine, D.W.7    Krokan, H.E.8
  • 37
    • 0034659935 scopus 로고    scopus 로고
    • The lyase activity of the DNA repair protein β-polymerase protects from DNA-damage-induced cytotoxicity
    • Sobol R.W., Prasad R., Evenski A., Baker A., Yang X.P., Horton J.K., and Wilson S.H. The lyase activity of the DNA repair protein β-polymerase protects from DNA-damage-induced cytotoxicity. Nature 405 (2000) 807-810
    • (2000) Nature , vol.405 , pp. 807-810
    • Sobol, R.W.1    Prasad, R.2    Evenski, A.3    Baker, A.4    Yang, X.P.5    Horton, J.K.6    Wilson, S.H.7
  • 39
    • 0031021533 scopus 로고    scopus 로고
    • Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism
    • Strauss P.R., Beard W.A., Patterson R.A., and Wilson S.H. Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism. J. Biol. Chem. 272 (1997) 1302-1307
    • (1997) J. Biol. Chem. , vol.272 , pp. 1302-1307
    • Strauss, P.R.1    Beard, W.A.2    Patterson, R.A.3    Wilson, S.H.4
  • 40
    • 0018799858 scopus 로고
    • Steady-state kinetics of mouse DNA polymerase β
    • Tanabe K., Bohn E.W., and Wilson S.H. Steady-state kinetics of mouse DNA polymerase β. Biochemistry 18 (1979) 3401-3406
    • (1979) Biochemistry , vol.18 , pp. 3401-3406
    • Tanabe, K.1    Bohn, E.W.2    Wilson, S.H.3
  • 41
    • 0035793560 scopus 로고    scopus 로고
    • DNA structure and aspartate 276 influence nucleotide binding to human DNA polymerase β: Implication for the identity of the rate-limiting conformational change
    • Vande Berg B.J., Beard W.A., and Wilson S.H. DNA structure and aspartate 276 influence nucleotide binding to human DNA polymerase β: Implication for the identity of the rate-limiting conformational change. J. Biol. Chem. 276 (2001) 3408-3416
    • (2001) J. Biol. Chem. , vol.276 , pp. 3408-3416
    • Vande Berg, B.J.1    Beard, W.A.2    Wilson, S.H.3
  • 42
    • 0037135556 scopus 로고    scopus 로고
    • Mismatch repair in human nuclear extracts: Quantitative analyses of excision of nicked circular mismatched DNA substrates, constructed by a new technique employing synthetic oligonucleotides
    • Wang H., and Hays J.B. Mismatch repair in human nuclear extracts: Quantitative analyses of excision of nicked circular mismatched DNA substrates, constructed by a new technique employing synthetic oligonucleotides. J. Biol. Chem. 277 (2002) 26136-26142
    • (2002) J. Biol. Chem. , vol.277 , pp. 26136-26142
    • Wang, H.1    Hays, J.B.2
  • 43
    • 0027970892 scopus 로고
    • Mammalian DNA ligase II is highly homologous with vaccinia DNA ligase: Identification of the DNA ligase II active site for enzyme-adenylate formation
    • Wang Y.C., Burkhart W.A., Mackey Z.B., Moyer M.B., Ramos W., Husain I., Chen J., Besterman J.M., and Tomkinson A.E. Mammalian DNA ligase II is highly homologous with vaccinia DNA ligase: Identification of the DNA ligase II active site for enzyme-adenylate formation. J. Biol. Chem. 269 (1994) 31923-31928
    • (1994) J. Biol. Chem. , vol.269 , pp. 31923-31928
    • Wang, Y.C.1    Burkhart, W.A.2    Mackey, Z.B.3    Moyer, M.B.4    Ramos, W.5    Husain, I.6    Chen, J.7    Besterman, J.M.8    Tomkinson, A.E.9
  • 44
    • 0036295231 scopus 로고    scopus 로고
    • Polymerase β simulations suggest that Arg258 rotation is a slow step rather than large subdomain motions per se
    • Yang L., Beard W.A., Wilson S.H., Broyde S., and Schlick T. Polymerase β simulations suggest that Arg258 rotation is a slow step rather than large subdomain motions per se. J. Mol. Biol. 317 (2002) 679-699
    • (2002) J. Mol. Biol. , vol.317 , pp. 679-699
    • Yang, L.1    Beard, W.A.2    Wilson, S.H.3    Broyde, S.4    Schlick, T.5


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