메뉴 건너뛰기




Volumn 289, Issue 23, 2014, Pages 16541-16550

Fluorescence resonance energy transfer studies of DNA polymerase β the critical role of fingers domain movements and a novel non-covalent step During nucleotide selection

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ENERGY TRANSFER; FLUORESCENCE; NAPHTHALENE; POLYMERS;

EID: 84902192012     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.561878     Document Type: Article
Times cited : (24)

References (59)
  • 1
    • 10944251591 scopus 로고    scopus 로고
    • Repair and genetic consequences of endogenous DNA base damage in mammalian cells
    • Barnes, D. E., and Lindahl, T. (2004) Repair and genetic consequences of endogenous DNA base damage in mammalian cells. Annu. Rev. Genet. 38, 445-476
    • (2004) Annu. Rev. Genet. , vol.38 , pp. 445-476
    • Barnes, D.E.1    Lindahl, T.2
  • 3
    • 77949571124 scopus 로고    scopus 로고
    • DNA polymerase family X: Function, structure, and cellular roles
    • Yamtich, J., and Sweasy, J. B. (2010) DNA polymerase family X: function, structure, and cellular roles. Biochim. Biophys. Acta 1804, 1136-1150
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1136-1150
    • Yamtich, J.1    Sweasy, J.B.2
  • 4
    • 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. (1998) Human DNA polymerase β deoxyribose phosphate lyase. Substrate specificity and catalytic mechanism. J. Biol. Chem. 273, 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
  • 5
    • 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
  • 6
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta 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 beta 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
  • 7
    • 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
  • 8
    • 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
  • 9
    • 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
    • Van de Berg, B. J., Beard, W. A., and Wilson, S. H. (2001) 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, 3408-3416
    • (2001) J. Biol. Chem. , vol.276 , pp. 3408-3416
    • Van De Berg, B.J.1    Beard, W.A.2    Wilson, S.H.3
  • 10
    • 0021872030 scopus 로고
    • The mutational specificity of DNA polymerase-β during in vitro DNA synthesis: Production of frameshift, base substitution, and deletion mutations
    • Kunkel, T. A. (1985) The mutational specificity of DNA polymerase-β during in vitro DNA synthesis: production of frameshift, base substitution, and deletion mutations. J. Biol. Chem. 260, 5787-5796
    • (1985) J. Biol. Chem. , vol.260 , pp. 5787-5796
    • Kunkel, T.A.1
  • 11
    • 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
  • 12
    • 0033544858 scopus 로고    scopus 로고
    • The E249K mutator mutant of DNA polymerase β extends mispaired termini
    • Kosa, J. L., and Sweasy, J. B. (1999) The E249K mutator mutant of DNA polymerase β extends mispaired termini. J. Biol. Chem. 274, 35866-35872
    • (1999) J. Biol. Chem. , vol.274 , pp. 35866-35872
    • Kosa, J.L.1    Sweasy, J.B.2
  • 13
    • 0035949644 scopus 로고    scopus 로고
    • A DNA polymerase β mutator mutant with reduced nucleotide discrimination and increased 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 increased 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
  • 14
    • 84863533866 scopus 로고    scopus 로고
    • The E288K colon tumor variant of DNA polymerase β is a sequence specific mutator
    • Murphy, D. L., Donigan, K. A., Jaeger, J., and Sweasy, J. B. (2012) The E288K colon tumor variant of DNA polymerase β is a sequence specific mutator. Biochemistry 51, 5269-5275
    • (2012) Biochemistry , vol.51 , pp. 5269-5275
    • Murphy, D.L.1    Donigan, K.A.2    Jaeger, J.3    Sweasy, J.B.4
  • 15
    • 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
  • 16
    • 0035815755 scopus 로고    scopus 로고
    • Y265H mutator mutant of DNA polymerase β: Proper teometric alignment is critical for fidelity
    • Shah, A. M., Li, S.-X., Anderson, K. S., and Sweasy, J. B. (2001) Y265H mutator mutant of DNA polymerase β: proper teometric alignment is critical for fidelity. J. Biol. Chem. 276, 10824-10831
    • (2001) J. Biol. Chem. , vol.276 , pp. 10824-10831
    • Shah, A.M.1    Li, S.-X.2    Anderson, K.S.3    Sweasy, J.B.4
  • 17
    • 80755156306 scopus 로고    scopus 로고
    • Kinetic mechanism of active site assembly and chemical catalysis of DNA polymeraseβ
    • Balbo, P. B., Wang, E. C, and Tsai, M.-D. (2011) Kinetic mechanism of active site assembly and chemical catalysis of DNA polymeraseβ. Biochemistry 50, 9865-9875
    • (2011) Biochemistry , vol.50 , pp. 9865-9875
    • Balbo, P.B.1    Wang, E.C.2    Tsai, M.-D.3
  • 18
    • 16344376908 scopus 로고    scopus 로고
    • Use of viscogens, dNTPαS, and rhodium (III) as probes in stoppedflow experiments to obtain new evidence for the mechanism of catalysis by DNA polymerase
    • Bakhtina, M., Lee, S., Wang, Y., Dunlap, C, Lamarche, B., and Tsai, M.-D. (2005) Use of viscogens, dNTPαS, and rhodium (III) as probes in stoppedflow experiments to obtain new evidence for the mechanism of catalysis by DNA polymerase. Biochemistry 44, 5177-5187
    • (2005) Biochemistry , vol.44 , pp. 5177-5187
    • Bakhtina, M.1    Lee, S.2    Wang, Y.3    Dunlap, C.4    Lamarche, B.5    Tsai, M.-D.6
  • 19
    • 0030760966 scopus 로고    scopus 로고
    • DNA polymeraseβ: Multiple conformational changes in the mechanism of catalysis
    • Zhong, X., Patel, S. S., Werneburg, B. G., and Tsai, M.-D. (1997) DNA polymeraseβ: multiple conformational changes in the mechanism of catalysis. Biochemistry 36, 11891-11900
    • (1997) Biochemistry , vol.36 , pp. 11891-11900
    • Zhong, X.1    Patel, S.S.2    Werneburg, B.G.3    Tsai, M.-D.4
  • 20
    • 0030783515 scopus 로고    scopus 로고
    • Increased activity and fidelity of DNA polymeraseβ on single-nucleotide gapped DNA
    • Chagovetz, A. M., Sweasy, J. B., and Preston, B. D. (1997) Increased activity and fidelity of DNA polymeraseβ on single-nucleotide gapped DNA. J. Biol. Chem. 272, 27501-27504
    • (1997) J. Biol. Chem. , vol.272 , pp. 27501-27504
    • Chagovetz, A.M.1    Sweasy, J.B.2    Preston, B.D.3
  • 21
    • 0027179827 scopus 로고
    • Short gap-filling synthesis by DNA polymeraseβ is processive
    • Singhal, R. K., and Wilson, S. H. (1993) Short gap-filling synthesis by DNA polymeraseβ 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
  • 22
    • 84889007271 scopus 로고    scopus 로고
    • The E295K cancer variant of human polymeraseβ favors the mismatch conformational pathway during nucleotide selection
    • Eckenroth, B. E., Towle-Weicksel, J. B., Sweasy, J. B., and Doublie, S. (2013) The E295K cancer variant of human polymeraseβ favors the mismatch conformational pathway during nucleotide selection. J. Biol. Chem. 288, 34850-34860
    • (2013) J. Biol. Chem. , vol.288 , pp. 34850-34860
    • Eckenroth, B.E.1    Towle-Weicksel, J.B.2    Sweasy, J.B.3    Doublie, S.4
  • 23
    • 44949114390 scopus 로고    scopus 로고
    • Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity
    • Joyce, C. M., Potapova, O., Delucia, A. M., Huang, X., Basu, V. P., and Grindley, N. D. (2008) Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. Biochemistry 47, 6103-6116
    • (2008) Biochemistry , vol.47 , pp. 6103-6116
    • Joyce, C.M.1    Potapova, O.2    Delucia, A.M.3    Huang, X.4    Basu, V.P.5    Grindley, N.D.6
  • 24
    • 48649103574 scopus 로고    scopus 로고
    • The Asp285 variant of DNA polymeraseβ extends mispaired primer termini via increased nucleotide binding
    • Murphy, D. L., Kosa, J., Jaeger, J., and Sweasy, J. B. (2008) The Asp285 variant of DNA polymeraseβ extends mispaired primer termini via increased nucleotide binding. Biochemistry 47, 8048-8057
    • (2008) Biochemistry , vol.47 , pp. 8048-8057
    • Murphy, D.L.1    Kosa, J.2    Jaeger, J.3    Sweasy, J.B.4
  • 25
    • 0018450898 scopus 로고
    • Measurement of the dead time of a fluorescence stopped-flow instrument
    • Peterman, B. F. (1979) Measurement of the dead time of a fluorescence stopped-flow instrument. Anal. Biochem. 93, 442-444
    • (1979) Anal. Biochem. , vol.93 , pp. 442-444
    • Peterman, B.F.1
  • 26
    • 60549105802 scopus 로고    scopus 로고
    • Global kinetic explorer: A new computer program for dynamic simulation and fitting of kinetic data
    • Johnson, K. A., Simpson, Z. B., and Blom, T. (2009) Global kinetic explorer: a new computer program for dynamic simulation and fitting of kinetic data. Anal. Biochem. 387, 20-29
    • (2009) Anal. Biochem. , vol.387 , pp. 20-29
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 27
    • 60549112465 scopus 로고    scopus 로고
    • FitSpace explorer: An algorithm to evaluate multidimensional parameter space in fitting kinetic data
    • Johnson, K. A., Simpson, Z. B., and Blom, T. (2009) FitSpace explorer: an algorithm to evaluate multidimensional parameter space in fitting kinetic data. Anal. Biochem. 387, 30-41
    • (2009) Anal. Biochem. , vol.387 , pp. 30-41
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 29
    • 84868595539 scopus 로고    scopus 로고
    • Catalytic effects of mutations of distant protein residues in human DNA polymeraseβ: Theory and experiment
    • Klvana, M., Murphy, D. L., Jeřábek, P., Goodman, M. F., Warshel, A., Sweasy, J. B., and Florian, J. (2012) Catalytic effects of mutations of distant protein residues in human DNA polymeraseβ: theory and experiment. Biochemistry 51, 8829-8843
    • (2012) Biochemistry , vol.51 , pp. 8829-8843
    • Klvana, M.1    Murphy, D.L.2    Jeřábek, P.3    Goodman, M.F.4    Warshel, A.5    Sweasy, J.B.6    Florian, J.7
  • 30
    • 0037125947 scopus 로고    scopus 로고
    • Use of 2-aminopurine and tryptophan fluorescence as probes in kinetic analyses of DNA polymerase
    • Dunlap, C. A., and Tsai, M.-D. (2002) Use of 2-aminopurine and tryptophan fluorescence as probes in kinetic analyses of DNA polymerase. Biochemistry 41, 11226-11235
    • (2002) Biochemistry , vol.41 , pp. 11226-11235
    • Dunlap, C.A.1    Tsai, M.-D.2
  • 31
    • 34248370198 scopus 로고    scopus 로고
    • A unified kinetic mechanism applicable to multiple DNA polymerases
    • Bakhtina, M., Roettger, M. P., Kumar, S., and Tsai, M.-D. (2007) A unified kinetic mechanism applicable to multiple DNA polymerases. Biochemistry 46, 5463-5472
    • (2007) Biochemistry , vol.46 , pp. 5463-5472
    • Bakhtina, M.1    Roettger, M.P.2    Kumar, S.3    Tsai, M.-D.4
  • 32
    • 84901036048 scopus 로고    scopus 로고
    • The S229L colon tumor-associated variant of DNA polymeraseβ induces cellular transformation as a result of decreased polymerization efficiency
    • Nemec, A. A., Murphy, D. L., Donigan, K. A., and Sweasy, J. B. (2014) The S229L colon tumor-associated variant of DNA polymeraseβ induces cellular transformation as a result of decreased polymerization efficiency. J. Biol. Chem. 289, 13708-13716
    • (2014) J. Biol. Chem. , vol.289 , pp. 13708-13716
    • Nemec, A.A.1    Murphy, D.L.2    Donigan, K.A.3    Sweasy, J.B.4
  • 33
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymeraseβ, a DNA template-primer, and ddCTP
    • Pelletier, H., Sawaya, M. R., Kumar, A., Wilson, S. H., and Kraut, J. (1994) Structures of ternary complexes of rat DNA polymeraseβ, 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, J.5
  • 34
    • 84863676249 scopus 로고    scopus 로고
    • Watching DNA polymerase 17 make a phosphodiester bond
    • Nakamura, T., Zhao, Y., Yamagata, Y., Hua, Y. J., and Yang, W. (2012) Watching DNA polymerase 17 make a phosphodiester bond. Nature 487, 196-201
    • (2012) Nature , vol.487 , pp. 196-201
    • Nakamura, T.1    Zhao, Y.2    Yamagata, Y.3    Hua, Y.J.4    Yang, W.5
  • 35
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation
    • Li, Y., Korolev, S., and Waksman, G. (1998) Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation. EMBO J. 17, 7514-7525
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 36
    • 79955016714 scopus 로고    scopus 로고
    • A triad interaction in the fingers subdomain of DNA polymeraseβ controls polymerase activity
    • Murphy, D. L., Jaeger, J., and Sweasy, J. B. (2011) A triad interaction in the fingers subdomain of DNA polymeraseβ controls polymerase activity. J. Am. Chem. Soc. 133, 6279-6287
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 6279-6287
    • Murphy, D.L.1    Jaeger, J.2    Sweasy, J.B.3
  • 37
    • 0031053276 scopus 로고    scopus 로고
    • DNA polymeraseβ: Structure-fidelity relationship from pre-steady-state kinetic analyses of all possible correct and incorrect base pairs for wild type and R283A mutant
    • Ahn, J., Werneburg, B. G., and Tsai, M.-D. (1997) DNA polymeraseβ: structure-fidelity relationship from pre-steady-state kinetic analyses of all possible correct and incorrect base pairs for wild type and R283A mutant. Biochemistry 36, 1100-1107
    • (1997) Biochemistry , vol.36 , pp. 1100-1107
    • Ahn, J.1    Werneburg, B.G.2    Tsai, M.-D.3
  • 38
    • 80054973131 scopus 로고    scopus 로고
    • Structural insights into complete metal ion coordination from ternary complexes of B family RB69 DNA polymerase
    • Xia, S., Wang, M., Blaha, G., Konigsberg W. H, and Wang J. (2011) Structural insights into complete metal ion coordination from ternary complexes of B family RB69 DNA polymerase. Biochemistry 50, 9114-9124
    • (2011) Biochemistry , vol.50 , pp. 9114-9124
    • Xia, S.1    Wang, M.2    Blaha, G.3    Konigsberg, W.H.4    Wang, J.5
  • 39
    • 84879897415 scopus 로고    scopus 로고
    • Observing a DNA polymerase choose right from wrong
    • Freudenthal, B. D, Beard, W. A, Shock, D. D, and Wilson, S. H. (2013) Observing a DNA polymerase choose right from wrong. Cell 154, 157-168
    • (2013) Cell , vol.154 , pp. 157-168
    • Freudenthal, B.D.1    Beard, W.A.2    Shock, D.D.3    Wilson, S.H.4
  • 40
    • 70350508554 scopus 로고    scopus 로고
    • Global conformational dynamics of a Y-family DNA polymerase during catalysis
    • Xu, C, Maxwell, B. A., Brown, J. A., Zhang, L., and Suo, Z. (2009) Global conformational dynamics of a Y-family DNA polymerase during catalysis. PLoS Biol. 7, e1000225
    • (2009) PLoS Biol. , vol.7
    • Xu, C.1    Maxwell, B.A.2    Brown, J.A.3    Zhang, L.4    Suo, Z.5
  • 41
    • 0037310493 scopus 로고    scopus 로고
    • Damage repair DNA polymerases Y
    • Yang, W. (2003) Damage repair DNA polymerases Y. Curr. Opin. Struct. Biol. 13, 23-30
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 23-30
    • Yang, W.1
  • 42
    • 84873284245 scopus 로고    scopus 로고
    • Watching the bacteriophage N4 RNA polymerase transcription by time-dependent soak-trigger-freeze xray crystallography
    • Basu, R. S., and Murakami, K. S. (2013) Watching the bacteriophage N4 RNA polymerase transcription by time-dependent soak-trigger-freeze xray crystallography. J. Biol. Chem. 288, 3305-3311
    • (2013) J. Biol. Chem. , vol.288 , pp. 3305-3311
    • Basu, R.S.1    Murakami, K.S.2
  • 44
    • 23044492225 scopus 로고    scopus 로고
    • Motions of the fingers subdomain of Klentaq1 are fast and not rate limiting: Implications for the molecular basis of fidelity in DNA polymerases
    • Rothwell, P. J, Mitaksov, V, and Waksman, G. (2005) Motions of the fingers subdomain of Klentaq1 are fast and not rate limiting: implications for the molecular basis of fidelity in DNA polymerases. Mol. Cell 19, 345-355
    • (2005) Mol. Cell , vol.19 , pp. 345-355
    • Rothwell, P.J.1    Mitaksov, V.2    Waksman, G.3
  • 45
    • 8544278025 scopus 로고    scopus 로고
    • DNA polymerase fidelity: Kinetics, structure, and checkpoints
    • Joyce, C. M., and Benkovic, S. J. (2004) DNA polymerase fidelity: kinetics, structure, and checkpoints. Biochemistry 43, 14317-14324
    • (2004) Biochemistry , vol.43 , pp. 14317-14324
    • Joyce, C.M.1    Benkovic, S.J.2
  • 46
    • 84876534117 scopus 로고    scopus 로고
    • Single-molecule investigation of substrate binding kinetics and protein conformational dynamics of aB-family replicative DNA polymerase
    • Maxwell, B. A., and Suo, Z. (2013) Single-molecule investigation of substrate binding kinetics and protein conformational dynamics of aB-family replicative DNA polymerase. J. Biol. Chem. 288, 11590-11600
    • (2013) J. Biol. Chem. , vol.288 , pp. 11590-11600
    • Maxwell, B.A.1    Suo, Z.2
  • 47
    • 14844346283 scopus 로고    scopus 로고
    • Hinge residue Ile260 of DNA polymeraseβ is important for enzyme activity and fidelity
    • Starcevic, D., Dalal, S., and Sweasy, J. (2005) Hinge residue Ile260 of DNA polymeraseβ 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.3
  • 48
    • 0037144446 scopus 로고    scopus 로고
    • Threonine 79 is a hinge residue that governs the fidelity of DNA polymeraseβ by helping to position the DNA within the active site
    • Maitra, M., Gudzelak, A., Jr., Li, S. X., Matsumoto, Y., Eckert, K. A., Jager, J., and Sweasy, J. B. (2002) Threonine 79 is a hinge residue that governs the fidelity of DNA polymeraseβ by helping to position the DNA within the active site. J. Biol. Chem. 277, 35550-35560
    • (2002) J. Biol. Chem. , vol.277 , pp. 35550-35560
    • Maitra, M.1    Gudzelak Jr., A.2    Li, S.X.3    Matsumoto, Y.4    Eckert, K.A.5    Jager, J.6    Sweasy, J.B.7
  • 49
    • 34250626890 scopus 로고    scopus 로고
    • Loop II of DNA polymeraseβ is important for polymerization activity and fidelity
    • Lin, G. C, Jaeger, J., and Sweasy, J. B. (2007) Loop II of DNA polymeraseβ 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
  • 51
    • 58149170452 scopus 로고    scopus 로고
    • Loop II of DNA polymeraseβ is important for discrimination during substrate binding
    • Lin, G. C, Jaeger, J., Eckert, K. A., and Sweasy, J. B. (2009) Loop II of DNA polymeraseβ is important for discrimination during substrate binding. DNA Repair 8, 182-189
    • (2009) DNA Repair , vol.8 , pp. 182-189
    • Lin, G.C.1    Jaeger, J.2    Eckert, K.A.3    Sweasy, J.B.4
  • 52
    • 84879513246 scopus 로고    scopus 로고
    • Structural changes in the hydrophobic hinge region adversely affect the activity and fidelity of the I260Q mutator DNA polymeraseβ
    • Gridley, C. L, Rangarajan, S., Firbank, S., Dalal, S., Sweasy, J. B., and Jaeger, J. (2013) Structural changes in the hydrophobic hinge region adversely affect the activity and fidelity of the I260Q mutator DNA polymeraseβ. Biochemistry 52, 4422-4432
    • (2013) Biochemistry , vol.52 , pp. 4422-4432
    • Gridley, C.L.1    Rangarajan, S.2    Firbank, S.3    Dalal, S.4    Sweasy, J.B.5    Jaeger, J.6
  • 53
    • 23344450425 scopus 로고    scopus 로고
    • The hydrophobic hinge region of rat DNA polymeraseβ 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 polymeraseβ 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
  • 54
    • 35349009532 scopus 로고    scopus 로고
    • A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1
    • Rothwell, P. J., and Waksman, G. (2007) A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1. J. Biol. Chem. 282, 28884-28892
    • (2007) J. Biol. Chem. , vol.282 , pp. 28884-28892
    • Rothwell, P.J.1    Waksman, G.2
  • 55
    • 79952759975 scopus 로고    scopus 로고
    • 2+ ligands, Asp-882 and Asp-705, of DNA polymerase I (Klenow fragment) during the prechemistry conformational transitions
    • 2+ ligands, Asp-882 and Asp-705, of DNA polymerase I (Klenow fragment) during the prechemistry conformational transitions. J. Biol. Chem. 286, 3755-3766
    • (2011) J. Biol. Chem. , vol.286 , pp. 3755-3766
    • Bermek, O.1    Grindley, N.D.2    Joyce, C.M.3
  • 56
    • 0029836483 scopus 로고    scopus 로고
    • Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymeraseβ 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 polymeraseβ by x-ray structural analysis. Biochemistry 35, 12778-12787
    • (1996) Biochemistry , vol.35 , pp. 12778-12787
    • Pelletier, H.1    Sawaya, M.R.2
  • 57
    • 0032005866 scopus 로고    scopus 로고
    • Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes
    • Brautigam, C. A., and Steitz, T. A. (1998) Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr. Opin. Struct. Biol. 8, 54-63
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 54-63
    • Brautigam, C.A.1    Steitz, T.A.2
  • 58
    • 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
  • 59


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.