메뉴 건너뛰기




Volumn 47, Issue 33, 2008, Pages 8614-8622

Uracil DNA glycosylase: Revisiting substrate-assisted catalysis by DNA phosphate anions

Author keywords

[No Author keywords available]

Indexed keywords

DNA; FOOD ADDITIVES; GENES; NUCLEIC ACIDS;

EID: 49749106226     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800854g     Document Type: Article
Times cited : (26)

References (28)
  • 1
    • 33748632358 scopus 로고    scopus 로고
    • Probing Enzyme Phosphoester Interactions by Combining Mutagenesis and Chemical Modification of Phosphate Ester Oxygens
    • Stivers, J. T., and Nagarajan, R. (2006) Probing Enzyme Phosphoester Interactions by Combining Mutagenesis and Chemical Modification of Phosphate Ester Oxygens. Chem. Rev. 106, 3443-3467.
    • (2006) Chem. Rev , vol.106 , pp. 3443-3467
    • Stivers, J.T.1    Nagarajan, R.2
  • 2
    • 0345270445 scopus 로고    scopus 로고
    • Powering DNA Repair through Substrate Electrostatic Interactions
    • Jiang, Y. L., Ichikawa, Y., Song, F., and Stivers, J. T. (2003) Powering DNA Repair through Substrate Electrostatic Interactions. Biochemistry 42, 1922-1929.
    • (2003) Biochemistry , vol.42 , pp. 1922-1929
    • Jiang, Y.L.1    Ichikawa, Y.2    Song, F.3    Stivers, J.T.4
  • 3
    • 0037013320 scopus 로고    scopus 로고
    • Probing the Limits of Electrostatic Catalysis by Uracil DNA Glycosylase using Transition-State Mimicry and Mutagenesis
    • Jiang, Y. L., Drohat, A. C., Ichikawa, Y., and Stivers, J. T. (2002) Probing the Limits of Electrostatic Catalysis by Uracil DNA Glycosylase using Transition-State Mimicry and Mutagenesis. J. Biol. Chem. 277, 15385-15392.
    • (2002) J. Biol. Chem , vol.277 , pp. 15385-15392
    • Jiang, Y.L.1    Drohat, A.C.2    Ichikawa, Y.3    Stivers, J.T.4
  • 4
    • 0035954406 scopus 로고    scopus 로고
    • Reconstructing the Substrate for Uracil DNA Glycosylase: Tracking the Transmission of Binding Energy in Catalysis
    • Jiang, Y. L., and Stivers, J. T. (2001) Reconstructing the Substrate for Uracil DNA Glycosylase: Tracking the Transmission of Binding Energy in Catalysis. Biochemistry 40, 7710-7719.
    • (2001) Biochemistry , vol.40 , pp. 7710-7719
    • Jiang, Y.L.1    Stivers, J.T.2
  • 5
    • 0035909316 scopus 로고    scopus 로고
    • Uracil-DNA Glycosylase Acts by Substrate Autocatalysis
    • Dinner, A. R., Blackburn, G. M., and Karplus, M. (2001) Uracil-DNA Glycosylase Acts by Substrate Autocatalysis. Nature 413, 752-755.
    • (2001) Nature , vol.413 , pp. 752-755
    • Dinner, A.R.1    Blackburn, G.M.2    Karplus, M.3
  • 6
    • 33751236524 scopus 로고    scopus 로고
    • Implications of Alternative Substrate Binding Modes for Catalysis by Uracil-DNA Glycosylase: An Apparent Discrepancy Resolved
    • Ma, A., Hu, J., Karplus, M., and Dinner, A. R. (2006) Implications of Alternative Substrate Binding Modes for Catalysis by Uracil-DNA Glycosylase: An Apparent Discrepancy Resolved. Biochemistry 45, 13687-13696.
    • (2006) Biochemistry , vol.45 , pp. 13687-13696
    • Ma, A.1    Hu, J.2    Karplus, M.3    Dinner, A.R.4
  • 7
    • 33748633480 scopus 로고    scopus 로고
    • Warshel, A., Sharma, P. K., Kato, M., Xiang, Y., Liu, H., and Olsson, M. H. (2006) Electrostatic Basis for Enzyme Catalysis. Chem. Rev. 106, 3210-3235.
    • Warshel, A., Sharma, P. K., Kato, M., Xiang, Y., Liu, H., and Olsson, M. H. (2006) Electrostatic Basis for Enzyme Catalysis. Chem. Rev. 106, 3210-3235.
  • 9
    • 0025732374 scopus 로고
    • Specificities and Kinetics of Uracil Excision from Uracil-Containing DNA Oligomers by Escherichia coli Uracil DNA Glycosylase
    • Varshney, U., and van de Sande, J. H. (1991) Specificities and Kinetics of Uracil Excision from Uracil-Containing DNA Oligomers by Escherichia coli Uracil DNA Glycosylase. Biochemistry 30, 4055-4061.
    • (1991) Biochemistry , vol.30 , pp. 4055-4061
    • Varshney, U.1    van de Sande, J.H.2
  • 10
    • 0028934537 scopus 로고
    • Crystal Structure and Mutational Analysis of Human Uracil-DNA Glycosylase: Structural Basis for Specificity and Catalysis
    • Mol, C. D., Arvai, A. S., Slupphaug, G., Kavli, B., Alseth, I., Krokan, H. E., and Tainer, J. A. (1995) Crystal Structure and Mutational Analysis of Human Uracil-DNA Glycosylase: Structural Basis for Specificity and Catalysis. Cell 80, 869-878.
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 11
    • 0033554424 scopus 로고    scopus 로고
    • Role of Electrophilic and General Base Catalysis in the Mechanism of Escherichia coli Uracil DNA Glycosylase
    • Drohat, A. C., Jagadeesh, J., Ferguson, E., and Stivers, J. T. (1999) Role of Electrophilic and General Base Catalysis in the Mechanism of Escherichia coli Uracil DNA Glycosylase. Biochemistry 38, 11866-11875.
    • (1999) Biochemistry , vol.38 , pp. 11866-11875
    • Drohat, A.C.1    Jagadeesh, J.2    Ferguson, E.3    Stivers, J.T.4
  • 12
  • 13
    • 0033554395 scopus 로고    scopus 로고
    • Hetronuclear NMR and Crystallographic Studies of Wild-Type and H187Q Escherichia coli Uracil DNA Glycosylase: Electrophilic Catalysis of Uracil Expulsion by a Neutral Histidine 187
    • Drohat, A. C., Xiao, G., Tordova, M., Jagadeesh, J., Pankiewicz, K. W., Watanabe, K. A., Gilliland, G. L., and Stivers, J. T. (1999) Hetronuclear NMR and Crystallographic Studies of Wild-Type and H187Q Escherichia coli Uracil DNA Glycosylase: Electrophilic Catalysis of Uracil Expulsion by a Neutral Histidine 187. Biochemistry 38, 11876-11886.
    • (1999) Biochemistry , vol.38 , pp. 11876-11886
    • Drohat, A.C.1    Xiao, G.2    Tordova, M.3    Jagadeesh, J.4    Pankiewicz, K.W.5    Watanabe, K.A.6    Gilliland, G.L.7    Stivers, J.T.8
  • 14
    • 0037018940 scopus 로고    scopus 로고
    • Inhibition of Uracil DNA Glycosylase by an Oxacarbenium Ion Mimic
    • Jiang, Y. L., Ichikawa, Y., and Stivers, J. T. (2002) Inhibition of Uracil DNA Glycosylase by an Oxacarbenium Ion Mimic. Biochemistry 41, 7116-7124.
    • (2002) Biochemistry , vol.41 , pp. 7116-7124
    • Jiang, Y.L.1    Ichikawa, Y.2    Stivers, J.T.3
  • 15
    • 0032529485 scopus 로고    scopus 로고
    • 2-Aminopurine Fluorescence Studies of Base Stacking Interactions at Abasic Sites in DNA: Metal-Ion and Base Sequence Effects
    • Stivers, J. T. (1998) 2-Aminopurine Fluorescence Studies of Base Stacking Interactions at Abasic Sites in DNA: Metal-Ion and Base Sequence Effects. Nucleic Acids Res. 26, 3837-3844.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3837-3844
    • Stivers, J.T.1
  • 16
    • 0034601807 scopus 로고    scopus 로고
    • Escherichia coli Uracil DNA Glycosylase: NMR Characterization of the Short Hydrogen Bond from His187 to Uracil O2
    • Drohat, A. C., and Stivers, J. T. (2000) Escherichia coli Uracil DNA Glycosylase: NMR Characterization of the Short Hydrogen Bond from His187 to Uracil O2. Biochemistry 39, 11865-11875.
    • (2000) Biochemistry , vol.39 , pp. 11865-11875
    • Drohat, A.C.1    Stivers, J.T.2
  • 17
    • 0027456412 scopus 로고
    • Tautomeric States of the Active-Site Histidines of Phosphorylated and Unphosphorylated IIIGlc, a Signal-Transducing Protein from Escherichia coli, using Two-Dimensional Heteronuclear NMR Techniques
    • Pelton, J. G., Torchia, D. A., Meadow, N. D., and Roseman, S. (1993) Tautomeric States of the Active-Site Histidines of Phosphorylated and Unphosphorylated IIIGlc, a Signal-Transducing Protein from Escherichia coli, using Two-Dimensional Heteronuclear NMR Techniques. Protein Sci. 2, 543-558.
    • (1993) Protein Sci , vol.2 , pp. 543-558
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Roseman, S.4
  • 18
    • 0029400480 scopus 로고
    • NMRPipe: A Multidimensional Spectral Processing System Based on UNIX Pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A Multidimensional Spectral Processing System Based on UNIX Pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 19
    • 0032511418 scopus 로고    scopus 로고
    • Conformational Flexibility of Phosphate, Phosphonate, and Phosphorothioate Methyl Esters in Aqueous Solution
    • Florian, J., Strajbl, M., and Warshel, A. (1998) Conformational Flexibility of Phosphate, Phosphonate, and Phosphorothioate Methyl Esters in Aqueous Solution. J. Am. Chem. Soc. 120, 7959-7966.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 7959-7966
    • Florian, J.1    Strajbl, M.2    Warshel, A.3
  • 20
    • 0003932766 scopus 로고    scopus 로고
    • W. H. Freeman and Co, New York
    • Creighton, T. E. (1997) Proteins, W. H. Freeman and Co., New York.
    • (1997) Proteins
    • Creighton, T.E.1
  • 22
    • 1242340307 scopus 로고    scopus 로고
    • Effect of Phosphorothioate Chirality on the Grooves of DNA Double Helices: A Molecular Dynamics Study
    • Mukherjee, S., and Bhattacharyya, D. (2004) Effect of Phosphorothioate Chirality on the Grooves of DNA Double Helices: A Molecular Dynamics Study. Biopolymers 73, 269-282.
    • (2004) Biopolymers , vol.73 , pp. 269-282
    • Mukherjee, S.1    Bhattacharyya, D.2
  • 23
    • 0242286685 scopus 로고    scopus 로고
    • Electrostatic Guidance of Glycosyl Cation Migration Along the Reaction Coordinate of Uracil DNA Glycosylase
    • Bianchet, M. A., Seiple, L. A., Jiang, Y. L., Ichikawa, Y., Amzel, L. M., and Stivers, J. T. (2003) Electrostatic Guidance of Glycosyl Cation Migration Along the Reaction Coordinate of Uracil DNA Glycosylase. Biochemistry 42, 12455-12460.
    • (2003) Biochemistry , vol.42 , pp. 12455-12460
    • Bianchet, M.A.1    Seiple, L.A.2    Jiang, Y.L.3    Ichikawa, Y.4    Amzel, L.M.5    Stivers, J.T.6
  • 24
    • 0034625082 scopus 로고    scopus 로고
    • Uracil-DNA Glycosylase-DNA Substrate and Product Structures: Conformational Strain Promotes Catalytic Efficiency by Coupled Stereoelectronic Effects
    • Parikh, S. S., Walcher, G., Jones, G. D., Slupphaug, G., Krokan, H. E., Blackburn, G. M., and Tainer, J. A. (2000) Uracil-DNA Glycosylase-DNA Substrate and Product Structures: Conformational Strain Promotes Catalytic Efficiency by Coupled Stereoelectronic Effects. Proc. Natl. Acad. Sci. U.S.A. 97, 5083-5088.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 5083-5088
    • Parikh, S.S.1    Walcher, G.2    Jones, G.D.3    Slupphaug, G.4    Krokan, H.E.5    Blackburn, G.M.6    Tainer, J.A.7
  • 25
    • 0033554424 scopus 로고    scopus 로고
    • The Role of Electrophilic and Base Catalysis in the Mechanism of Escherichia coli Uracil DNA Glycosylase
    • Drohat, A. C., Jagadeesh, J., Ferguson, E., and Stivers, J. T. (1999) The Role of Electrophilic and Base Catalysis in the Mechanism of Escherichia coli Uracil DNA Glycosylase. Biochemistry 38, 11866-11875.
    • (1999) Biochemistry , vol.38 , pp. 11866-11875
    • Drohat, A.C.1    Jagadeesh, J.2    Ferguson, E.3    Stivers, J.T.4
  • 26
    • 34848899274 scopus 로고    scopus 로고
    • Enzymatic Capture of an Extrahelical Thymine in the Search for Uracil in DNA
    • Parker, J. B., Bianchet, M. A., Krosky, D. J., Friedman, J. I., Amzel, L. M., and Stivers, J. T. (2007) Enzymatic Capture of an Extrahelical Thymine in the Search for Uracil in DNA. Nature 449, 433-438.
    • (2007) Nature , vol.449 , pp. 433-438
    • Parker, J.B.1    Bianchet, M.A.2    Krosky, D.J.3    Friedman, J.I.4    Amzel, L.M.5    Stivers, J.T.6
  • 27
    • 0030451496 scopus 로고    scopus 로고
    • Structures of Active Site Histidine Mutants of IIIGlc, a Major Signal-Transducing Protein in Escherichia coli: Effects on the Mechanism of Regulation and Phosphoryl Transfer
    • Pelton, J. G., Torchia, D. A., Remington, S. J., Murphy, K. P., Meadow, N. D., and Roseman, S. (1996) Structures of Active Site Histidine Mutants of IIIGlc, a Major Signal-Transducing Protein in Escherichia coli: Effects on the Mechanism of Regulation and Phosphoryl Transfer. J. Biol. Chem. 271, 33446-33456.
    • (1996) J. Biol. Chem , vol.271 , pp. 33446-33456
    • Pelton, J.G.1    Torchia, D.A.2    Remington, S.J.3    Murphy, K.P.4    Meadow, N.D.5    Roseman, S.6
  • 28
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the Analysis of Enzyme Kinetic Data: Application to HIV Proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the Analysis of Enzyme Kinetic Data: Application to HIV Proteinase. Anal. Biochem. 237, 260-273.
    • (1996) Anal. Biochem , vol.237 , pp. 260-273
    • Kuzmic, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.