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Volumn 45, Issue 32, 2006, Pages 9675-9687

A new paradigm for DNA polymerase specificity

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; COMPLEXATION; CONFORMATIONS; DNA; REACTION KINETICS; SUBSTRATES;

EID: 33747462891     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060993z     Document Type: Article
Times cited : (220)

References (42)
  • 3
    • 0016232066 scopus 로고
    • Catalysis, binding and enzyme-substrate complementarity
    • Fersht, A. R. (1974) Catalysis, binding and enzyme-substrate complementarity, Proc. R. Soc. London, Ser. B 187, 397-407.
    • (1974) Proc. R. Soc. London, Ser. B , vol.187 , pp. 397-407
    • Fersht, A.R.1
  • 4
    • 0028839740 scopus 로고
    • Re-examination of induced fit as a determinant of substrate specificity in enzymatic reactions
    • Post, C. B., and Ray, W. J., Jr. (1995) Re-examination of induced fit as a determinant of substrate specificity in enzymatic reactions, Biochemistry 34, 15881-15885.
    • (1995) Biochemistry , vol.34 , pp. 15881-15885
    • Post, C.B.1    Ray Jr., W.J.2
  • 5
    • 0027220197 scopus 로고
    • Conformational coupling in DNA polymerase fidelity
    • Johnson, K. A. (1993) Conformational coupling in DNA polymerase fidelity, Annu. Rev. Biochem. 62, 685-713.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 685-713
    • Johnson, K.A.1
  • 6
    • 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
  • 8
    • 0030924437 scopus 로고    scopus 로고
    • Hydrogen bonding revisited: Geometric selection as a principal determinant of DNA replication fidelity
    • Goodman, M. F. (1997) Hydrogen bonding revisited: Geometric selection as a principal determinant of DNA replication fidelity, Proc. Natl. Acad. Sci. U.S.A. 94, 10493-10495.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 10493-10495
    • Goodman, M.F.1
  • 9
    • 0026033193 scopus 로고
    • Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant
    • Patel, S. S., Wong, I., and Johnson, K. A. (1991) Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant, Biochemistry 30, 511-525.
    • (1991) Biochemistry , vol.30 , pp. 511-525
    • Patel, S.S.1    Wong, I.2    Johnson, K.A.3
  • 10
    • 0026026192 scopus 로고
    • An induced-fit kinetic mechanism for DNA replication fidelily-Direct measurement by single-turnover kinetics
    • Wong, I., Patel, S. S., and Johnson, K. A. (1991) An induced-fit kinetic mechanism for DNA replication fidelily-Direct measurement by single-turnover kinetics, Biochemistry 30, 526-537.
    • (1991) Biochemistry , vol.30 , pp. 526-537
    • Wong, I.1    Patel, S.S.2    Johnson, K.A.3
  • 12
    • 0027092323 scopus 로고
    • Mechanism and fidelity of HIV reverse transcriptase
    • Kali, W. M., Johnson, K. A., Jerva, L. F., and Anderson, K. S. (1992) Mechanism and fidelity of HIV reverse transcriptase, J. Biol. Chem. 267, 25988-25997.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25988-25997
    • Kali, W.M.1    Johnson, K.A.2    Jerva, L.F.3    Anderson, K.S.4
  • 13
    • 0028925773 scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors
    • Spence, R. A., Kati, W. M., Anderson, K. S., and Johnson, K. A. (1995) Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors, Science 267, 988-993.
    • (1995) Science , vol.267 , pp. 988-993
    • Spence, R.A.1    Kati, W.M.2    Anderson, K.S.3    Johnson, K.A.4
  • 14
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublie, S., Tabor, S., Long, A. M., Richardson, C. C., and Ellenberger, T. (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution, Nature 391, 251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 15
    • 0028049441 scopus 로고
    • Structures 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, J. (1994) Structures 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, J.5
  • 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
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance
    • Huang, H. F., Chopra, R., Verdine, G. L., and Harrison, S. C. (1998) Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance, Science 282, 1669-1675.
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.F.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 18
    • 0035906661 scopus 로고    scopus 로고
    • Prokaryotic DNA polymerase 1: Evolution, structure, and "base flipping" mechanism for nucleotide selection
    • Patel, P. H., Suzuki, M., Adman, E., Shinkai, A., and Loeb, L. A. (2001) Prokaryotic DNA polymerase 1: Evolution, structure, and "base flipping" mechanism for nucleotide selection, J. Mol. Biol. 308, 823-837.
    • (2001) J. Mol. Biol. , vol.308 , pp. 823-837
    • Patel, P.H.1    Suzuki, M.2    Adman, E.3    Shinkai, A.4    Loeb, L.A.5
  • 19
    • 0037125947 scopus 로고    scopus 로고
    • Use of 2-aminopurine and tryptophan fluorescence as probes in kinetic analyses of DNA polymerase β
    • Dunlap, C. A., and Tsai, M. D. (2002) Use of 2-aminopurine and tryptophan fluorescence as probes in kinetic analyses of DNA polymerase β, Biochemistry 41, 11226-11235.
    • (2002) Biochemistry , vol.41 , pp. 11226-11235
    • Dunlap, C.A.1    Tsai, M.D.2
  • 20
    • 0037183526 scopus 로고    scopus 로고
    • A reexamination of the nucleotide incorporation fidelity of DNA polymerases
    • Showalter, A. K., and Tsai, M. D. (2002) A reexamination of the nucleotide incorporation fidelity of DNA polymerases, Biochemistry 41, 10571-10576.
    • (2002) Biochemistry , vol.41 , pp. 10571-10576
    • Showalter, A.K.1    Tsai, M.D.2
  • 21
    • 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
  • 22
    • 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. (1991) Ribozyme-catalyzed and nonenzymatic reactions of phosphate diesters: Rate effects upon substitution of sulfur for a nonbridging phosphoryl oxygen atom, Biochemistry 30, 4844-4854.
    • (1991) Biochemistry , vol.30 , pp. 4844-4854
    • Herschlag, D.1    Piccirilli, J.A.2    Cech, T.R.3
  • 24
    • 0041823551 scopus 로고    scopus 로고
    • Use of 2-aminopurine fluorescence to examine conformational changes during nucleotide incorporation by DNA polymerase 1 (Klenow fragment)
    • Purohit, V., Grindley, N. D. F., and Joyce, C. M. (2003) Use of 2-aminopurine fluorescence to examine conformational changes during nucleotide incorporation by DNA polymerase 1 (Klenow fragment), Biochemistry 42, 10200-10211.
    • (2003) Biochemistry , vol.42 , pp. 10200-10211
    • Purohit, V.1    Grindley, N.D.F.2    Joyce, C.M.3
  • 26
    • 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
  • 27
    • 0021256117 scopus 로고
    • Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12
    • Lunn, C. A., Kathju, S., Wallace, B. J., Kushner, S. R., and Pigiet, V. (1984) Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12, J. Biol. Chem. 259, 469-474.
    • (1984) J. Biol. Chem. , vol.259 , pp. 469-474
    • Lunn, C.A.1    Kathju, S.2    Wallace, B.J.3    Kushner, S.R.4    Pigiet, V.5
  • 28
    • 33747499914 scopus 로고    scopus 로고
    • Site-specific labeling of T7 DNA polymerase with a conformationally sensitive fluorophore
    • manuscript in preparation
    • Tsai, Y.-C., Jin, Z., and Johnson, K. A. (2006) Site-specific labeling of T7 DNA polymerase with a conformationally sensitive fluorophore, J. Biol. Chem., manuscript in preparation.
    • (2006) J. Biol. Chem.
    • Tsai, Y.-C.1    Jin, Z.2    Johnson, K.A.3
  • 29
    • 20444441145 scopus 로고    scopus 로고
    • Discrimination of single-nucleotide alterations by G-specific fluorescence quenching
    • Dohno, C., and Saito, I. (2005) Discrimination of single-nucleotide alterations by G-specific fluorescence quenching, ChemBioChem 6, 1075-1081.
    • (2005) ChemBioChem , vol.6 , pp. 1075-1081
    • Dohno, C.1    Saito, I.2
  • 30
    • 18744402486 scopus 로고    scopus 로고
    • Computer simulations of protein functions: Searching for the molecular origin of the replication fidelity of DNA polymerases
    • Florian, J., Goodman, M. F., and Warshel, A. (2005) Computer simulations of protein functions: Searching for the molecular origin of the replication fidelity of DNA polymerases, Proc. Natl. Acad. Sci. U.S.A. 102, 6819-6824.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 6819-6824
    • Florian, J.1    Goodman, M.F.2    Warshel, A.3
  • 31
    • 33644617062 scopus 로고    scopus 로고
    • Mechanistic comparison of high-fidelity and error-prone DNA polymerases and ligases involved in DNA repair
    • Showalter, A. K., Lamarche, B. J., Bakhtina, M., Su, M. I., Tang, K. H., and Tsai, M. D. (2006) Mechanistic comparison of high-fidelity and error-prone DNA polymerases and ligases involved in DNA repair, Chem. Rev. 106, 340-360.
    • (2006) Chem. Rev. , vol.106 , pp. 340-360
    • Showalter, A.K.1    Lamarche, B.J.2    Bakhtina, M.3    Su, M.I.4    Tang, K.H.5    Tsai, M.D.6
  • 32
    • 0346995096 scopus 로고    scopus 로고
    • Toxicity of nucleoside analogues used to treat AIDS and the selectivity of the mitochondrial DNA polymerase
    • Lee, H., Hanes, J., and Johnson, K. A. (2003) Toxicity of nucleoside analogues used to treat AIDS and the selectivity of the mitochondrial DNA polymerase, Biochemistry 42, 14711-14719.
    • (2003) Biochemistry , vol.42 , pp. 14711-14719
    • Lee, H.1    Hanes, J.2    Johnson, K.A.3
  • 33
    • 0028916224 scopus 로고
    • Rapid quench kinetic analysis of polymerases, adenosine triphosphatases, and enzyme intermediates
    • Johnson, K. A. (1995) Rapid quench kinetic analysis of polymerases, adenosine triphosphatases, and enzyme intermediates, Methods Enzymol. 249, 38-61.
    • (1995) Methods Enzymol. , vol.249 , pp. 38-61
    • Johnson, K.A.1
  • 34
    • 0642315208 scopus 로고
    • Transient-slate kinetic analysis of enzyme reaction pathways
    • Academic Press, Inc., New York
    • Johnson, K. A. (1992) Transient-slate kinetic analysis of enzyme reaction pathways, in The Enzymes, pp 1-61, Academic Press, Inc., New York.
    • (1992) The Enzymes , pp. 1-61
    • Johnson, K.A.1
  • 35
    • 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
  • 36
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz, T. A., and Steitz, J. A. (1993) A general two-metal-ion mechanism for catalytic RNA, Proc. Natl. Acad. Sci. U.S.A. 90, 6498-6502.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 37
    • 0002724139 scopus 로고
    • The role of induced fit and conformational changes of enzymes in specificity and catalysis
    • Herschlag, D. (1988) The role of induced fit and conformational changes of enzymes in specificity and catalysis, Bioorg. Chem. 16, 62-96.
    • (1988) Bioorg. Chem. , vol.16 , pp. 62-96
    • Herschlag, D.1
  • 38
    • 1642588255 scopus 로고    scopus 로고
    • Structures of mismatch replication errors observed in a DNA polymerase
    • Johnson, S. J., and Beese, L. S. (2004) Structures of mismatch replication errors observed in a DNA polymerase, Cell 116, 803-816.
    • (2004) Cell , vol.116 , pp. 803-816
    • Johnson, S.J.1    Beese, L.S.2
  • 39
    • 4644258145 scopus 로고    scopus 로고
    • Structural insights into DNA polymerase β deterrents for misincorporation support an induced-fit mechanism for fidelity
    • Krahn, J. M., Beard, W. A., and Wilson, S. H. (2004) Structural insights into DNA polymerase β deterrents for misincorporation support an induced-fit mechanism for fidelity, Structure 12, 1823-1832.
    • (2004) Structure , vol.12 , pp. 1823-1832
    • Krahn, J.M.1    Beard, W.A.2    Wilson, S.H.3
  • 40
    • 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
  • 41
    • 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
  • 42
    • 0141448966 scopus 로고    scopus 로고
    • Thermodynamic and extrathermodynamic requirements of enzyme catalysis
    • Wolfenden, R. (2003) Thermodynamic and extrathermodynamic requirements of enzyme catalysis, Biophys. Chem. 105, 559-572.
    • (2003) Biophys. Chem. , vol.105 , pp. 559-572
    • Wolfenden, R.1


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