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Volumn 6, Issue 2, 2007, Pages 213-223

A unique error signature for human DNA polymerase ν

Author keywords

Base substitutions; Error prone polymerase; Infidelity

Indexed keywords

BETA GALACTOSIDASE; DNA; DNA DIRECTED DNA POLYMERASE GAMMA; DNA POLYMERASE; DNA POLYMERASE NU; M13MP2 DNA; THYMIDINE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 33846246423     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2006.09.012     Document Type: Article
Times cited : (42)

References (74)
  • 1
  • 5
    • 0035914329 scopus 로고    scopus 로고
    • The fidelity of human DNA polymerase gamma with and without exonucleolytic proofreading and the p55 accessory subunit
    • Longley M.J., Nguyen D., Kunkel T.A., and Copeland W.C. The fidelity of human DNA polymerase gamma with and without exonucleolytic proofreading and the p55 accessory subunit. J. Biol. Chem. 276 (2001) 38555-38562
    • (2001) J. Biol. Chem. , vol.276 , pp. 38555-38562
    • Longley, M.J.1    Nguyen, D.2    Kunkel, T.A.3    Copeland, W.C.4
  • 6
    • 0025160871 scopus 로고
    • The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I
    • Bebenek K., Joyce C.M., Fitzgerald M.P., and Kunkel T.A. The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. J. Biol. Chem. 265 (1990) 13878-13887
    • (1990) J. Biol. Chem. , vol.265 , pp. 13878-13887
    • Bebenek, K.1    Joyce, C.M.2    Fitzgerald, M.P.3    Kunkel, T.A.4
  • 7
    • 0026029379 scopus 로고
    • A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity
    • Carroll S.S., Cowart M., and Benkovic S.J. A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity. Biochemistry 30 (1991) 804-813
    • (1991) Biochemistry , vol.30 , pp. 804-813
    • Carroll, S.S.1    Cowart, M.2    Benkovic, S.J.3
  • 8
    • 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
  • 9
    • 33644864228 scopus 로고    scopus 로고
    • Functional evidence for a small and rigid active site in a high fidelity DNA polymerase: probing T7 DNA polymerase with variably sized base pairs
    • Kim T.W., Brieba L.G., Ellenberger T., and Kool E.T. Functional evidence for a small and rigid active site in a high fidelity DNA polymerase: probing T7 DNA polymerase with variably sized base pairs. J. Biol. Chem. 281 (2006) 2289-2295
    • (2006) J. Biol. Chem. , vol.281 , pp. 2289-2295
    • Kim, T.W.1    Brieba, L.G.2    Ellenberger, T.3    Kool, E.T.4
  • 10
    • 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. Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. Biochemistry 30 (1991) 511-525
    • (1991) Biochemistry , vol.30 , pp. 511-525
    • Patel, S.S.1    Wong, I.2    Johnson, K.A.3
  • 11
    • 0026026192 scopus 로고
    • An induced-fit kinetic mechanism for DNA replication fidelity: direct measurement by single-turnover kinetics
    • Wong I., Patel S.S., and Johnson K.A. An induced-fit kinetic mechanism for DNA replication fidelity: direct measurement by single-turnover kinetics. Biochemistry 30 (1991) 526-537
    • (1991) Biochemistry , vol.30 , pp. 526-537
    • Wong, I.1    Patel, S.S.2    Johnson, K.A.3
  • 12
    • 27644567193 scopus 로고    scopus 로고
    • Probing the active site tightness of DNA polymerase in subangstrom increments
    • Kim T.W., Delaney J.C., Essigmann J.M., and Kool E.T. Probing the active site tightness of DNA polymerase in subangstrom increments. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 15803-15808
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15803-15808
    • Kim, T.W.1    Delaney, J.C.2    Essigmann, J.M.3    Kool, E.T.4
  • 13
    • 0024282746 scopus 로고
    • Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase
    • Tindall K.R., and Kunkel T.A. Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase. Biochemistry 27 (1988) 6008-6013
    • (1988) Biochemistry , vol.27 , pp. 6008-6013
    • Tindall, K.R.1    Kunkel, T.A.2
  • 14
    • 0025315366 scopus 로고
    • High fidelity DNA synthesis by the Thermus aquaticus DNA polymerase
    • Eckert K.A., and Kunkel T.A. High fidelity DNA synthesis by the Thermus aquaticus DNA polymerase. Nucleic Acids Res. 18 (1990) 3739-3744
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3739-3744
    • Eckert, K.A.1    Kunkel, T.A.2
  • 15
    • 0035019856 scopus 로고    scopus 로고
    • Crystal structures of a ddATP-, ddTTP-, ddCTP, and ddGTP-trapped ternary complex of Klentaq1: insights into nucleotide incorporation and selectivity
    • Li Y., and Waksman G. Crystal structures of a ddATP-, ddTTP-, ddCTP, and ddGTP-trapped ternary complex of Klentaq1: insights into nucleotide incorporation and selectivity. Protein Sci. 10 (2001) 1225-1233
    • (2001) Protein Sci. , vol.10 , pp. 1225-1233
    • Li, Y.1    Waksman, G.2
  • 16
    • 0035906661 scopus 로고    scopus 로고
    • Prokaryotic DNA polymerase I: evolution, structure, and "base flipping" mechanism for nucleotide selection
    • Patel P.H., Suzuki M., Adman E., Shinkai A., and Loeb L.A. Prokaryotic DNA polymerase I: evolution, structure, and "base flipping" mechanism for nucleotide selection. J. Mol. Biol. 308 (2001) 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
  • 17
  • 18
    • 1642588255 scopus 로고    scopus 로고
    • Structures of mismatch replication errors observed in a DNA polymerase
    • Johnson S.J., and Beese L.S. Structures of mismatch replication errors observed in a DNA polymerase. Cell 116 (2004) 803-816
    • (2004) Cell , vol.116 , pp. 803-816
    • Johnson, S.J.1    Beese, L.S.2
  • 19
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
    • Ollis D.L., Brick P., Hamlin R., Xuong N.G., and Steitz T.A. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature 313 (1985) 762-766
    • (1985) Nature , vol.313 , pp. 762-766
    • Ollis, D.L.1    Brick, P.2    Hamlin, R.3    Xuong, N.G.4    Steitz, T.A.5
  • 20
    • 0027730441 scopus 로고
    • Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate
    • Beese L.S., Friedman J.M., and Steitz T.A. Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate. Biochemistry 32 (1993) 14095-14101
    • (1993) Biochemistry , vol.32 , pp. 14095-14101
    • Beese, L.S.1    Friedman, J.M.2    Steitz, T.A.3
  • 21
    • 0027231782 scopus 로고
    • Structure of DNA polymerase I Klenow fragment bound to duplex DNA
    • Beese L.S., Derbyshire V., and Steitz T.A. Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Science 260 (1993) 352-355
    • (1993) Science , vol.260 , pp. 352-355
    • Beese, L.S.1    Derbyshire, V.2    Steitz, T.A.3
  • 22
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • Doublie S., Tabor S., Long A.M., Richardson C.C., and Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution. Nature 391 (1998) 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
  • 23
  • 24
    • 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. 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 (1998) 7514-7525
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 26
    • 0025783442 scopus 로고
    • Fidelity mechanisms in DNA replication
    • Echols H., and Goodman M.F. Fidelity mechanisms in DNA replication. Annu. Rev. Biochem. 60 (1991) 477-511
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 477-511
    • Echols, H.1    Goodman, M.F.2
  • 28
    • 0035997351 scopus 로고    scopus 로고
    • Active site tightness and substrate fit in DNA replication
    • Kool E.T. Active site tightness and substrate fit in DNA replication. Annu. Rev. Biochem. 71 (2002) 191-219
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 191-219
    • Kool, E.T.1
  • 29
    • 26844566830 scopus 로고    scopus 로고
    • Structure and mechanism of DNA polymerases
    • Rothwell P.J., and Waksman G. Structure and mechanism of DNA polymerases. Adv. Protein Chem. 71 (2005) 401-440
    • (2005) Adv. Protein Chem. , vol.71 , pp. 401-440
    • Rothwell, P.J.1    Waksman, G.2
  • 30
    • 0027220197 scopus 로고
    • Conformational coupling in DNA polymerase fidelity
    • Johnson K.A. Conformational coupling in DNA polymerase fidelity. Annu. Rev. Biochem. 62 (1993) 685-713
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 685-713
    • Johnson, K.A.1
  • 31
    • 0033166143 scopus 로고    scopus 로고
    • Cloning and chromosomal mapping of the human DNA polymerase theta (POLQ), the eighth human DNA polymerase
    • Sharief F.S., Vojta P.J., Ropp P.A., and Copeland W.C. Cloning and chromosomal mapping of the human DNA polymerase theta (POLQ), the eighth human DNA polymerase. Genomics 59 (1999) 90-96
    • (1999) Genomics , vol.59 , pp. 90-96
    • Sharief, F.S.1    Vojta, P.J.2    Ropp, P.A.3    Copeland, W.C.4
  • 32
    • 0344011127 scopus 로고    scopus 로고
    • POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells
    • Seki M., Marini F., and Wood R.D. POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res. 31 (2003) 6117-6126
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6117-6126
    • Seki, M.1    Marini, F.2    Wood, R.D.3
  • 34
    • 0042357095 scopus 로고    scopus 로고
    • POLN, a nuclear PolA family DNA polymerase homologous to the DNA cross-link sensitivity protein Mus308
    • Marini F., Kim N., Schuffert A., and Wood R.D. POLN, a nuclear PolA family DNA polymerase homologous to the DNA cross-link sensitivity protein Mus308. J. Biol. Chem. 278 (2003) 32014-32019
    • (2003) J. Biol. Chem. , vol.278 , pp. 32014-32019
    • Marini, F.1    Kim, N.2    Schuffert, A.3    Wood, R.D.4
  • 35
    • 33747666822 scopus 로고    scopus 로고
    • Human DNA polymerase N (POLN) is a low fidelity enzyme capable of error-free bypass of 5S-thymine glycol
    • Takata K.-I., Shimizu T., Iwai S., and Wood R.D. Human DNA polymerase N (POLN) is a low fidelity enzyme capable of error-free bypass of 5S-thymine glycol. J. Biol. Chem. 281 (2006) 23445-23455
    • (2006) J. Biol. Chem. , vol.281 , pp. 23445-23455
    • Takata, K.-I.1    Shimizu, T.2    Iwai, S.3    Wood, R.D.4
  • 36
    • 0027215749 scopus 로고
    • Mechanism of HIV-1 reverse transcriptase. Termination of processive synthesis on a natural DNA template is influenced by the sequence of the template-primer stem
    • Abbotts J., Bebenek K., Kunkel T.A., and Wilson S.H. Mechanism of HIV-1 reverse transcriptase. Termination of processive synthesis on a natural DNA template is influenced by the sequence of the template-primer stem. J. Biol. Chem. 268 (1993) 10312-10323
    • (1993) J. Biol. Chem. , vol.268 , pp. 10312-10323
    • Abbotts, J.1    Bebenek, K.2    Kunkel, T.A.3    Wilson, S.H.4
  • 37
    • 0028857175 scopus 로고
    • Analyzing fidelity of DNA polymerases
    • Bebenek K., and Kunkel T.A. Analyzing fidelity of DNA polymerases. Methods Enzymol. 262 (1995) 217-232
    • (1995) Methods Enzymol. , vol.262 , pp. 217-232
    • Bebenek, K.1    Kunkel, T.A.2
  • 38
    • 0347379857 scopus 로고    scopus 로고
    • The efficiency and specificity of apurinic/apyrimidinic site bypass by human DNA polymerase eta and Sulfolobus solfataricus Dpo4
    • Kokoska R.J., McCulloch S.D., and Kunkel T.A. The efficiency and specificity of apurinic/apyrimidinic site bypass by human DNA polymerase eta and Sulfolobus solfataricus Dpo4. J. Biol. Chem. 278 (2003) 50537-50545
    • (2003) J. Biol. Chem. , vol.278 , pp. 50537-50545
    • Kokoska, R.J.1    McCulloch, S.D.2    Kunkel, T.A.3
  • 40
    • 23844522523 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae DNA polymerase delta: high fidelity for base substitutions but lower fidelity for single- and multi-base deletions
    • Fortune J.M., Pavlov Y.I., Welch C.M., Johansson E., Burgers P.M., and Kunkel T.A. Saccharomyces cerevisiae DNA polymerase delta: high fidelity for base substitutions but lower fidelity for single- and multi-base deletions. J. Biol. Chem. 280 (2005) 29980-29987
    • (2005) J. Biol. Chem. , vol.280 , pp. 29980-29987
    • Fortune, J.M.1    Pavlov, Y.I.2    Welch, C.M.3    Johansson, E.4    Burgers, P.M.5    Kunkel, T.A.6
  • 41
    • 33749996082 scopus 로고    scopus 로고
    • RPA and PCNA suppress formation of large deletion errors by yeast DNA polymerase {delta}
    • Fortune J.M., Stith C.M., Kissling G.E., Burgers P.M.J., and Kunkel T.A. RPA and PCNA suppress formation of large deletion errors by yeast DNA polymerase {delta}. Nucl. Acids Res. 34 (2006) 4335-4341
    • (2006) Nucl. Acids Res. , vol.34 , pp. 4335-4341
    • Fortune, J.M.1    Stith, C.M.2    Kissling, G.E.3    Burgers, P.M.J.4    Kunkel, T.A.5
  • 42
    • 0023790391 scopus 로고
    • Mutagenesis by transient misalignment
    • Kunkel T.A., and Soni A. Mutagenesis by transient misalignment. J. Biol. Chem. 263 (1988) 14784-14789
    • (1988) J. Biol. Chem. , vol.263 , pp. 14784-14789
    • Kunkel, T.A.1    Soni, A.2
  • 43
    • 31044450194 scopus 로고    scopus 로고
    • Structural analysis of strand misalignment during DNA synthesis by a human DNA polymerase
    • Garcia-Diaz M., Bebenek K., Krahn J.M., Pedersen L.C., and Kunkel T.A. Structural analysis of strand misalignment during DNA synthesis by a human DNA polymerase. Cell 124 (2006) 331-342
    • (2006) Cell , vol.124 , pp. 331-342
    • Garcia-Diaz, M.1    Bebenek, K.2    Krahn, J.M.3    Pedersen, L.C.4    Kunkel, T.A.5
  • 44
    • 0013997442 scopus 로고
    • Frameshift mutations and the genetic code. This paper is dedicated to Professor Theodosius Dobzhansky on the occasion of his 66th birthday
    • Streisinger G., Okada Y., Emrich J., Newton J., Tsugita A., Terzaghi E., and Inouye M. Frameshift mutations and the genetic code. This paper is dedicated to Professor Theodosius Dobzhansky on the occasion of his 66th birthday. Cold Spring Harb. Symp. Quant. Biol. 31 (1966) 77-84
    • (1966) Cold Spring Harb. Symp. Quant. Biol. , vol.31 , pp. 77-84
    • Streisinger, G.1    Okada, Y.2    Emrich, J.3    Newton, J.4    Tsugita, A.5    Terzaghi, E.6    Inouye, M.7
  • 45
    • 0027491535 scopus 로고
    • Effect of reaction pH on the fidelity and processivity of exonuclease-deficient Klenow polymerase
    • Eckert K.A., and Kunkel T.A. Effect of reaction pH on the fidelity and processivity of exonuclease-deficient Klenow polymerase. J Biol Chem 268 (1993) 13462-13471
    • (1993) J Biol Chem , vol.268 , pp. 13462-13471
    • Eckert, K.A.1    Kunkel, T.A.2
  • 46
    • 19444383801 scopus 로고    scopus 로고
    • Trading places: how do DNA polymerases switch during translesion DNA synthesis?
    • Friedberg E.C., Lehmann A.R., and Fuchs R.P. Trading places: how do DNA polymerases switch during translesion DNA synthesis?. Mol. Cell 18 (2005) 499-505
    • (2005) Mol. Cell , vol.18 , pp. 499-505
    • Friedberg, E.C.1    Lehmann, A.R.2    Fuchs, R.P.3
  • 47
    • 33744546833 scopus 로고    scopus 로고
    • Translesion synthesis DNA polymerases and control of genome stability
    • Shcherbakova P.V., and Fijalkowska I.J. Translesion synthesis DNA polymerases and control of genome stability. Front Biosci. 11 (2006) 2496-2517
    • (2006) Front Biosci. , vol.11 , pp. 2496-2517
    • Shcherbakova, P.V.1    Fijalkowska, I.J.2
  • 48
    • 32644456504 scopus 로고    scopus 로고
    • Clubbing together on clamps: the key to translesion synthesis
    • Lehmann A.R. Clubbing together on clamps: the key to translesion synthesis. DNA Rep. (Amst.) 5 (2006) 404-407
    • (2006) DNA Rep. (Amst.) , vol.5 , pp. 404-407
    • Lehmann, A.R.1
  • 53
    • 0037020269 scopus 로고    scopus 로고
    • Human DNA polymerase kappa bypasses and extends beyond thymine glycols during translesion synthesis in vitro, preferentially incorporating correct nucleotides
    • Fischhaber P.L., Gerlach V.L., Feaver W.J., Hatahet Z., Wallace S.S., and Friedberg E.C. Human DNA polymerase kappa bypasses and extends beyond thymine glycols during translesion synthesis in vitro, preferentially incorporating correct nucleotides. J. Biol. Chem. 277 (2002) 37604-37611
    • (2002) J. Biol. Chem. , vol.277 , pp. 37604-37611
    • Fischhaber, P.L.1    Gerlach, V.L.2    Feaver, W.J.3    Hatahet, Z.4    Wallace, S.S.5    Friedberg, E.C.6
  • 54
    • 33744789415 scopus 로고    scopus 로고
    • The Y-family DNA polymerase kappa (pol kappa) functions in mammalian nucleotide-excision repair
    • Ogi T., and Lehmann A.R. The Y-family DNA polymerase kappa (pol kappa) functions in mammalian nucleotide-excision repair. Nat. Cell Biol. 8 (2006) 640-642
    • (2006) Nat. Cell Biol. , vol.8 , pp. 640-642
    • Ogi, T.1    Lehmann, A.R.2
  • 56
    • 33646815702 scopus 로고    scopus 로고
    • DNA interstrand cross-link repair in the cell cycle: a critical role for polymerase zeta in G1 phase
    • McHugh P.J., and Sarkar S. DNA interstrand cross-link repair in the cell cycle: a critical role for polymerase zeta in G1 phase. Cell Cycle 5 (2006) 1044-1047
    • (2006) Cell Cycle , vol.5 , pp. 1044-1047
    • McHugh, P.J.1    Sarkar, S.2
  • 57
    • 33645312939 scopus 로고    scopus 로고
    • DNA interstrand crosslink repair during G1 involves nucleotide excision repair and DNA polymerase zeta
    • Sarkar S., Davies A.A., Ulrich H.D., and McHugh P.J. DNA interstrand crosslink repair during G1 involves nucleotide excision repair and DNA polymerase zeta. EMBO J. 25 (2006) 1285-1294
    • (2006) EMBO J. , vol.25 , pp. 1285-1294
    • Sarkar, S.1    Davies, A.A.2    Ulrich, H.D.3    McHugh, P.J.4
  • 59
    • 27744483444 scopus 로고    scopus 로고
    • The translesion DNA polymerase theta plays a dominant role in immunoglobulin gene somatic hypermutation
    • Zan H., Shima N., Xu Z., Al-Qahtani A., Evinger Iii A.J., Zhong Y., Schimenti J.C., and Casali P. The translesion DNA polymerase theta plays a dominant role in immunoglobulin gene somatic hypermutation. EMBO J. 24 (2005) 3757-3769
    • (2005) EMBO J. , vol.24 , pp. 3757-3769
    • Zan, H.1    Shima, N.2    Xu, Z.3    Al-Qahtani, A.4    Evinger Iii, A.J.5    Zhong, Y.6    Schimenti, J.C.7    Casali, P.8
  • 60
    • 0037162552 scopus 로고    scopus 로고
    • Correlation of somatic hypermutation specificity and A-T base pair substitution errors by DNA polymerase eta during copying of a mouse immunoglobulin kappa light chain transgene
    • Pavlov Y.I., Rogozin I.B., Galkin A.P., Aksenova A.Y., Hanaoka F., Rada C., and Kunkel T.A. Correlation of somatic hypermutation specificity and A-T base pair substitution errors by DNA polymerase eta during copying of a mouse immunoglobulin kappa light chain transgene. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 9954-9959
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 9954-9959
    • Pavlov, Y.I.1    Rogozin, I.B.2    Galkin, A.P.3    Aksenova, A.Y.4    Hanaoka, F.5    Rada, C.6    Kunkel, T.A.7
  • 61
    • 0035379581 scopus 로고    scopus 로고
    • Somatic mutation hotspots correlate with DNA polymerase eta error spectrum
    • Rogozin I.B., Pavlov Y.I., Bebenek K., Matsuda T., and Kunkel T.A. Somatic mutation hotspots correlate with DNA polymerase eta error spectrum. Nat. Immunol. 2 (2001) 530-536
    • (2001) Nat. Immunol. , vol.2 , pp. 530-536
    • Rogozin, I.B.1    Pavlov, Y.I.2    Bebenek, K.3    Matsuda, T.4    Kunkel, T.A.5
  • 62
    • 20444427642 scopus 로고    scopus 로고
    • DNA polymerase eta contributes to strand bias of mutations of A versus T in immunoglobulin genes
    • Mayorov V.I., Rogozin I.B., Adkison L.R., and Gearhart P.J. DNA polymerase eta contributes to strand bias of mutations of A versus T in immunoglobulin genes. J. Immunol. 174 (2005) 7781-7786
    • (2005) J. Immunol. , vol.174 , pp. 7781-7786
    • Mayorov, V.I.1    Rogozin, I.B.2    Adkison, L.R.3    Gearhart, P.J.4
  • 63
  • 64
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
    • Kiefer J.R., Mao C., Braman J.C., and Beese L.S. Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Nature 391 (1998) 304-307
    • (1998) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 65
    • 0031861823 scopus 로고    scopus 로고
    • Crystal structures of the Klenow fragment of Thermus aquaticus DNA polymerase I complexed with deoxyribonucleoside triphosphates
    • Li Y., Kong Y., Korolev S., and Waksman G. Crystal structures of the Klenow fragment of Thermus aquaticus DNA polymerase I complexed with deoxyribonucleoside triphosphates. Protein Sci. 7 (1998) 1116-1123
    • (1998) Protein Sci. , vol.7 , pp. 1116-1123
    • Li, Y.1    Kong, Y.2    Korolev, S.3    Waksman, G.4
  • 66
    • 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. Structural basis for the dual coding potential of 8-oxoguanosine by a high-fidelity DNA polymerase. EMBO J. 23 (2004) 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
  • 67
    • 0037022239 scopus 로고    scopus 로고
    • Discrimination against purine-pyrimidine mispairs in the polymerase active site of DNA polymerase I: a structural explanation
    • Minnick D.T., Liu L., Grindley N.D., Kunkel T.A., and Joyce C.M. Discrimination against purine-pyrimidine mispairs in the polymerase active site of DNA polymerase I: a structural explanation. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 1194-1199
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1194-1199
    • Minnick, D.T.1    Liu, L.2    Grindley, N.D.3    Kunkel, T.A.4    Joyce, C.M.5
  • 68
    • 0030897085 scopus 로고    scopus 로고
    • Low fidelity mutants in the O-helix of Thermus aquaticus DNA polymerase I
    • Suzuki M., Avicola A.K., Hood L., and Loeb L.A. Low fidelity mutants in the O-helix of Thermus aquaticus DNA polymerase I. J. Biol. Chem. 272 (1997) 11228-11235
    • (1997) J. Biol. Chem. , vol.272 , pp. 11228-11235
    • Suzuki, M.1    Avicola, A.K.2    Hood, L.3    Loeb, L.A.4
  • 69
    • 0034693321 scopus 로고    scopus 로고
    • Thermus aquaticus DNA polymerase I mutants with altered fidelity. Interacting mutations in the O-helix
    • Suzuki M., Yoshida S., Adman E.T., Blank A., and Loeb L.A. Thermus aquaticus DNA polymerase I mutants with altered fidelity. Interacting mutations in the O-helix. J. Biol. Chem. 275 (2000) 32728-32735
    • (2000) J. Biol. Chem. , vol.275 , pp. 32728-32735
    • Suzuki, M.1    Yoshida, S.2    Adman, E.T.3    Blank, A.4    Loeb, L.A.5
  • 70
    • 0029784881 scopus 로고    scopus 로고
    • A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity
    • Minnick D.T., Astatke M., Joyce C.M., and Kunkel T.A. A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. J. Biol. Chem. 271 (1996) 24954-24961
    • (1996) J. Biol. Chem. , vol.271 , pp. 24954-24961
    • Minnick, D.T.1    Astatke, M.2    Joyce, C.M.3    Kunkel, T.A.4
  • 72
    • 0141483284 scopus 로고    scopus 로고
    • The frameshift infidelity of human DNA polymerase lambda. Implications for function
    • Bebenek K., Garcia-Diaz M., Blanco L., and Kunkel T.A. The frameshift infidelity of human DNA polymerase lambda. Implications for function. J. Biol. Chem. 278 (2003) 34685-34690
    • (2003) J. Biol. Chem. , vol.278 , pp. 34685-34690
    • Bebenek, K.1    Garcia-Diaz, M.2    Blanco, L.3    Kunkel, T.A.4
  • 73


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