메뉴 건너뛰기




Volumn 47, Issue 33, 2008, Pages 8527-8537

Mechanism and dynamics of translesion DNA synthesis catalyzed by the Escherichia coli Klenow fragment

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DYNAMICS; ESCHERICHIA COLI; GENES; HYDROGEN; MECHANISMS; NONMETALS; NUCLEOTIDES; ORGANIC ACIDS;

EID: 49449086560     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800324r     Document Type: Article
Times cited : (22)

References (50)
  • 1
    • 0018881742 scopus 로고
    • Enzyme-catalyzed phosphoryl transfer reactions
    • Knowles, J. R. (1980) Enzyme-catalyzed phosphoryl transfer reactions. Annu. Rev. Biochem. 49, 877-919.
    • (1980) Annu. Rev. Biochem , vol.49 , pp. 877-919
    • Knowles, J.R.1
  • 3
    • 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
  • 4
    • 0031917762 scopus 로고    scopus 로고
    • DNA polymerase fidelity: From genetics toward a biochemical understanding
    • Goodman, M. F., and Fygenson, K. D. (1998) DNA polymerase fidelity: From genetics toward a biochemical understanding. Genetics 148, 1475-1482.
    • (1998) Genetics , vol.148 , pp. 1475-1482
    • Goodman, M.F.1    Fygenson, K.D.2
  • 5
    • 0027848722 scopus 로고
    • Multi-stage proofreading in DNA replication
    • Beckman, R. A., and Loeb, L. A. (1993) Multi-stage proofreading in DNA replication. Q. Rev. Biophys. 26, 225-331.
    • (1993) Q. Rev. Biophys , vol.26 , pp. 225-331
    • Beckman, R.A.1    Loeb, L.A.2
  • 6
    • 0020018105 scopus 로고
    • Fidelity of DNA synthesis
    • Loeb, L. A., and Kunkel, T. A. (1982) Fidelity of DNA synthesis. Annu. Rev. Biochem. 51, 429-457.
    • (1982) Annu. Rev. Biochem , vol.51 , pp. 429-457
    • Loeb, L.A.1    Kunkel, T.A.2
  • 7
    • 0000619168 scopus 로고
    • Comparison of nucleotide interactions in water, proteins, and vacuum: Model for DNA polymerase fidelity
    • Petruska, J., Sowers, L. C., and Goodman, M. F. (1986) Comparison of nucleotide interactions in water, proteins, and vacuum: Model for DNA polymerase fidelity. Proc. Natl. Acad. Sci. U.S.A. 83, 1559-1562.
    • (1986) Proc. Natl. Acad. Sci. U.S.A , vol.83 , pp. 1559-1562
    • Petruska, J.1    Sowers, L.C.2    Goodman, M.F.3
  • 8
    • 0029045480 scopus 로고
    • Recognition by viral and cellular DNA polymerases of nucleosides bearing bases with nonstandard hydrogen bonding patterns
    • Horlacher, J., Hottiger, M., Podust, V. N., Hubscher, U., and Benner, S. A. (1995) Recognition by viral and cellular DNA polymerases of nucleosides bearing bases with nonstandard hydrogen bonding patterns. Proc. Natl. Acad. Sci. U.S.A. 92, 6329-6933.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 6329-6933
    • Horlacher, J.1    Hottiger, M.2    Podust, V.N.3    Hubscher, U.4    Benner, S.A.5
  • 9
    • 4344630267 scopus 로고    scopus 로고
    • The fidelity of replication of the three-base-pair set adenine/thymine, hypoxanthine/cytosine and 6-thiopurine/5-methyl-2-pyrimidinone with T7 DNA polymerase
    • Rappaport, H. P. (2004) The fidelity of replication of the three-base-pair set adenine/thymine, hypoxanthine/cytosine and 6-thiopurine/5-methyl-2-pyrimidinone with T7 DNA polymerase. Biochem. J. 381, 709-717.
    • (2004) Biochem. J , vol.381 , pp. 709-717
    • Rappaport, H.P.1
  • 10
    • 0030967829 scopus 로고    scopus 로고
    • A thymidine triphosphate shape analog lacking Watson-Crick pairing ability is replicated with high sequence selectivity
    • Moran, S., Ren, R. X., and Kool, E. T. (1997) A thymidine triphosphate shape analog lacking Watson-Crick pairing ability is replicated with high sequence selectivity. Proc. Natl. Acad. Sci. U.S.A. 94, 10506-10511.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 10506-10511
    • Moran, S.1    Ren, R.X.2    Kool, E.T.3
  • 11
    • 0031792598 scopus 로고    scopus 로고
    • Efficient replication between non-hydrogen-bonded nucleoside shape analogs
    • Morales, J. C., and Kool, E. T. (1998) Efficient replication between non-hydrogen-bonded nucleoside shape analogs. Nat. Struct. Biol. 5, 950-954.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 950-954
    • Morales, J.C.1    Kool, E.T.2
  • 12
    • 0034835786 scopus 로고    scopus 로고
    • Efforts toward expansion of the genetic alphabet: Replication of DNA with three base pairs
    • Tae, E. L., Wu, Y., Xia, G., Schultz, P. G., and Romesberg, F. E. (2001) Efforts toward expansion of the genetic alphabet: Replication of DNA with three base pairs. J. Am. Chem. Soc. 123, 7439-7440.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 7439-7440
    • Tae, E.L.1    Wu, Y.2    Xia, G.3    Schultz, P.G.4    Romesberg, F.E.5
  • 13
    • 0141640828 scopus 로고    scopus 로고
    • DNA polymerase template interactions probed by degenerate isosteric nucleobase analogs
    • Paul, N., Nashine, V. C., Hoops, G., Zhang, P., Zhou, J., Bergstrom, D. E., and Davisson, V. J. (2003) DNA polymerase template interactions probed by degenerate isosteric nucleobase analogs. Chem. Biol. 10, 815-825.
    • (2003) Chem. Biol , vol.10 , pp. 815-825
    • Paul, N.1    Nashine, V.C.2    Hoops, G.3    Zhang, P.4    Zhou, J.5    Bergstrom, D.E.6    Davisson, V.J.7
  • 14
    • 0042318450 scopus 로고    scopus 로고
    • Facile polymerization of dNTPs bearing unnatural base analogues by DNA polymerase α and Klenow fragment (DNA polymerase I)
    • Chiaramonte, M., Moore, C. L., Kincaid, K., and Kuchta, R. D. (2003) Facile polymerization of dNTPs bearing unnatural base analogues by DNA polymerase α and Klenow fragment (DNA polymerase I). Biochemistry 42, 10472-10481.
    • (2003) Biochemistry , vol.42 , pp. 10472-10481
    • Chiaramonte, M.1    Moore, C.L.2    Kincaid, K.3    Kuchta, R.D.4
  • 15
    • 0141782150 scopus 로고    scopus 로고
    • Hirao, I., Fujiwara, T., Kimoto, M., Mitsui, T., Okuni, T., Ohtsuki, T., and Yokoyama, S. (2000) Unnatural base pairs between 2-amino-6-(2-thienyl)purine and the complementary bases. Nucleic Acids Symp. Ser. 44, 261-262.
    • Hirao, I., Fujiwara, T., Kimoto, M., Mitsui, T., Okuni, T., Ohtsuki, T., and Yokoyama, S. (2000) Unnatural base pairs between 2-amino-6-(2-thienyl)purine and the complementary bases. Nucleic Acids Symp. Ser. 44, 261-262.
  • 16
    • 0346463162 scopus 로고    scopus 로고
    • Evaluating the contribution of base stacking during translesion DNA replication
    • Reineks, E. Z., and Berdis, A. J. (2004) Evaluating the contribution of base stacking during translesion DNA replication. Biochemistry 43, 393-404.
    • (2004) Biochemistry , vol.43 , pp. 393-404
    • Reineks, E.Z.1    Berdis, A.J.2
  • 17
    • 3042798863 scopus 로고    scopus 로고
    • Evaluating the contributions of desolvation and base-stacking during translesion DNA synthesis
    • Zhang, X., Lee, I., and Berdis, A. J. (2004) Evaluating the contributions of desolvation and base-stacking during translesion DNA synthesis. Org. Biomol. Chem. 2, 1703-1711.
    • (2004) Org. Biomol. Chem , vol.2 , pp. 1703-1711
    • Zhang, X.1    Lee, I.2    Berdis, A.J.3
  • 18
    • 25444443087 scopus 로고    scopus 로고
    • The use of nonnatural nucleotides to probe the contributions of shape complementarity and π-electron surface area during DNA polymerization
    • Zhang, X., Lee, I., and Berdis, A. J. (2005) The use of nonnatural nucleotides to probe the contributions of shape complementarity and π-electron surface area during DNA polymerization. Biochemistry 44, 13101-13110.
    • (2005) Biochemistry , vol.44 , pp. 13101-13110
    • Zhang, X.1    Lee, I.2    Berdis, A.J.3
  • 19
    • 30744471162 scopus 로고    scopus 로고
    • Hydrophobicity, shape, and π-electron contributions during translesion DNA synthesis
    • Zhang, X., Lee, I., Zhou, X., and Berdis, A. J. (2006) Hydrophobicity, shape, and π-electron contributions during translesion DNA synthesis. J. Am. Chem. Soc. 128, 143-149.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 143-149
    • Zhang, X.1    Lee, I.2    Zhou, X.3    Berdis, A.J.4
  • 20
    • 36849053354 scopus 로고    scopus 로고
    • Enhancing the "A-rule" of translesion DNA synthesis: Promutagenic DNA synthesis using modified nucleoside triphosphates
    • Devadoss, B., Lee, I., and Berdis, A. J. (2007) Enhancing the "A-rule" of translesion DNA synthesis: Promutagenic DNA synthesis using modified nucleoside triphosphates. Biochemistry 46, 13752-13761.
    • (2007) Biochemistry , vol.46 , pp. 13752-13761
    • Devadoss, B.1    Lee, I.2    Berdis, A.J.3
  • 21
    • 35649000372 scopus 로고    scopus 로고
    • Optimization of non-natural nucleotides for selective incorporation opposite damaged DNA
    • Vineyard, D., Zhang, X., Donnelly, A., Lee, I., and Berdis, A. J. (2007) Optimization of non-natural nucleotides for selective incorporation opposite damaged DNA. Org. Biomol. Chem. 5, 3623-3630.
    • (2007) Org. Biomol. Chem , vol.5 , pp. 3623-3630
    • Vineyard, D.1    Zhang, X.2    Donnelly, A.3    Lee, I.4    Berdis, A.J.5
  • 22
    • 0020650113 scopus 로고
    • Infidelity of DNA synthesis associated with bypass of apurinic sites
    • Schaaper, R. M., Kunkel, T. A., and Loeb, L. A. (1983) Infidelity of DNA synthesis associated with bypass of apurinic sites. Proc. Natl. Acad. Sci. U.S.A. 80, 487-491.
    • (1983) Proc. Natl. Acad. Sci. U.S.A , vol.80 , pp. 487-491
    • Schaaper, R.M.1    Kunkel, T.A.2    Loeb, L.A.3
  • 23
    • 0020488536 scopus 로고
    • Coding properties of poly(deoxycytidylic acid) templates containing uracil or apyrimidinic sites: In vitro modulation of mutagenesis by deoxyribonucleic acid repair enzymes
    • Boiteux, S., and Laval, J. (1982) Coding properties of poly(deoxycytidylic acid) templates containing uracil or apyrimidinic sites: In vitro modulation of mutagenesis by deoxyribonucleic acid repair enzymes. Biochemistry 21, 6746-6751.
    • (1982) Biochemistry , vol.21 , pp. 6746-6751
    • Boiteux, S.1    Laval, J.2
  • 24
    • 0031038053 scopus 로고    scopus 로고
    • Abasic translesion synthesis by DNA polymerase β violates the "A-rule". Novel types of nucleotide incorporation by human DNA polymerase β at an abasic lesion in different sequence contexts
    • Efrati, E., Tocco, G., Eritja, R., Wilson, S. H., and Goodman, M. F. (1997) Abasic translesion synthesis by DNA polymerase β violates the "A-rule". Novel types of nucleotide incorporation by human DNA polymerase β at an abasic lesion in different sequence contexts. J. Biol. Chem. 272, 2559-2569.
    • (1997) J. Biol. Chem , vol.272 , pp. 2559-2569
    • Efrati, E.1    Tocco, G.2    Eritja, R.3    Wilson, S.H.4    Goodman, M.F.5
  • 25
    • 0035912947 scopus 로고    scopus 로고
    • Dynamics of translesion DNA synthesis catalyzed by the bacteriophage T4 exonuclease-deficient DNA polymerase
    • Berdis, A. J. (2001) Dynamics of translesion DNA synthesis catalyzed by the bacteriophage T4 exonuclease-deficient DNA polymerase. Biochemistry 40, 7180-7191.
    • (2001) Biochemistry , vol.40 , pp. 7180-7191
    • Berdis, A.J.1
  • 26
    • 0028827318 scopus 로고
    • Purification of Escherichia coli DNA polymerase I and Klenow fragment
    • Joyce, C. M., and Derbyshire, V. (1995) Purification of Escherichia coli DNA polymerase I and Klenow fragment. Methods Enzymol. 262, 3-13.
    • (1995) Methods Enzymol , vol.262 , pp. 3-13
    • Joyce, C.M.1    Derbyshire, V.2
  • 27
    • 0026464542 scopus 로고
    • Kinetic characterization of the polymerase and exonuclease activities of the gene 43 protein of bacteriophage T4
    • Capson, T. L., Peliska, J. A., Kaboord, B. F., Frey, M. W., Lively, C., Dahlberg, M., and Benkovic, S. J. (1992) Kinetic characterization of the polymerase and exonuclease activities of the gene 43 protein of bacteriophage T4. Biochemistry 31, 10984-10994.
    • (1992) Biochemistry , vol.31 , pp. 10984-10994
    • Capson, T.L.1    Peliska, J.A.2    Kaboord, B.F.3    Frey, M.W.4    Lively, C.5    Dahlberg, M.6    Benkovic, S.J.7
  • 28
    • 0022537369 scopus 로고
    • Mechanism of DNA polymerase I: Exonuclease/polymerase activity switch and DNA sequence dependence of pyro-phosphorolysis and misincorporation reactions
    • Mizrahi, V., Benkovic, P. A., and Benkovic, S. J. (1986) Mechanism of DNA polymerase I: Exonuclease/polymerase activity switch and DNA sequence dependence of pyro-phosphorolysis and misincorporation reactions. Proc. Natl. Acad. Sci. U.S.A. 83, 5769-5773.
    • (1986) Proc. Natl. Acad. Sci. U.S.A , vol.83 , pp. 5769-5773
    • Mizrahi, V.1    Benkovic, P.A.2    Benkovic, S.J.3
  • 29
    • 33845462841 scopus 로고    scopus 로고
    • Fluorescent analysis of translesion DNA synthesis by using a novel, non-natural nucleotide analogue
    • Lee, I., and Berdis, A. (2006) Fluorescent analysis of translesion DNA synthesis by using a novel, non-natural nucleotide analogue. ChemBioChem 7, 1990-1997.
    • (2006) ChemBioChem , vol.7 , pp. 1990-1997
    • Lee, I.1    Berdis, A.2
  • 31
    • 0030971099 scopus 로고    scopus 로고
    • Translesional synthesis on DNA templates containing a single abasic site. A mechanistic study of the "A rule
    • Shibutani, S., Takeshita, M., and Grollman, A. P. (1997) Translesional synthesis on DNA templates containing a single abasic site. A mechanistic study of the "A rule". J. Biol. Chem. 27, 13916-13922.
    • (1997) J. Biol. Chem , vol.27 , pp. 13916-13922
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 32
    • 0031034183 scopus 로고    scopus 로고
    • Mechanism of bypass synthesis through an abasic site analog by DNA polymerase I
    • Paz-Elizur, T., Takeshita, M., and Livneh, Z. (1997) Mechanism of bypass synthesis through an abasic site analog by DNA polymerase I. Biochemistry 36, 1766-1773.
    • (1997) Biochemistry , vol.36 , pp. 1766-1773
    • Paz-Elizur, T.1    Takeshita, M.2    Livneh, Z.3
  • 33
    • 0026111317 scopus 로고
    • The 'A rule' of mutagen specificity: A consequence of DNA polymerase bypass of non-instructional lesions?
    • Strauss, B. S. (1991) The 'A rule' of mutagen specificity: A consequence of DNA polymerase bypass of non-instructional lesions? BioEssays 13, 79-84.
    • (1991) BioEssays , vol.13 , pp. 79-84
    • Strauss, B.S.1
  • 34
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz, T. A. (1999) DNA polymerases: Structural diversity and common mechanisms. J. Biol. Chem. 274, 17395-17398.
    • (1999) J. Biol. Chem , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 35
    • 0026510657 scopus 로고
    • A molecular model of the complete three-dimensional structure of the Klenow fragment of Escherichia coli DNA polymerase I: Binding of the dNTP substrate and template-primer
    • Yadav, P. N., Yadav, J. S., and Modak, M. J. (1992) A molecular model of the complete three-dimensional structure of the Klenow fragment of Escherichia coli DNA polymerase I: Binding of the dNTP substrate and template-primer. Biochemistry 31, 2879-2886.
    • (1992) Biochemistry , vol.31 , pp. 2879-2886
    • Yadav, P.N.1    Yadav, J.S.2    Modak, M.J.3
  • 36
    • 0027231782 scopus 로고
    • Structure of DNA polymerase I Klenow fragment bound to duplex DNA
    • Beese, L. S., Derbyshire, V., and Steitz, T. A. (1993) Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Science 260, 352-355.
    • (1993) Science , vol.260 , pp. 352-355
    • Beese, L.S.1    Derbyshire, V.2    Steitz, T.A.3
  • 37
    • 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. (1993) Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate. Biochemistry 32, 14095-14101.
    • (1993) Biochemistry , vol.32 , pp. 14095-14101
    • Beese, L.S.1    Friedman, J.M.2    Steitz, T.A.3
  • 38
    • 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
  • 39
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol α family DNA polymerase
    • Franklin, M. C., Wang, J., and Steitz, T. A. (2001) Structure of the replicating complex of a pol α family DNA polymerase. Cell 105, 657-667.
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 40
    • 2342537864 scopus 로고    scopus 로고
    • Crystallographic snapshots of a replicative DNA polymerase encountering an abasic site
    • Hogg, M., Wallace, S. S., and Doublie, S. (2004) Crystallographic snapshots of a replicative DNA polymerase encountering an abasic site. EMBO J. 23, 1483-1493.
    • (2004) EMBO J , vol.23 , pp. 1483-1493
    • Hogg, M.1    Wallace, S.S.2    Doublie, S.3
  • 41
    • 2342484512 scopus 로고    scopus 로고
    • Lesion (in)tolerance reveals insights into DNA replication fidelity
    • Freisinger, E., Grollman, A. P., Miller, H., and Kisker, C. (2004) Lesion (in)tolerance reveals insights into DNA replication fidelity. EMBO J. 23, 1494-1505.
    • (2004) EMBO J , vol.23 , pp. 1494-1505
    • Freisinger, E.1    Grollman, A.P.2    Miller, H.3    Kisker, C.4
  • 42
    • 34548699886 scopus 로고    scopus 로고
    • Caught bending the A-rule: Crystal structures of translesion DNA synthesis with a non-natural nucleotide
    • Zahn, K. E., Belrhali, H., Wallace, S. S., and Doublié, S. (2007) Caught bending the A-rule: Crystal structures of translesion DNA synthesis with a non-natural nucleotide. Biochemistry 46, 10551-10561.
    • (2007) Biochemistry , vol.46 , pp. 10551-10561
    • Zahn, K.E.1    Belrhali, H.2    Wallace, S.S.3    Doublié, S.4
  • 44
    • 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
  • 45
    • 0036897848 scopus 로고    scopus 로고
    • Aromatic interactions in model systems
    • Waters, M. L. (2002) Aromatic interactions in model systems. Curr. Opin. Chem. Biol. 6, 736-741.
    • (2002) Curr. Opin. Chem. Biol , vol.6 , pp. 736-741
    • Waters, M.L.1
  • 46
    • 0031774216 scopus 로고    scopus 로고
    • Replication of non-hydrogen bonded bases by DNA polymerases: A mechanism for steric matching
    • Kool, E. T. (1998) Replication of non-hydrogen bonded bases by DNA polymerases: A mechanism for steric matching. Biopolymers 48, 3-17.
    • (1998) Biopolymers , vol.48 , pp. 3-17
    • Kool, E.T.1
  • 47
    • 0033578081 scopus 로고    scopus 로고
    • A specific partner for abasic damage in DNA
    • Matray, T. J., and Kool, E. T. (1999) A specific partner for abasic damage in DNA. Nature 399, 704-708.
    • (1999) Nature , vol.399 , pp. 704-708
    • Matray, T.J.1    Kool, E.T.2
  • 48
    • 0026029379 scopus 로고
    • A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity
    • Carroll, S. S., Cowart, M., and Benkovic, S. J. (1991) A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity. Biochemistry 30, 804-813.
    • (1991) Biochemistry , vol.30 , pp. 804-813
    • Carroll, S.S.1    Cowart, M.2    Benkovic, S.J.3
  • 49
    • 0030906056 scopus 로고    scopus 로고
    • Base miscoding and strand misalignment errors by mutator Klenow polymerases with amino acid substitutions at tyrosine 766 in the O helix of the fingers subdomain
    • Bell, J. B., Eckert, K. A., Joyce, C. M., and Kunkel, T. A. (1997) Base miscoding and strand misalignment errors by mutator Klenow polymerases with amino acid substitutions at tyrosine 766 in the O helix of the fingers subdomain. J. Biol. Chem. 272, 7345-7351.
    • (1997) J. Biol. Chem , vol.272 , pp. 7345-7351
    • Bell, J.B.1    Eckert, K.A.2    Joyce, C.M.3    Kunkel, T.A.4
  • 50
    • 0037426351 scopus 로고    scopus 로고
    • Mechanistic insights into replication across from bulky DNA adducts: A mutant polymerase I allows an N-acetyl-2-aminofluorene adduct to be accommodated during DNA synthesis
    • Lone, S., and Romano, L. J. (2003) Mechanistic insights into replication across from bulky DNA adducts: A mutant polymerase I allows an N-acetyl-2-aminofluorene adduct to be accommodated during DNA synthesis. Biochemistry 42, 3826-3834.
    • (2003) Biochemistry , vol.42 , pp. 3826-3834
    • Lone, S.1    Romano, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.