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Volumn 23, Issue 14, 2003, Pages 5107-5112

Requirement of Watson-Crick hydrogen bonding for DNA synthesis by yeast DNA polymerase η

Author keywords

[No Author keywords available]

Indexed keywords

DIFLUOROTOLUENE; DNA BASE; DNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 0037773539     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.14.5107-5112.2003     Document Type: Article
Times cited : (80)

References (49)
  • 1
    • 0022423486 scopus 로고
    • Base-base mismatches. Thermodynamics of double helix formation for dCA3XA3G + dCT3YT3G (X, Y = A, C, G, T)
    • Aboul-ela, F., D. Koh, I. J. Tinoco, Jr., and F. H. Martin. 1985. Base-base mismatches. Thermodynamics of double helix formation for dCA3XA3G + dCT3YT3G (X, Y = A, C, G, T). Nucleic Acids Res. 13:4811-4825.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 4811-4825
    • Aboul-ela, F.1    Koh, D.2    Tinoco I.J., Jr.3    Martin, F.H.4
  • 2
    • 0020490305 scopus 로고
    • Determination of pyrimidine dimer unwinding angle by measurement of DNA electrophoretic mobility
    • Ciarrocchi, G., and A. M. Pedrini. 1982. Determination of pyrimidine dimer unwinding angle by measurement of DNA electrophoretic mobility. J. Mol. Biol. 155:177-183.
    • (1982) J. Mol. Biol. , vol.155 , pp. 177-183
    • Ciarrocchi, G.1    Pedrini, A.M.2
  • 3
    • 0028834955 scopus 로고
    • Gel fidelity assay measuring nucleotide misinsertion, exonucleolytic proofreading, and lesion bypass efficiencies
    • Creighton, S., L. B. Bloom, and M. F. Goodman. 1995. Gel fidelity assay measuring nucleotide misinsertion, exonucleolytic proofreading, and lesion bypass efficiencies. Methods Enzymol. 262:232-256.
    • (1995) Methods Enzymol. , vol.262 , pp. 232-256
    • Creighton, S.1    Bloom, L.B.2    Goodman, M.F.3
  • 4
    • 0025285869 scopus 로고
    • The abasic site as a challenge to DNA polymerase. A nuclear magnetic resonance study of G, C, and T opposite a model abasic site
    • Cuniasse, P., G. V. Fazakerley, W. Guschlbauer, B. E. Kaplan, and L. C. Sowers. 1990. The abasic site as a challenge to DNA polymerase. A nuclear magnetic resonance study of G, C, and T opposite a model abasic site. J. Mol. Biol. 213:303-314.
    • (1990) J. Mol. Biol. , vol.213 , pp. 303-314
    • Cuniasse, P.1    Fazakerley, G.V.2    Guschlbauer, W.3    Kaplan, B.E.4    Sowers, L.C.5
  • 6
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublie, S., S. Tabor, A. M. Long, C. C. Richardson, and T. Ellenberger. 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
  • 7
    • 0025783442 scopus 로고
    • Fidelity mechanisms in DNA replication
    • Echols, H., and M. F. Goodman. 1991. Fidelity mechanisms in DNA replication. Annu. Rev. Biochem. 60:477-511.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 477-511
    • Echols, H.1    Goodman, M.F.2
  • 8
    • 0030592095 scopus 로고    scopus 로고
    • Structure of Taq polymerase with DNA at the polymerase active site
    • Eom, S. H., J. Wang, and T. A. Steitz. 1996. Structure of Taq polymerase with DNA at the polymerase active site. Nature 382:278-281.
    • (1996) Nature , vol.382 , pp. 278-281
    • Eom, S.H.1    Wang, J.2    Steitz, T.A.3
  • 9
    • 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. USA 94:10493-10495.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10493-10495
    • Goodman, M.F.1
  • 10
    • 0035794165 scopus 로고    scopus 로고
    • Inefficient bypass of an abasic site by DNA polymerase η
    • Haracska, L., M. T. Washington, S. Prakash, and L. Prakash. 2001. Inefficient bypass of an abasic site by DNA polymerase η. J. Biol. Chem. 276:6861-6866.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6861-6866
    • Haracska, L.1    Washington, M.T.2    Prakash, S.3    Prakash, L.4
  • 11
    • 0034425754 scopus 로고    scopus 로고
    • Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase η
    • Haracska, L., S.-L. Yu, R. E. Johnson, L. Prakash, and S. Prakash. 2000. Efficient and accurate replication in the presence of 7,8-dihydro-8-oxoguanine by DNA polymerase η. Nat. Genet. 25:458-461.
    • (2000) Nat. Genet. , vol.25 , pp. 458-461
    • Haracska, L.1    Yu, S.-L.2    Johnson, R.E.3    Prakash, L.4    Prakash, S.5
  • 13
    • 0035034974 scopus 로고    scopus 로고
    • Role of DNA polymerase η in the bypass of a (6-4) TT photoproduct
    • Johnson, R. E., L. Haracska, S. Prakash, and L. Prakash. 2001. Role of DNA polymerase η in the bypass of a (6-4) TT photoproduct. Mol. Cell. Biol. 21:3558-3563.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3558-3563
    • Johnson, R.E.1    Haracska, L.2    Prakash, S.3    Prakash, L.4
  • 14
    • 0033538470 scopus 로고    scopus 로고
    • hRAD30 mutations in the variant form of xeroderma pigmentosum
    • Johnson, R. E., C. M. Kondratick, S. Prakash, and L. Prakash. 1999. hRAD30 mutations in the variant form of xeroderma pigmentosum. Science 285:263-265.
    • (1999) Science , vol.285 , pp. 263-265
    • Johnson, R.E.1    Kondratick, C.M.2    Prakash, S.3    Prakash, L.4
  • 15
    • 0033548231 scopus 로고    scopus 로고
    • Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Polη
    • Johnson, R. E., S. Prakash, and L. Prakash. 1999. Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Polη. Science 283:1001-1004.
    • (1999) Science , vol.283 , pp. 1001-1004
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 17
    • 0023845142 scopus 로고
    • NMR studies of abasic sites in DNA duplexes: Deoxyadenosine stacks into the helix opposite the cyclic analogue of 2-deoxyribose
    • Kalnik, M. W., C.-N. Chang, A. P. Grollman, and D. J. Patel. 1988. NMR studies of abasic sites in DNA duplexes: deoxyadenosine stacks into the helix opposite the cyclic analogue of 2-deoxyribose. Biochemistry 27:924-931.
    • (1988) Biochemistry , vol.27 , pp. 924-931
    • Kalnik, M.W.1    Chang, C.-N.2    Grollman, A.P.3    Patel, D.J.4
  • 19
    • 0032518524 scopus 로고    scopus 로고
    • Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
    • Kiefer, J. R., C. Mao, J. C. Braman, and L. S. Beese. 1998. Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Nature 391:304-307.
    • (1998) Nature , vol.391 , pp. 304-307
    • Kiefer, J.R.1    Mao, C.2    Braman, J.C.3    Beese, L.S.4
  • 20
    • 0029338999 scopus 로고
    • Contrasting structural impacts induced by cis-syn cyclobutane dimer and (6-4) adduct in DNA duplex decamers: Implication in mutagenesis and repair activity
    • Kim, J.-K., D. Patel, and B.-S. Choi. 1995. Contrasting structural impacts induced by cis-syn cyclobutane dimer and (6-4) adduct in DNA duplex decamers: implication in mutagenesis and repair activity. Photochem. Photobiol. 62:44-50.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 44-50
    • Kim, J.-K.1    Patel, D.2    Choi, B.-S.3
  • 21
    • 0035997351 scopus 로고    scopus 로고
    • Active site tightness and substrate fit in DNA replication
    • Kool, E. T. 2002. Active site tightness and substrate fit in DNA replication. Annu. Rev. Biochem. 71:191-219.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 191-219
    • Kool, E.T.1
  • 22
    • 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
  • 23
    • 0025891866 scopus 로고
    • NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (-8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex. 8-oxo-7H-dG(syn)·dA(anti) alignment at lesion site
    • Kouchakdjian, M., V. Bodepudi, S. Shibutani, M. Eisenberg, F. Johnson, A. P. Grollman, and D. J. Patel. 1991. NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (-8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex. 8-oxo-7H-dG(syn)·dA(anti) alignment at lesion site. Biochemistry 30:1403-1412.
    • (1991) Biochemistry , vol.30 , pp. 1403-1412
    • Kouchakdjian, M.1    Bodepudi, V.2    Shibutani, S.3    Eisenberg, M.4    Johnson, F.5    Grollman, A.P.6    Patel, D.J.7
  • 24
    • 0029758746 scopus 로고    scopus 로고
    • Spectroscopic and calorimetric characterizations of DNA duplexes containing 2-aminopurine
    • Law, S. M., R. Eritja, M. F. Goodman, and K. J. Breslauer. 1996. Spectroscopic and calorimetric characterizations of DNA duplexes containing 2-aminopurine. Biochemistry 35:12329-12337.
    • (1996) Biochemistry , vol.35 , pp. 12329-12337
    • Law, S.M.1    Eritja, R.2    Goodman, M.F.3    Breslauer, K.J.4
  • 25
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • Ling, H., F. Bondsocq, R. Woodgate, and W. Yang. 2001. Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication. Cell 107:91-102.
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Bondsocq, F.2    Woodgate, R.3    Yang, W.4
  • 28
    • 0034720285 scopus 로고    scopus 로고
    • Low fidelity DNA synthesis by human DNA polymerase η
    • Matsuda, T., K. Bebenek, C. Masutani, F. Hanaoka, and T. A. Kunkel. 2000. Low fidelity DNA synthesis by human DNA polymerase η. Nature 404:1011-1013.
    • (2000) Nature , vol.404 , pp. 1011-1013
    • Matsuda, T.1    Bebenek, K.2    Masutani, C.3    Hanaoka, F.4    Kunkel, T.A.5
  • 30
    • 0031792598 scopus 로고    scopus 로고
    • Efficient replication between non-hydrogen-bonded nucleoside shape analogs
    • Morales, J. C., and E. T. Kool. 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
  • 31
    • 0034711010 scopus 로고    scopus 로고
    • A functional hydrogen-bonding map of the minor groove binding tracks of six DNA polymerases
    • Morales, J. C., and E. T. Kool. 2000. A functional hydrogen-bonding map of the minor groove binding tracks of six DNA polymerases. Biochemistry 39:12979-12988.
    • (2000) Biochemistry , vol.39 , pp. 12979-12988
    • Morales, J.C.1    Kool, E.T.2
  • 32
    • 0034673294 scopus 로고    scopus 로고
    • Varied molecular interactions at the active sites of several DNA polymerases: Nonpolar nucleotide isosteres as probes
    • Morales, J. C., and E. T. Kool. 2000. Varied molecular interactions at the active sites of several DNA polymerases: nonpolar nucleotide isosteres as probes. J. Am. Chem. Soc. 122:1001-1007.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 1001-1007
    • Morales, J.C.1    Kool, E.T.2
  • 33
    • 0030967829 scopus 로고    scopus 로고
    • A thymidine triphosphate shape analog lacking Watson-Crick pairing ability is replicated with high sequence selectivity
    • Moran, S., R. X.-F. Ren, and E. T. Kool. 1997. A thymidine triphosphate shape analog lacking Watson-Crick pairing ability is replicated with high sequence selectivity. Proc. Natl. Acad. Sci. USA 94:10506-10511.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10506-10511
    • Moran, S.1    Ren, R.X.-F.2    Kool, E.T.3
  • 37
    • 0028575379 scopus 로고
    • Aromatic nonpolar nucleosides as hydrophobic isosteres of pyrimidine and purine nucleosides
    • Schweitzer, B. A., and E. T. Kool. 1994. Aromatic nonpolar nucleosides as hydrophobic isosteres of pyrimidine and purine nucleosides. J. Org. Chem. 59:7238-7242.
    • (1994) J. Org. Chem. , vol.59 , pp. 7238-7242
    • Schweitzer, B.A.1    Kool, E.T.2
  • 38
    • 0028886621 scopus 로고
    • Hydrophobic, non-hydrogen-bonding bases and base pairs in DNA
    • Schweitzer, B. A., and E. T. Kool. 1995. Hydrophobic, non-hydrogen-bonding bases and base pairs in DNA. J. Am. Chem. Soc. 117:1863-1872.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1863-1872
    • Schweitzer, B.A.1    Kool, E.T.2
  • 39
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani, S., M. Takeshita, and A. P. Grollman. 1991. Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature 349:431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 40
    • 0034762679 scopus 로고    scopus 로고
    • Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus
    • Silvian, L. F., E. A. Toth, P. Pham, M. F. Goodman, and T. Ellenberger. 2001. Crystal structure of a DinB family error-prone DNA polymerase from Sulfolobus solfataricus. Nat. Struct. Biol. 8:984-989.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 984-989
    • Silvian, L.F.1    Toth, E.A.2    Pham, P.3    Goodman, M.F.4    Ellenberger, T.5
  • 41
    • 0035814929 scopus 로고    scopus 로고
    • Identification of hydrogen bonds betweeen Escherichia coli DNA polymerase I (Klenow fragment) and the minor groove of DNA by amino acid substitution of the polymerase and atomic substitution of the DNA
    • Spratt, T. E. 2001. Identification of hydrogen bonds betweeen Escherichia coli DNA polymerase I (Klenow fragment) and the minor groove of DNA by amino acid substitution of the polymerase and atomic substitution of the DNA. Biochemistry 40:2647-2652.
    • (2001) Biochemistry , vol.40 , pp. 2647-2652
    • Spratt, T.E.1
  • 42
    • 0034847259 scopus 로고    scopus 로고
    • Structure of the catalytic core of S. cerevisiae DNA polymerase η: Implications for translesion DNA synthesis
    • Trincao, J., R. E. Johnson, C. R. Escalante, S. Prakash, L. Prakash, and A. K. Aggarwal. 2001. Structure of the catalytic core of S. cerevisiae DNA polymerase η: implications for translesion DNA synthesis. Mol. Cell 8:417-426.
    • (2001) Mol. Cell , vol.8 , pp. 417-426
    • Trincao, J.1    Johnson, R.E.2    Escalante, C.R.3    Prakash, S.4    Prakash, L.5    Aggarwal, A.K.6
  • 43
    • 0027159226 scopus 로고
    • Evidence from mutation spectra that the UV hypermutability of xeroderma pigmentosum variant cells reflects abnormal, error-prone replication on a template containing photoproducts
    • Wang, Y.-C., V. M. Maher, D. L. Mitchell, and J. J. McCormick. 1993. Evidence from mutation spectra that the UV hypermutability of xeroderma pigmentosum variant cells reflects abnormal, error-prone replication on a template containing photoproducts. Mol. Cell. Biol. 13:4276-4283.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4276-4283
    • Wang, Y.-C.1    Maher, V.M.2    Mitchell, D.L.3    McCormick, J.J.4
  • 44
    • 0034724287 scopus 로고    scopus 로고
    • Accuracy of thymine-thymine dimer bypass by Saccharomyces cerevisiae DNA polymerase η
    • Washington, M. T., R. E. Johnson, S. Prakash, and L. Prakash. 2000. Accuracy of thymine-thymine dimer bypass by Saccharomyces cerevisiae DNA polymerase η. Proc. Natl. Acad. Sci. USA 97:3094-3099.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3094-3099
    • Washington, M.T.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4
  • 45
    • 0033601194 scopus 로고    scopus 로고
    • Fidelity and processivity of Saccharomyces cerevisiae DNA polymerase η
    • Washington, M. T., R. E. Johnson, S. Prakash, and L. Prakash. 1999. Fidelity and processivity of Saccharomyces cerevisiae DNA polymerase η. J. Biol. Chem. 274:36835-36838.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36835-36838
    • Washington, M.T.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4
  • 46
    • 0035966270 scopus 로고    scopus 로고
    • Yeast DNA polymerase η utilizes an induced fit mechanism of nucleotide incorporation
    • Washington, M. T., L. Prakash, and S. Prakash. 2001. Yeast DNA polymerase η utilizes an induced fit mechanism of nucleotide incorporation. Cell 107:917-927.
    • (2001) Cell , vol.107 , pp. 917-927
    • Washington, M.T.1    Prakash, L.2    Prakash, S.3
  • 47
    • 0037693883 scopus 로고    scopus 로고
    • Yeast DNA polymerase η makes functional contacts with the DNA minor groove only at the incoming nucleoside triphosphate
    • Washington, M. T., W. T. Wolfle, T. E. Spratt, L. Prakash, and S. Prakash. 2003. Yeast DNA polymerase η makes functional contacts with the DNA minor groove only at the incoming nucleoside triphosphate. Proc. Natl. Acad. Sci. USA 100:5113-5118.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5113-5118
    • Washington, M.T.1    Wolfle, W.T.2    Spratt, T.E.3    Prakash, L.4    Prakash, S.5
  • 48
    • 0034747804 scopus 로고    scopus 로고
    • Requirement of DNA polymerase η for error-free bypass of UV-induced CC and TC photoproducts
    • Yu, S.-L., R. E. Johnson, S. Prakash, and L. Prakash. 2001. Requirement of DNA polymerase η for error-free bypass of UV-induced CC and TC photoproducts. Mol. Cell. Biol. 21:185-188.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 185-188
    • Yu, S.-L.1    Johnson, R.E.2    Prakash, S.3    Prakash, L.4
  • 49
    • 0034857266 scopus 로고    scopus 로고
    • Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain
    • Zhou, B.-L., J. D. Pata, and T. A. Steitz. 2001. Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain. Mol. Cell 8:427-437.
    • (2001) Mol. Cell , vol.8 , pp. 427-437
    • Zhou, B.-L.1    Pata, J.D.2    Steitz, T.A.3


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