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Volumn 23, Issue 8, 2003, Pages 3008-3012

Deoxynucleotide triphosphate binding mode conserved in Y family DNA polymerases

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEOTIDE; DNA POLYMERASE;

EID: 0345269987     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.8.3008-3012.2003     Document Type: Article
Times cited : (20)

References (22)
  • 1
    • 0028947982 scopus 로고
    • Deoxynucleoside triphosphate and pyrophosphate binding sites in the catalytically competent ternary complex for the polymerase reaction catalyzed by DNA polymerase I (Klenow fragment)
    • Astatke, M., N. D. F. Grindley, and C. M. Joyce. 1995. Deoxynucleoside triphosphate and pyrophosphate binding sites in the catalytically competent ternary complex for the polymerase reaction catalyzed by DNA polymerase I (Klenow fragment). J. Biol. Chem. 270:1945-1954.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1945-1954
    • Astatke, M.1    Grindley, N.D.F.2    Joyce, C.M.3
  • 2
    • 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
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A 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 A 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
  • 5
    • 0037126608 scopus 로고    scopus 로고
    • Mutations in human DNA polymerase η motif II alter bypass of DNA lesions
    • Glick, E., K. L. Vigna, and L. A. Loeb. 2001. Mutations in human DNA polymerase η motif II alter bypass of DNA lesions. EMBO J. 20:7303-7312.
    • (2001) EMBO J. , vol.20 , pp. 7303-7312
    • Glick, E.1    Vigna, K.L.2    Loeb, L.A.3
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0033548231 scopus 로고    scopus 로고
    • Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase
    • 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) Polη. Science , vol.283 , pp. 1001-1004
    • Johnson, R.E.1    Prakash, S.2    Prakash, L.3
  • 10
    • 0029894752 scopus 로고    scopus 로고
    • Significance of the O-helix residues of Escherichia coli DNA polymerase I in DNA synthesis: Dynamics of the dNTP binding pocket
    • Kaushik, M., V. N. Pandey, and M. J. Modak. 1996. Significance of the O-helix residues of Escherichia coli DNA polymerase I in DNA synthesis: dynamics of the dNTP binding pocket. Biochemistry 35:7256-7266.
    • (1996) Biochemistry , vol.35 , pp. 7256-7266
    • Kaushik, M.1    Pandey, V.N.2    Modak, M.J.3
  • 11
    • 0035012235 scopus 로고    scopus 로고
    • Acidic residues critical for the activity and biological function of yeast DNA polymerase η
    • Kondratick, C. M., M. T. Washington, S. Prakash, and L. Prakash. 2001. Acidic residues critical for the activity and biological function of yeast DNA polymerase η. Mol. Cell. Biol. 21:2018-2025.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2018-2025
    • Kondratick, C.M.1    Washington, M.T.2    Prakash, S.3    Prakash, L.4
  • 12
    • 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. Boudsocq, 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    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 14
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
    • Ollis, D. L., P. Brick, R. Hamlin, N. G. Xuong, and T. Steitz. 1985. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature 313:762-766.
    • (1985) Nature , vol.313 , pp. 762-766
    • Ollis, D.L.1    Brick, P.2    Hamlin, R.3    Xuong, N.G.4    Steitz, T.5
  • 15
    • 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
  • 16
    • 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
  • 17
    • 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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0027384099 scopus 로고
    • Ultraviolet hypermutability of a shuttle vector propagated in xeroderma pigmentosum variant cells
    • Waters, H. L., S. Seetharam, M. M. Seidman, and K. H. Kraemer. 1993. Ultraviolet hypermutability of a shuttle vector propagated in xeroderma pigmentosum variant cells. J. Investig. Dermatol. 101:744-748.
    • (1993) J. Investig. Dermatol. , vol.101 , pp. 744-748
    • Waters, H.L.1    Seetharam, S.2    Seidman, M.M.3    Kraemer, K.H.4
  • 22
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.