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Volumn 16, Issue 4, 1997, Pages 880-888

UvrAB activity at a damaged DNA site: Is unpaired DNA present?

Author keywords

DNA repair; Nucleotide excision repair; Pre incision complex formation; UvrAB complex

Indexed keywords

DNA; N (2 FLUORENYL)ACETAMIDE; NUCLEASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE;

EID: 0031046737     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.4.880     Document Type: Article
Times cited : (18)

References (38)
  • 1
    • 0026296795 scopus 로고
    • Identification of the different intermediates in the interaction of (A)BC excinuclease with its substrates by DNase I footprinting on two uniquely modified oligonucleotides
    • Bertrand-Burggraf, E., Selby, C.P., Hearst, J.E. and Sancar, A. (1991) Identification of the different intermediates in the interaction of (A)BC excinuclease with its substrates by DNase I footprinting on two uniquely modified oligonucleotides. J. Mol. Biol., 219, 27-36.
    • (1991) J. Mol. Biol. , vol.219 , pp. 27-36
    • Bertrand-Burggraf, E.1    Selby, C.P.2    Hearst, J.E.3    Sancar, A.4
  • 2
    • 0000559719 scopus 로고
    • Primer on the topology and geometry of DNA supercoiling
    • Cozzarelli, N.R. and Wang, J.C. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Cozzarelli, N.R., Boles, T.C. and White, J.H. (1990) Primer on the topology and geometry of DNA supercoiling. In Cozzarelli, N.R. and Wang, J.C. (eds), DNA Topology and its Biological Effects. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 139-184.
    • (1990) DNA Topology and Its Biological Effects , pp. 139-184
    • Cozzarelli, N.R.1    Boles, T.C.2    White, J.H.3
  • 3
    • 0028808098 scopus 로고
    • Role of the Rad1 and Rad10 proteins in nucleotide excision repair and recombination
    • Davies, A.A., Friedberg, E.C., Tomkinson, A.E., Wood, R.D. and West, S.C. (1995) Role of the Rad1 and Rad10 proteins in nucleotide excision repair and recombination. J. Biol. Chem., 270, 24638-24641.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24638-24641
    • Davies, A.A.1    Friedberg, E.C.2    Tomkinson, A.E.3    Wood, R.D.4    West, S.C.5
  • 4
    • 0028631162 scopus 로고
    • DNA bending by Cro protein in specific and nonspecific complexes: Implications for protein site recognition and specificity
    • Erie, D.A., Yang, G., Schultz, H.C. and Bustamante, C. (1994) DNA bending by Cro protein in specific and nonspecific complexes: implications for protein site recognition and specificity. Science, 266, 1562-1566.
    • (1994) Science , vol.266 , pp. 1562-1566
    • Erie, D.A.1    Yang, G.2    Schultz, H.C.3    Bustamante, C.4
  • 6
    • 0031039924 scopus 로고    scopus 로고
    • The limited strand-separating activity of the UvrAB protein complex and its role in the recognition of DNA damage
    • Gordienko, I. and Rupp, W.D. (1997) The limited strand-separating activity of the UvrAB protein complex and its role in the recognition of DNA damage. EMBO J., 16, 889-895.
    • (1997) EMBO J. , vol.16 , pp. 889-895
    • Gordienko, I.1    Rupp, W.D.2
  • 7
    • 0026458478 scopus 로고
    • Structural analysis of ternary complexes of vaccinia RNA polymerase
    • Hagler, J. and Shuman, S. (1992) Structural analysis of ternary complexes of vaccinia RNA polymerase. Proc. Natl Acad. Sci. USA, 89, 10099-10103.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10099-10103
    • Hagler, J.1    Shuman, S.2
  • 8
    • 0024840350 scopus 로고
    • Localization of DNa repair synthesis by human cell extracts to a short region at the site of a lesion
    • Hansson, J., Munn, M. Rupp, W.D., Kahn, R. and Wood, R.D. (1989) Localization of DNA repair synthesis by human cell extracts to a short region at the site of a lesion. J. Biol. Chem., 264, 21788-21792.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21788-21792
    • Hansson, J.1    Munn, M.2    Rupp, W.D.3    Kahn, R.4    Wood, R.D.5
  • 9
    • 0027968833 scopus 로고
    • Flow linear dichroism and electron microscopic analysis of protein-DNa complexes of a mutant UvrB protein that binds to but cannot kink DNA
    • Hsu, D.S., Takahashi, M. Delagoutte, E., Bertrand-Burggraf, E., Wang, Y.H., Norden, B., Fuchs, R.P., Griffith, J. and Sancar, A. (1994) Flow linear dichroism and electron microscopic analysis of protein-DNA complexes of a mutant UvrB protein that binds to but cannot kink DNA. J. Mol. Biol., 241, 645-650.
    • (1994) J. Mol. Biol. , vol.241 , pp. 645-650
    • Hsu, D.S.1    Takahashi, M.2    Delagoutte, E.3    Bertrand-Burggraf, E.4    Wang, Y.H.5    Norden, B.6    Fuchs, R.P.7    Griffith, J.8    Sancar, A.9
  • 10
    • 0022133407 scopus 로고
    • Chemical probes of DNA conformation: Detection of Z-DNA at nucleotide resolution
    • Johnston, B.H. and Rich, A. (1985) Chemical probes of DNA conformation: detection of Z-DNA at nucleotide resolution. Cell, 42, 713-724.
    • (1985) Cell , vol.42 , pp. 713-724
    • Johnston, B.H.1    Rich, A.2
  • 11
    • 0026766290 scopus 로고
    • Protein-induced bending and DNA cyclization
    • Kahn, J.D. and Crothers, M.D. (1992) Protein-induced bending and DNA cyclization. Proc. Natl Acad. Sci. USA, 89, 6343-6347.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6343-6347
    • Kahn, J.D.1    Crothers, M.D.2
  • 12
    • 0023918097 scopus 로고
    • Efficient synthesis of a supercoiled M13 DNa molecule containing a site specifically placed psoralen adduct and its use as a substrate for DNa replication
    • Kodadek, T. and Gamper, H. (1988) Efficient synthesis of a supercoiled M13 DNA molecule containing a site specifically placed psoralen adduct and its use as a substrate for DNA replication. Biochemistry, 27, 3210-3215.
    • (1988) Biochemistry , vol.27 , pp. 3210-3215
    • Kodadek, T.1    Gamper, H.2
  • 13
    • 0014045470 scopus 로고
    • 8-(N-2-fluorenylacetamido)guanosine, an arylamidation reaction product of guanosine and the carcinogen N-acetoxy-N-2-fluorenylacetamide in neutral solution
    • Kriek, E., Miller, J.A., Juhl, U. and Miller, E.C. (1967) 8-(N-2-fluorenylacetamido)guanosine, an arylamidation reaction product of guanosine and the carcinogen N-acetoxy-N-2-fluorenylacetamide in neutral solution. Biochemistry, 6, 177-182.
    • (1967) Biochemistry , vol.6 , pp. 177-182
    • Kriek, E.1    Miller, J.A.2    Juhl, U.3    Miller, E.C.4
  • 14
    • 0026702582 scopus 로고
    • Active site of (A)BC excinuclease. II. Binding, bending, and catalysis mutants of UvrB reveal a direct role in 3′ and an indirect role in 5′ incision
    • Lin, J.J., Phillips, A.M., Hearst, J.E. and Sancar, A. (1992) Active site of (A)BC excinuclease. II. Binding, bending, and catalysis mutants of UvrB reveal a direct role in 3′ and an indirect role in 5′ incision. J. Biol. Chem., 267, 17693-17700.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17693-17700
    • Lin, J.J.1    Phillips, A.M.2    Hearst, J.E.3    Sancar, A.4
  • 15
    • 0028066920 scopus 로고
    • Helicase motifs V and VI of the Escherichia coli UvrB protein of the UvrABC endonuclease are essential for the formation of the pre-incision complex
    • Moolenaar, G.F., Visse, R., Ortiz-Buysse, M., Goosen, N. and van de Putte, P. (1994) Helicase motifs V and VI of the Escherichia coli UvrB protein of the UvrABC endonuclease are essential for the formation of the pre-incision complex. J. Mol. Biol., 40, 294-307.
    • (1994) J. Mol. Biol. , vol.40 , pp. 294-307
    • Moolenaar, G.F.1    Visse, R.2    Ortiz-Buysse, M.3    Goosen, N.4    Van De Putte, P.5
  • 16
    • 0018673443 scopus 로고
    • Purification of the gene 43, 44, 45 and 62 proteins of the bacteriophage T4 DNA replication apparatus
    • Morris, C.F., Hama-Inaba, H., Mace, D., Sinha, N.K. and Alberts, B. (1979) Purification of the gene 43, 44, 45 and 62 proteins of the bacteriophage T4 DNA replication apparatus. J. Biol. Chem., 254, 6787-6796.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6787-6796
    • Morris, C.F.1    Hama-Inaba, H.2    Mace, D.3    Sinha, N.K.4    Alberts, B.5
  • 17
    • 0026329271 scopus 로고
    • Interaction of the UvrABC endonuclease with DNa containing a psoralen monoadduct or crosslink. Differential effects of superhelical density and comparison of pre-incision complexes
    • Munn, M.M. and Rupp, W.D. (1991) Interaction of the UvrABC endonuclease with DNA containing a psoralen monoadduct or crosslink. Differential effects of superhelical density and comparison of pre-incision complexes. J. Biol. Chem., 266, 24748-24756.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24748-24756
    • Munn, M.M.1    Rupp, W.D.2
  • 18
    • 0018289977 scopus 로고
    • DNa replication with bacteriophage T4 protiens. Purification of the protiens encoded by T4 genes 41, 45, 44 and 62 using a complementation assay
    • Nossal, N.G. (1979) DNA replication with bacteriophage T4 protiens. Purification of the protiens encoded by T4 genes 41, 45, 44 and 62 using a complementation assay. J. Biol. Chem., 54, 6026-6031.
    • (1979) J. Biol. Chem. , vol.54 , pp. 6026-6031
    • Nossal, N.G.1
  • 19
    • 0028085556 scopus 로고
    • XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repair
    • O'Donovan, A., Davies, A.A., Moggs, J.G., West, S.C. and Wood, R.D. (1994) XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repair. Nature, 371, 432-435.
    • (1994) Nature , vol.371 , pp. 432-435
    • O'Donovan, A.1    Davies, A.A.2    Moggs, J.G.3    West, S.C.4    Wood, R.D.5
  • 20
    • 0023047220 scopus 로고
    • The effect of Escherichia coli Uvr protein binding on the topology of supercoiled DNA
    • Oh, E.Y. and Grossman, L. (1986) The effect of Escherichia coli Uvr protein binding on the topology of supercoiled DNA. Nucleic Acids Res., 14, 8557-8571.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 8557-8571
    • Oh, E.Y.1    Grossman, L.2
  • 21
    • 1842396307 scopus 로고
    • Helicase properties of the Escherichia coli UvrAB protein complex
    • Oh, E.Y. and Grossman, L. (1987) Helicase properties of the Escherichia coli UvrAB protein complex. Proc. Natl Acad. Sci. USA, 84, 3638-3642.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 3638-3642
    • Oh, E.Y.1    Grossman, L.2
  • 22
    • 0025150833 scopus 로고
    • Formation and enzymatic properties of the UvrB:DNA complex
    • Orren, D.K. and Sancar, A. (1990) Formation and enzymatic properties of the UvrB:DNA complex. J. Biol. Chem., 265, 15796-15803.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15796-15803
    • Orren, D.K.1    Sancar, A.2
  • 23
    • 0026595890 scopus 로고
    • Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I
    • Orren, D.K., Selby, C.P., Hearst, J.E. and Sancar, A. (1992) Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase I. J. Biol. Chem., 267, 780-788.
    • (1992) J. Biol. Chem. , vol.267 , pp. 780-788
    • Orren, D.K.1    Selby, C.P.2    Hearst, J.E.3    Sancar, A.4
  • 24
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo, C.O. and Sauer, R.T. (1992) Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem., 61, 1053-1095.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.O.1    Sauer, R.T.2
  • 26
  • 27
    • 0020641572 scopus 로고
    • A novel repair enzyme: UvrABC excision nuclease of Escherichia coli cuts a DNa strand on both sides of the damaged region
    • Sancar, A. and Rupp, W.D. (1983) A novel repair enzyme: UvrABC excision nuclease of Escherichia coli cuts a DNA strand on both sides of the damaged region. Cell, 33, 249-260.
    • (1983) Cell , vol.33 , pp. 249-260
    • Sancar, A.1    Rupp, W.D.2
  • 28
    • 0024376689 scopus 로고
    • Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity
    • Seeley, T.W. and Grossman, L. (1989) Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity. Proc. Natl Acad. Sci. USA, 86, 6577-6581.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6577-6581
    • Seeley, T.W.1    Grossman, L.2
  • 29
    • 0025327095 scopus 로고
    • The role of Escherichia coli UvrB in nucleotide excision repair
    • Seeley, T.W. and Grossman, L.J. (1990) The role of Escherichia coli UvrB in nucleotide excision repair. J. Biol. Chem., 265, 7158-7165.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7158-7165
    • Seeley, T.W.1    Grossman, L.J.2
  • 30
    • 0026654184 scopus 로고
    • Electron microscopic study of (A)BC excinulease. DNA is sharply bent in the UvrB-DNA complex
    • Shi, Q., Thresher, R., Sancar, A. and Griffith, J. (1992) Electron microscopic study of (A)BC excinulease. DNA is sharply bent in the UvrB-DNA complex. J. Mol. Biol., 226, 425-432.
    • (1992) J. Mol. Biol. , vol.226 , pp. 425-432
    • Shi, Q.1    Thresher, R.2    Sancar, A.3    Griffith, J.4
  • 31
    • 0025745435 scopus 로고
    • Initiation of the UVrABC nuclease cleavage reaction. Effeciency of incision is not correlated with UvrA binding affinity
    • Snowden, A. and Van Houten, B.J. (1991) Initiation of the UVrABC nuclease cleavage reaction. Effeciency of incision is not correlated with UvrA binding affinity. J. Mol. Biol., 220, 19-33.
    • (1991) J. Mol. Biol. , vol.220 , pp. 19-33
    • Snowden, A.1    Van Houten, B.J.2
  • 32
    • 0343096641 scopus 로고
    • Detection of unusual DNA structures and DNA-protein interactions by diethylpyrocarbonate carbethoxylation
    • Jost, J.P. and Saluz, H.P. (eds), Birkhauser, Basel
    • Toth, M. (1991) Detection of unusual DNA structures and DNA-protein interactions by diethylpyrocarbonate carbethoxylation. In Jost, J.P. and Saluz, H.P. (eds), A Laboratory Guide to In Vitro Studies of Protein-DNA Interactions. Birkhauser, Basel, pp. 145-152.
    • (1991) A Laboratory Guide to in Vitro Studies of Protein-DNA Interactions , pp. 145-152
    • Toth, M.1
  • 33
    • 0025054962 scopus 로고
    • Nucleotide excision repair in Escherichia coli
    • Van Houten, B. (1990) Nucleotide excision repair in Escherichia coli. Microbiol. Rev., 54, 18-51.
    • (1990) Microbiol. Rev. , vol.54 , pp. 18-51
    • Van Houten, B.1
  • 35
    • 0026705750 scopus 로고
    • Analysis of UvrABC endonuclease reaction intermediates on cisplatin-damged DNA using mobility shift gel electrophoresis
    • Visse, R., de Ruijter, M., Moolenaar, G.F. and van de Putte, P. (1992) Analysis of UvrABC endonuclease reaction intermediates on cisplatin-damged DNA using mobility shift gel electrophoresis. J. Biol. Chem., 267, 6736-6742.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6736-6742
    • Visse, R.1    De Ruijter, M.2    Moolenaar, G.F.3    Van De Putte, P.4
  • 36
    • 0027980824 scopus 로고
    • Protein-DNA interactions and alterations in the DNA structure upon UvrB-DNA pre-incision complex formation during nucleotide excision repair in Escherichia coli
    • Visse, R., King, A., Moolenaar, G.F., Goosen, N. and van de Putte, P. (1994) Protein-DNA interactions and alterations in the DNA structure upon UvrB-DNA pre-incision complex formation during nucleotide excision repair in Escherichia coli. Biochemistry, 33, 9881-9888.
    • (1994) Biochemistry , vol.33 , pp. 9881-9888
    • Visse, R.1    King, A.2    Moolenaar, G.F.3    Goosen, N.4    Van De Putte, P.5
  • 37
    • 0023056518 scopus 로고
    • Protein complexes formed during the incision reaction catalyzed by the Escherichia coli UvrABC endonuclease
    • Yeung, A.T., Mattes, W.B. and Grossman, L. (1986a) Protein complexes formed during the incision reaction catalyzed by the Escherichia coli UvrABC endonuclease. Nucleic Acids Res., 14, 2567-2582.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 2567-2582
    • Yeung, A.T.1    Mattes, W.B.2    Grossman, L.3


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