메뉴 건너뛰기




Volumn 18, Issue 17, 1999, Pages 4889-4901

Strand opening by the UvrA2B complex allows dynamic recognition of DNA damage

Author keywords

DNA; Recognition; Repair; Structures; UvrABC

Indexed keywords

ABC EXCINUCLEASE; DNA; DOUBLE STRANDED DNA; SINGLE STRANDED DNA;

EID: 0033199492     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.17.4889     Document Type: Article
Times cited : (94)

References (39)
  • 1
    • 0024095899 scopus 로고
    • Localized melting and structural changes in the SV40 origin of replication induced by T antigen
    • Borowiec, J.A., Dean, F.B., Bullock, P.A. and Hurwitz, J. (1988) Localized melting and structural changes in the SV40 origin of replication induced by T antigen. EMBO J., 7, 3149-3158.
    • (1988) EMBO J. , vol.7 , pp. 3149-3158
    • Borowiec, J.A.1    Dean, F.B.2    Bullock, P.A.3    Hurwitz, J.4
  • 2
    • 0027215240 scopus 로고
    • Solution conformation of the (+)-cis-anti-[BP]dG adduct in a DNA duplex: Intercalation of the covalently attached benzo[a]pyrenyl ring into the helix and displacement of the modified deoxyguanosine
    • Cosman, M. et al. (1993) Solution conformation of the (+)-cis-anti-[BP]dG adduct in a DNA duplex: intercalation of the covalently attached benzo[a]pyrenyl ring into the helix and displacement of the modified deoxyguanosine. Biochemistry, 32, 4146-4155.
    • (1993) Biochemistry , vol.32 , pp. 4146-4155
    • Cosman, M.1
  • 3
    • 0031013308 scopus 로고    scopus 로고
    • Open complex formation around a lesion during nucleotide repair provides a structure for cleavage by human XPG protein
    • Evans, E., Fellows, J., Coffer, A. and Wood, R.D. (1997) Open complex formation around a lesion during nucleotide repair provides a structure for cleavage by human XPG protein. EMBO J., 16, 625-638.
    • (1997) EMBO J. , vol.16 , pp. 625-638
    • Evans, E.1    Fellows, J.2    Coffer, A.3    Wood, R.D.4
  • 4
    • 0031046737 scopus 로고    scopus 로고
    • UvrAB activity at a damaged DNA site: Is unpaired DNA present?
    • Gordienko, I. and Rupp, W.D. (1997) UvrAB activity at a damaged DNA site: is unpaired DNA present? EMBO J., 16, 880-888.
    • (1997) EMBO J. , vol.16 , pp. 880-888
    • Gordienko, I.1    Rupp, W.D.2
  • 5
    • 0344765478 scopus 로고    scopus 로고
    • A specific 3′ exonuclease activity of UvrABC
    • Gordienko, I. and Rupp, W.D. (1998) A specific 3′ exonuclease activity of UvrABC. EMBO J., 17, 626-633.
    • (1998) EMBO J. , vol.17 , pp. 626-633
    • Gordienko, I.1    Rupp, W.D.2
  • 6
    • 0023728921 scopus 로고
    • Repair of DNA-containing pyrimidine dimers
    • Grossman, L., Caron, P.R., Mazur, S.J. and Oh, E.Y. (1988) Repair of DNA-containing pyrimidine dimers. FASEB J., 2, 2696-2701.
    • (1988) FASEB J. , vol.2 , pp. 2696-2701
    • Grossman, L.1    Caron, P.R.2    Mazur, S.J.3    Oh, E.Y.4
  • 7
    • 0028925960 scopus 로고
    • Structure and function of the UvrB protein
    • Hsu, D.S., Kim, S.-T., Sun, Q. and Sancar, A. (1995) Structure and function of the UvrB protein. J. Biol. Chem., 270, 8319-8327.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8319-8327
    • Hsu, D.S.1    Kim, S.-T.2    Sun, Q.3    Sancar, A.4
  • 8
    • 77956933603 scopus 로고
    • Deoxyribonuclease I
    • Laskowski, M. (1971) Deoxyribonuclease I. Enzymes, 4, 289-311.
    • (1971) Enzymes , vol.4 , pp. 289-311
    • Laskowski, M.1
  • 10
    • 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
  • 12
    • 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 preincision 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 preincision complex. J. Mol. Biol., 240, 294-307.
    • (1994) J. Mol. Biol. , vol.240 , pp. 294-307
    • Moolenaar, G.F.1    Visse, R.2    Ortiz-Buysse, M.3    Goosen, N.4    Van De Putte, P.5
  • 13
    • 0029557494 scopus 로고
    • The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the pre-incision complex but not the catalytic site for 3′ incision
    • Moolenaar, G.F., Franken, K.L.M.C., Dijkstra, D.M., Thomas-Oates, J.E., Visse, R., van de Putte, P. and Goosen, N. (1995) The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the pre-incision complex but not the catalytic site for 3′ incision. J. Biol. Chem., 270, 30508-30515.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30508-30515
    • Moolenaar, G.F.1    Franken, K.L.M.C.2    Dijkstra, D.M.3    Thomas-Oates, J.E.4    Visse, R.5    Van De Putte, P.6    Goosen, N.7
  • 14
    • 0031423316 scopus 로고    scopus 로고
    • Function of the homologous regions of the Escherichia coli DNA excision repair proteins UvrB and UvrC in stabilization of the UvrBC-DNA complex and in 3′ incision
    • Moolenaar, G.F., Franken, K.L.M.C., van de Putte, P. and Goosen, N. (1997) Function of the homologous regions of the Escherichia coli DNA excision repair proteins UvrB and UvrC in stabilization of the UvrBC-DNA complex and in 3′ incision. Mutat. Res., 385, 195-203.
    • (1997) Mutat. Res. , vol.385 , pp. 195-203
    • Moolenaar, G.F.1    Franken, K.L.M.C.2    Van De Putte, P.3    Goosen, N.4
  • 15
    • 0032567471 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli damageindependent UvrbC endonuclease activity
    • Moolenaar, G.F., Bazuine, M., van Knippenberg, I.C, Visse, R. and Goosen, N. (1998) Characterization of the Escherichia coli damageindependent UvrBC endonuclease activity. J. Biol. Chem., 273, 34896-34903.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34896-34903
    • Moolenaar, G.F.1    Bazuine, M.2    Van Knippenberg, I.C.3    Visse, R.4    Goosen, N.5
  • 16
    • 0030716255 scopus 로고    scopus 로고
    • Characterization of reaction intermediates of human excision repair nuclease
    • Mu, D., Wakasugi, M., Hsu, D.S. and Sancar, A. (1997) Characterization of reaction intermediates of human excision repair nuclease. J. Biol. Chem., 272, 28971-28979.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28971-28979
    • Mu, D.1    Wakasugi, M.2    Hsu, D.S.3    Sancar, A.4
  • 17
    • 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
  • 18
    • 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
  • 19
    • 0024570144 scopus 로고
    • Characterization of the helicase activity of the Escherichia coli UvrAB protein complex
    • Oh, E.Y. and Grossman, L. (1989) Characterization of the helicase activity of the Escherichia coli UvrAB protein complex. J. Biol. Chem., 264, 1336-1343.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1336-1343
    • Oh, E.Y.1    Grossman, L.2
  • 20
    • 0024371067 scopus 로고
    • The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex
    • Orren, D.K. and Sancar, A. (1989) The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex. Proc. Natl Acad Sci. USA, 86, 5237-5241.
    • (1989) Proc. Natl Acad Sci. USA , vol.86 , pp. 5237-5241
    • Orren, D.K.1    Sancar, A.2
  • 21
    • 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
  • 22
    • 0026595890 scopus 로고
    • Post-incision steps of nucleotide excision repair in Escherichia coli
    • Orren D.K., Selby, C.P, Hearst, J.E. and Sancar, A. (1992) Post-incision steps of nucleotide excision repair in Escherichia coli. 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
  • 23
    • 0029892790 scopus 로고    scopus 로고
    • DNA excision repair
    • Sancar, A. (1996) DNA excision repair. Annu. Rev. Biochem., 65, 43-48.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 43-48
    • Sancar, A.1
  • 24
    • 0027522357 scopus 로고
    • Molecular matchmakers
    • Sancar, A. and Hearst, J.E. (1993) Molecular matchmakers. Science, 259, 1415-1420.
    • (1993) Science , vol.259 , pp. 1415-1420
    • Sancar, A.1    Hearst, J.E.2
  • 25
    • 0025327095 scopus 로고
    • The role of Escherichia coli UvrB in nucleotide excision repair
    • Seeley, T.W. and Grossman, L. (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.2
  • 26
    • 0026654184 scopus 로고
    • Electron microscopic study of (A)BC excinuclease. DNA is sharply bent in the UvrB-DNA complex
    • Shi, Q., Thresher, R., Sancar,A. and Griffith,:. (1992) Electron microscopic study of (A)BC excinuclease. 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
  • 27
    • 0022476864 scopus 로고
    • Structure of DNase I at 2.0 Å resolution suggests a mechanism for binding to and cutting DNA
    • Suck, D. and Oefner, C. (1986) Structure of DNase I at 2.0 Å resolution suggests a mechanism for binding to and cutting DNA. Nature, 321, 620-625.
    • (1986) Nature , vol.321 , pp. 620-625
    • Suck, D.1    Oefner, C.2
  • 29
    • 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
  • 30
    • 0028061328 scopus 로고
    • Nucleotide excision repair in E.Coli
    • Van Houten, B. and McCullough, A. (1994) Nucleotide excision repair in E.coli. Ann. NY Acad. Sci., 726, 236-251.
    • (1994) Ann. NY Acad. Sci. , vol.726 , pp. 236-251
    • Van Houten, B.1    McCullough, A.2
  • 31
    • 0027350849 scopus 로고
    • Mechanism of action of the Escherichia coli UvrABC nuclease: Clues to the damage recognition problem
    • Van Houten, B. and Snowden, A. (1993) Mechanism of action of the Escherichia coli UvrABC nuclease: clues to the damage recognition problem. BioEssays, 15, 51-59.
    • (1993) BioEssays , vol.15 , pp. 51-59
    • Van Houten, B.1    Snowden, A.2
  • 32
    • 0023024986 scopus 로고
    • Construction of DNA substrates modified with psoralen at a unique site and study of the action mechanism of ABC excinuclease on these uniformly modified substrates
    • Van Houten, B., Gamper, H., Hearst, J.E. and Sancar, A. (1986) Construction of DNA substrates modified with psoralen at a unique site and study of the action mechanism of ABC excinuclease on these uniformly modified substrates. J. Biol. Chem., 261, 14135-14141.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14135-14141
    • Van Houten, B.1    Gamper, H.2    Hearst, J.E.3    Sancar, A.4
  • 33
    • 0027980824 scopus 로고
    • Protein-DNA interactions and alterations in the DNA structure upon UvrB-DNA preincision 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 preincision 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
  • 34
    • 0032499719 scopus 로고    scopus 로고
    • Assembly, subunit composition and footprint of human DNA repair excision nuclease
    • Wakasugi, M. and Sancar, A. (1998) Assembly, subunit composition and footprint of human DNA repair excision nuclease. Proc. Natl Acad. Sci. USA, 95, 6669-6674.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6669-6674
    • Wakasugi, M.1    Sancar, A.2
  • 35
    • 0030768038 scopus 로고    scopus 로고
    • Nucleotide excision repair in mammalian cells
    • Wood, R. (1997) Nucleotide excision repair in mammalian cells. J. Biol. Chem., 272, 23465-23468.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23465-23468
    • Wood, R.1
  • 36
    • 0028784624 scopus 로고
    • Interaction of the UvrABC nuclease system with a DNA duplex containing a single stereoisomer of dG-( + )-or dG-(-)-anti-BPDE
    • Zou,Y., Liu, T.M., Geacintov, N.E. and Van Houten, B. (1995) Interaction of the UvrABC nuclease system with a DNA duplex containing a single stereoisomer of dG-( + )-or dG-(-)-anti-BPDE. Biochemistry, 34, 13582-13593.
    • (1995) Biochemistry , vol.34 , pp. 13582-13593
    • Liu, T.M.1    Geacintov, N.E.2    Van Houten, B.3
  • 37
    • 0031046795 scopus 로고    scopus 로고
    • Formalion of DNA repair intermediates and incision by the ATP-dependent UvrB-UvrC endonuclease
    • Zou, Y., Walker, R., Bassett, H., Geacintov, N.E. and Van Houten, B. (1997) Formalion of DNA repair intermediates and incision by the ATP-dependent UvrB-UvrC endonuclease. J. Biol. Chem., 272, 4820-4827.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4820-4827
    • Zou, Y.1    Walker, R.2    Bassett, H.3    Geacintov, N.E.4    Van Houten, B.5
  • 38
    • 0032493790 scopus 로고    scopus 로고
    • Hydrophobic forces dominate the thermodynamic characteristics of UvrA-DNA damage interactions
    • Zou, Y., Bassett, H., Walker, R., Bishop. A., Amin, S., Geacintov, N.E. and Van Houten, B. (1998a) Hydrophobic forces dominate the thermodynamic characteristics of UvrA-DNA damage interactions. J. Mol. Biol., 281, 107-119.
    • (1998) J. Mol. Biol. , vol.281 , pp. 107-119
    • Zou, Y.1    Bassett, H.2    Walker, R.3    Bishop, A.4    Amin, S.5    Geacintov, N.E.6    Van Houten, B.7
  • 39
    • 0032557562 scopus 로고    scopus 로고
    • Involvement of molecular chaperonins in nucleotide excision repair. Dnak leads to increased thermal stability of UvrA, catalytic UvrB loading, enhanced repair and increased UV resistance
    • Zou, Y., Crowley, D.J. and Van Houten, B. (1998b) Involvement of molecular chaperonins in nucleotide excision repair. Dnak leads to increased thermal stability of UvrA, catalytic UvrB loading, enhanced repair and increased UV resistance. J. Biol. Chem., 273, 12887-12892.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12887-12892
    • Zou, Y.1    Crowley, D.J.2    Van Houten, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.