메뉴 건너뛰기




Volumn 5, Issue 4, 2010, Pages 427-436

Hopping enables a DNA repair glycosylase to search both strands and bypass a bound protein

Author keywords

[No Author keywords available]

Indexed keywords

DNA GLYCOSYLTRANSFERASE; DOUBLE STRANDED DNA;

EID: 77951113170     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb1000185     Document Type: Article
Times cited : (60)

References (42)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl, T. (1993) Instability and decay of the primary structure of DNA Nature 362, 709-715
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 0029079249 scopus 로고
    • Processivity of Escherichia coli and rat liver mitochondrial uracil-DNA glycosylase is affected by NaCl concentration
    • Bennett, S. E., Sanderson, R. J., and Mosbaugh, D. W. (1995) Processivity of Escherichia coli and rat liver mitochondrial uracil-DNA glycosylase is affected by NaCl concentration Biochemistry 34, 6109-6119
    • (1995) Biochemistry , vol.34 , pp. 6109-6119
    • Bennett, S.E.1    Sanderson, R.J.2    Mosbaugh, D.W.3
  • 3
    • 33645807371 scopus 로고    scopus 로고
    • A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA
    • Blainey, P. C., van Oijen, A. M., Banerjee, A., Verdine, G. L., and Xie, X. S. (2006) A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA Proc. Natl. Acad. Sci. U.S.A. 103, 5752-5757
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 5752-5757
    • Blainey, P.C.1    Van Oijen, A.M.2    Banerjee, A.3    Verdine, G.L.4    Xie, X.S.5
  • 4
    • 0037469130 scopus 로고    scopus 로고
    • Escherichia coli MutY and Fpg utilize a processive mechanism for target location
    • Francis, A. W. and David, S. S. (2003) Escherichia coli MutY and Fpg utilize a processive mechanism for target location Biochemistry 42, 801-810
    • (2003) Biochemistry , vol.42 , pp. 801-810
    • Francis, A.W.1    David, S.S.2
  • 5
    • 55249097156 scopus 로고    scopus 로고
    • Human alkyladenine DNA glycosylase employs a processive search for DNA damage
    • Hedglin, M. and O'Brien, P. J. (2008) Human alkyladenine DNA glycosylase employs a processive search for DNA damage Biochemistry 47, 11434-11445
    • (2008) Biochemistry , vol.47 , pp. 11434-11445
    • Hedglin, M.1    O'brien, P.J.2
  • 6
    • 0027300148 scopus 로고
    • Processivity of uracil DNA glycosylase
    • Higley, M. and Lloyd, R. S. (1993) Processivity of uracil DNA glycosylase Mutat. Res. 294, 109-116
    • (1993) Mutat. Res. , vol.294 , pp. 109-116
    • Higley, M.1    Lloyd, R.S.2
  • 7
    • 49449088997 scopus 로고    scopus 로고
    • Uracil DNA glycosylase uses DNA hopping and short-range sliding to trap extrahelical uracils
    • Porecha, R. H. and Stivers, J. T. (2008) Uracil DNA glycosylase uses DNA hopping and short-range sliding to trap extrahelical uracils Proc. Natl. Acad. Sci. U.S.A. 105, 10791-10796
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10791-10796
    • Porecha, R.H.1    Stivers, J.T.2
  • 8
    • 50149091510 scopus 로고    scopus 로고
    • Correlated cleavage of damaged DNA by bacterial and human 8-oxoguanine-DNA glycosylases
    • Sidorenko, V. S. and Zharkov, D. O. (2008) Correlated cleavage of damaged DNA by bacterial and human 8-oxoguanine-DNA glycosylases Biochemistry 47, 8970-8976
    • (2008) Biochemistry , vol.47 , pp. 8970-8976
    • Sidorenko, V.S.1    Zharkov, D.O.2
  • 9
    • 0024974966 scopus 로고
    • Biological consequences of a reduction in the non-target DNA scanning capacity of a DNA repair enzyme
    • Dowd, D. R. and Lloyd, R. S. (1989) Biological consequences of a reduction in the non-target DNA scanning capacity of a DNA repair enzyme J. Mol. Biol. 208, 701-707
    • (1989) J. Mol. Biol. , vol.208 , pp. 701-707
    • Dowd, D.R.1    Lloyd, R.S.2
  • 10
    • 0025257431 scopus 로고
    • Biological significance of facilitated diffusion in protein-DNA interactions. Applications to T4 endonuclease V-initiated DNA repair
    • Dowd, D. R. and Lloyd, R. S. (1990) Biological significance of facilitated diffusion in protein-DNA interactions. Applications to T4 endonuclease V-initiated DNA repair J. Biol. Chem. 265, 3424-3431
    • (1990) J. Biol. Chem. , vol.265 , pp. 3424-3431
    • Dowd, D.R.1    Lloyd, R.S.2
  • 11
    • 0029790522 scopus 로고    scopus 로고
    • Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzyme
    • Jeltsch, A., Wenz, C., Stahl, F., and Pingoud, A. (1996) Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzyme EMBO J. 15, 5104-5111
    • (1996) EMBO J. , vol.15 , pp. 5104-5111
    • Jeltsch, A.1    Wenz, C.2    Stahl, F.3    Pingoud, A.4
  • 12
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory
    • Berg, O. G., Winter, R. B., and von Hippel, P. H. (1981) Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory Biochemistry 20, 6929-6948
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    Von Hippel, P.H.3
  • 13
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNA-binding proteins find their targets?
    • Halford, S. E. and Marko, J. F. (2004) How do site-specific DNA-binding proteins find their targets? Nucleic Acids Res. 32, 3040-3052
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 14
    • 49449107340 scopus 로고    scopus 로고
    • Visualizing one-dimensional diffusion of proteins along DNA
    • Gorman, J. and Greene, E. C. (2008) Visualizing one-dimensional diffusion of proteins along DNA Nat. Struct. Mol. Biol. 15, 768-774
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 768-774
    • Gorman, J.1    Greene, E.C.2
  • 17
    • 0037451299 scopus 로고    scopus 로고
    • Protein motion from non-specific to specific DNA by three-dimensional routes aided by supercoiling
    • Gowers, D. M. and Halford, S. E. (2003) Protein motion from non-specific to specific DNA by three-dimensional routes aided by supercoiling EMBO J. 22, 1410-1418
    • (2003) EMBO J. , vol.22 , pp. 1410-1418
    • Gowers, D.M.1    Halford, S.E.2
  • 18
    • 27644460480 scopus 로고    scopus 로고
    • Measurement of the contributions of 1D and 3D pathways to the translocation of a protein along DNA
    • Gowers, D. M., Wilson, G. G., and Halford, S. E. (2005) Measurement of the contributions of 1D and 3D pathways to the translocation of a protein along DNA Proc. Natl. Acad. Sci. U.S.A. 102, 15883-15888
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15883-15888
    • Gowers, D.M.1    Wilson, G.G.2    Halford, S.E.3
  • 19
    • 65549171477 scopus 로고    scopus 로고
    • An end to 40 years of mistakes in DNA-protein association kinetics?
    • Halford, S. E. (2009) An end to 40 years of mistakes in DNA-protein association kinetics? Biochem. Soc. Trans. 37, 343-348
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 343-348
    • Halford, S.E.1
  • 20
    • 0036656143 scopus 로고    scopus 로고
    • How to get from A to B: Strategies for analysing protein motion on DNA
    • Halford, S. E. and Szczelkun, M. D. (2002) How to get from A to B: strategies for analysing protein motion on DNA Eur. Biophys. J. 31, 257-267
    • (2002) Eur. Biophys. J. , vol.31 , pp. 257-267
    • Halford, S.E.1    Szczelkun, M.D.2
  • 22
    • 0034387984 scopus 로고    scopus 로고
    • One- and three-dimensional pathways for proteins to reach specific DNA sites
    • Stanford, N. P., Szczelkun, M. D., Marko, J. F., and Halford, S. E. (2000) One- and three-dimensional pathways for proteins to reach specific DNA sites EMBO J. 19, 6546-6557
    • (2000) EMBO J. , vol.19 , pp. 6546-6557
    • Stanford, N.P.1    Szczelkun, M.D.2    Marko, J.F.3    Halford, S.E.4
  • 23
    • 6944221433 scopus 로고    scopus 로고
    • RNA polymerase can track a DNA groove during promoter search
    • Sakata-Sogawa, K. and Shimamoto, N. (2004) RNA polymerase can track a DNA groove during promoter search Proc. Natl. Acad. Sci. U.S.A. 101, 14731-14735
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14731-14735
    • Sakata-Sogawa, K.1    Shimamoto, N.2
  • 24
    • 65549117030 scopus 로고    scopus 로고
    • Using the bias from flow to elucidate single DNA repair protein sliding and interactions with DNA
    • Lin, Y., Zhao, T., Jian, X., Farooqui, Z., Qu, X., He, C., Dinner, A. R., and Scherer, N. F. (2009) Using the bias from flow to elucidate single DNA repair protein sliding and interactions with DNA Biophys. J. 96, 1911-1917
    • (2009) Biophys. J. , vol.96 , pp. 1911-1917
    • Lin, Y.1    Zhao, T.2    Jian, X.3    Farooqui, Z.4    Qu, X.5    He, C.6    Dinner, A.R.7    Scherer, N.F.8
  • 25
    • 0028782732 scopus 로고
    • Pausing of the restriction endonuclease EcoRI during linear diffusion on DNA
    • Jeltsch, A., Alves, J., Wolfes, H., Maass, G., and Pingoud, A. (1994) Pausing of the restriction endonuclease EcoRI during linear diffusion on DNA Biochemistry 33, 10215-10219 (Pubitemid 2133358)
    • (1994) Biochemistry , vol.33 , Issue.34 , pp. 10215-10219
    • Jeltsch, A.1    Alves, J.2    Wolfes, H.3    Maass, G.4    Pingoud, A.5
  • 26
    • 24044492241 scopus 로고    scopus 로고
    • The DNA trackwalkers: Principles of lesion search and recognition by DNA glycosylases
    • Zharkov, D. O. and Grollman, A. P. (2005) The DNA trackwalkers: principles of lesion search and recognition by DNA glycosylases Mutat. Res. 577, 24-54
    • (2005) Mutat. Res. , vol.577 , pp. 24-54
    • Zharkov, D.O.1    Grollman, A.P.2
  • 28
    • 73149092550 scopus 로고    scopus 로고
    • Kinetic mechanism for the flipping and excision of 1,N(6)-ethenoadenine by human alkyladenine DNA glycosylase
    • Wolfe, A. E. and O'Brien, P. J. (2009) Kinetic mechanism for the flipping and excision of 1,N(6)-ethenoadenine by human alkyladenine DNA glycosylase Biochemistry 48, 11357-11369
    • (2009) Biochemistry , vol.48 , pp. 11357-11369
    • Wolfe, A.E.1    O'brien, P.J.2
  • 29
    • 67649592232 scopus 로고    scopus 로고
    • Human AP endonuclease i stimulates multiple-turnover base excision by alkyladenine DNA glycosylase
    • Baldwin, M. R. and O'Brien, P. J. (2009) Human AP endonuclease I stimulates multiple-turnover base excision by alkyladenine DNA glycosylase Biochemistry 48, 6022-6033
    • (2009) Biochemistry , vol.48 , pp. 6022-6033
    • Baldwin, M.R.1    O'brien, P.J.2
  • 30
    • 0029121733 scopus 로고
    • Exceptionally stable nucleic acid hairpins
    • Varani, G. (1995) Exceptionally stable nucleic acid hairpins Annu. Rev. Biophys. Biomol. Struct. 24, 379-404
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 379-404
    • Varani, G.1
  • 31
    • 34547882768 scopus 로고    scopus 로고
    • Protein roadblocks and helix discontinuities are barriers to the initiation of mismatch repair
    • Pluciennik, A. and Modrich, P. (2007) Protein roadblocks and helix discontinuities are barriers to the initiation of mismatch repair Proc. Natl. Acad. Sci. U.S.A. 104, 12709-12713
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12709-12713
    • Pluciennik, A.1    Modrich, P.2
  • 32
    • 0025309753 scopus 로고
    • Elongation by Escherichia coli RNA polymerase is blocked in vitro by a site-specific DNA binding protein
    • Pavco, P. A. and Steege, D. A. (1990) Elongation by Escherichia coli RNA polymerase is blocked in vitro by a site-specific DNA binding protein J. Biol. Chem. 265, 9960-9969
    • (1990) J. Biol. Chem. , vol.265 , pp. 9960-9969
    • Pavco, P.A.1    Steege, D.A.2
  • 33
    • 0023771741 scopus 로고
    • Empirical estimation of protein-induced DNA bending angles: Applications to lambda site-specific recombination complexes
    • Thompson, J. F. and Landy, A. (1988) Empirical estimation of protein-induced DNA bending angles: applications to lambda site-specific recombination complexes Nucleic Acids Res. 16, 9687-9705
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9687-9705
    • Thompson, J.F.1    Landy, A.2
  • 34
    • 0021112461 scopus 로고
    • Thermodynamic parameters governing interaction of EcoRI endonuclease with specific and nonspecific DNA sequences
    • Terry, B. J., Jack, W. E., Rubin, R. A., and Modrich, P. (1983) Thermodynamic parameters governing interaction of EcoRI endonuclease with specific and nonspecific DNA sequences J. Biol. Chem. 258, 9820-9825
    • (1983) J. Biol. Chem. , vol.258 , pp. 9820-9825
    • Terry, B.J.1    Jack, W.E.2    Rubin, R.A.3    Modrich, P.4
  • 35
    • 0020160863 scopus 로고
    • Involvement of outside DNA sequences in the major kinetic path by which EcoRI endonuclease locates and leaves its recognition sequence
    • Jack, W. E., Terry, B. J., and Modrich, P. (1982) Involvement of outside DNA sequences in the major kinetic path by which EcoRI endonuclease locates and leaves its recognition sequence Proc. Natl. Acad. Sci. U.S.A. 79, 4010-4014
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 4010-4014
    • Jack, W.E.1    Terry, B.J.2    Modrich, P.3
  • 36
    • 0035883723 scopus 로고    scopus 로고
    • Structure and function of type II restriction endonucleases
    • Pingoud, A. and Jeltsch, A. (2001) Structure and function of type II restriction endonucleases Nucleic Acids Res. 29, 3705-3727
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3705-3727
    • Pingoud, A.1    Jeltsch, A.2
  • 37
    • 73149119125 scopus 로고    scopus 로고
    • Diffusion of the restriction nuclease EcoRI along DNA
    • Rau, D. C. and Sidorova, N. Y. (2010) Diffusion of the restriction nuclease EcoRI along DNA J. Mol. Biol. 395, 408-416
    • (2010) J. Mol. Biol. , vol.395 , pp. 408-416
    • Rau, D.C.1    Sidorova, N.Y.2
  • 38
    • 0033527546 scopus 로고    scopus 로고
    • The kinetic mechanism of EcoRI endonuclease
    • Wright, D. J., Jack, W. E., and Modrich, P. (1999) The kinetic mechanism of EcoRI endonuclease J. Biol. Chem. 274, 31896-31902
    • (1999) J. Biol. Chem. , vol.274 , pp. 31896-31902
    • Wright, D.J.1    Jack, W.E.2    Modrich, P.3
  • 39
    • 58149345492 scopus 로고    scopus 로고
    • Protein sliding along DNA: Dynamics and structural characterization
    • Givaty, O. and Levy, Y. (2009) Protein sliding along DNA: dynamics and structural characterization J. Mol. Biol. 385, 1087-1097
    • (2009) J. Mol. Biol. , vol.385 , pp. 1087-1097
    • Givaty, O.1    Levy, Y.2
  • 40
    • 0021161793 scopus 로고
    • Isolation of gram quantities of EcoRI restriction and modification enzymes from an overproducing strain
    • Cheng, S. C., Kim, R., King, K., Kim, S. H., and Modrich, P. (1984) Isolation of gram quantities of EcoRI restriction and modification enzymes from an overproducing strain J. Biol. Chem. 259, 11571-11575
    • (1984) J. Biol. Chem. , vol.259 , pp. 11571-11575
    • Cheng, S.C.1    Kim, R.2    King, K.3    Kim, S.H.4    Modrich, P.5
  • 41
    • 0025187081 scopus 로고
    • Refinement of Eco RI endonuclease crystal structure: A revised protein chain tracing
    • Kim, Y. C., Grable, J. C., Love, R., Greene, P. J., and Rosenberg, J. M. (1990) Refinement of Eco RI endonuclease crystal structure: a revised protein chain tracing Science 249, 1307-1309
    • (1990) Science , vol.249 , pp. 1307-1309
    • Kim, Y.C.1    Grable, J.C.2    Love, R.3    Greene, P.J.4    Rosenberg, J.M.5
  • 42
    • 0034610336 scopus 로고    scopus 로고
    • Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG
    • Lau, A. Y., Wyatt, M. D., Glassner, B. J., Samson, L. D., and Ellenberger, T. (2000) Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG Proc. Natl. Acad. Sci. U.S.A. 97, 13573-13578
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13573-13578
    • Lau, A.Y.1    Wyatt, M.D.2    Glassner, B.J.3    Samson, L.D.4    Ellenberger, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.