메뉴 건너뛰기




Volumn 42, Issue 14, 2014, Pages 9295-9303

Microscopic mechanism of DNA damage searching by hOGG1

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA GLYCOSYLTRANSFERASE; HUMAN 8 OXOGUANINE DNA GLYCOSYLASE 1; PHOSPHATE; UNCLASSIFIED DRUG;

EID: 84906240225     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku621     Document Type: Article
Times cited : (36)

References (42)
  • 1
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani, S., Takeshita, M. and Grollman, A.P. (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
  • 2
    • 4544273926 scopus 로고    scopus 로고
    • Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase
    • Hsu, G.W., Ober, M., Carell, T. and Beese, L.S. (2004) Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Nature, 431, 217-221.
    • (2004) Nature , vol.431 , pp. 217-221
    • Hsu, G.W.1    Ober, M.2    Carell, T.3    Beese, L.S.4
  • 3
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • David, S.S., O'Shea, V.L. and Kundu, S. (2007) Base-excision repair of oxidative DNA damage. Nature, 447, 941-950.
    • (2007) Nature , vol.447 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 5
    • 77953654163 scopus 로고    scopus 로고
    • Detection of damaged DNA bases by DNA glycosylase enzymes
    • Friedman, J.I. and Stivers, J.T. (2010) Detection of damaged DNA bases by DNA glycosylase enzymes. Biochemistry, 49, 4957-4967.
    • (2010) Biochemistry , vol.49 , pp. 4957-4967
    • Friedman, J.I.1    Stivers, J.T.2
  • 6
    • 38849207616 scopus 로고    scopus 로고
    • Extrahelical damaged base recognition by DNA glycosylase enzymes
    • Stivers, J.T. (2008) Extrahelical damaged base recognition by DNA glycosylase enzymes. Chemistry, 14, 786-793.
    • (2008) Chemistry , vol.14 , pp. 786-793
    • Stivers, J.T.1
  • 7
    • 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
  • 8
    • 79957549084 scopus 로고    scopus 로고
    • Dancing on DNA: Kinetic aspects of search processes on DNA
    • Tafvizi, A., Mirny, L.A. and van Oijen, A.M. (2011) Dancing on DNA: kinetic aspects of search processes on DNA. Chemphyschem, 12, 1481-1489.
    • (2011) Chemphyschem , vol.12 , pp. 1481-1489
    • Tafvizi, A.1    Mirny, L.A.2    Van Oijen, A.M.3
  • 9
    • 0019867850 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: Kinetic measurements and conclusions
    • Winter, R.B., Berg, O.G. and Hippel, P.H. (1981) Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: kinetic measurements and conclusions. Biochemistry, 20, 6961-6977.
    • (1981) Biochemistry , vol.20 , pp. 6961-6977
    • Winter, R.B.1    Berg, O.G.2    Hippel, P.H.3
  • 10
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory
    • Berg, O.G., Winter, R.B. and 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    Hippel, P.H.3
  • 11
    • 0019816896 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 2. The Escherichia coli lac repressor-operator interaction: Equilibrium measurements
    • Winter, R.B. and Hippel, P.H. (1981) Diffusion-driven mechanisms of protein translocation on nucleic acids. 2. The Escherichia coli lac repressor-operator interaction: equilibrium measurements. Biochemistry, 20, 6948-6960.
    • (1981) Biochemistry , vol.20 , pp. 6948-6960
    • Winter, R.B.1    Hippel, P.H.2
  • 12
    • 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
  • 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
  • 15
    • 84890531231 scopus 로고    scopus 로고
    • Exploring bacterial cell biology with single-molecule tracking and super-resolution imaging
    • Gahlmann, A. and Moerner, W.E. (2014) Exploring bacterial cell biology with single-molecule tracking and super-resolution imaging. Nat. Rev. Microbiol., 12, 9-22.
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 9-22
    • Gahlmann, A.1    Moerner, W.E.2
  • 16
    • 80053206516 scopus 로고    scopus 로고
    • Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA
    • Dunn, A.R., Kad, N.M., Nelson, S.R., Warshaw, D.M. and Wallace, S.S. (2011) Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA. Nucleic Acids Res., 39, 7487-7498.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 7487-7498
    • Dunn, A.R.1    Kad, N.M.2    Nelson, S.R.3    Warshaw, D.M.4    Wallace, S.S.5
  • 17
    • 84856117713 scopus 로고    scopus 로고
    • Timing facilitated site transfer of an enzyme on DNA
    • Schonhoft, J.D. and Stivers, J.T. (2012) Timing facilitated site transfer of an enzyme on DNA. Nat. Chem. Biol., 8, 205-210.
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 205-210
    • Schonhoft, J.D.1    Stivers, J.T.2
  • 18
    • 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
  • 19
    • 0141790433 scopus 로고    scopus 로고
    • Recognition and removal of oxidized guanines in duplex DNA by the base excision repair enzymes hOGG1, yOGG1, and yOGG2
    • Leipold, M.D., Workman, H., Muller, J.G., Burrows, C.J. and David, S.S. (2003) Recognition and removal of oxidized guanines in duplex DNA by the base excision repair enzymes hOGG1, yOGG1, and yOGG2. Biochemistry, 42, 11373-11381.
    • (2003) Biochemistry , vol.42 , pp. 11373-11381
    • Leipold, M.D.1    Workman, H.2    Muller, J.G.3    Burrows, C.J.4    David, S.S.5
  • 20
    • 40849135868 scopus 로고    scopus 로고
    • Potent inhibition of human apurinic/apyrimidinic endonuclease 1 by arylstibonic acids
    • Seiple, L.A., Cardellina, J.H., Akee, R. and Stivers, J.T. (2008) Potent inhibition of human apurinic/apyrimidinic endonuclease 1 by arylstibonic acids. Mol. Pharmacol., 73, 669-677.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 669-677
    • Seiple, L.A.1    Cardellina, J.H.2    Akee, R.3    Stivers, J.T.4
  • 21
    • 0022381905 scopus 로고
    • Facilitated diffusion during catalysis by EcoRI endonuclease. Nonspecific interactions in EcoRI catalysis
    • Terry, B.J., Jack, W.E. and Modrich, P. (1985) Facilitated diffusion during catalysis by EcoRI endonuclease. Nonspecific interactions in EcoRI catalysis. J. Biol. Chem., 260, 13130-13137.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13130-13137
    • Terry, B.J.1    Jack, W.E.2    Modrich, P.3
  • 22
    • 34247862129 scopus 로고    scopus 로고
    • Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations
    • Radom, C.T., Banerjee, A. and Verdine, G.L. (2007) Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations. J. Biol. Chem., 282, 9182-9194.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9182-9194
    • Radom, C.T.1    Banerjee, A.2    Verdine, G.L.3
  • 23
    • 84876279199 scopus 로고    scopus 로고
    • DNA translocation by human uracil DNA glycosylase: Role of DNA phosphate charge
    • Schonhoft, J.D., Kosowicz, J.G. and Stivers, J.T. (2013) DNA translocation by human uracil DNA glycosylase: role of DNA phosphate charge. Biochemistry, 52, 2526-2535.
    • (2013) Biochemistry , vol.52 , pp. 2526-2535
    • Schonhoft, J.D.1    Kosowicz, J.G.2    Stivers, J.T.3
  • 24
    • 84876234449 scopus 로고    scopus 로고
    • DNA translocation by human uracil DNA glycosylase: The case of single-stranded DNA and clustered uracils
    • Schonhoft, J.D. and Stivers, J.T. (2013) DNA translocation by human uracil DNA glycosylase: the case of single-stranded DNA and clustered uracils. Biochemistry, 52, 2536-2544.
    • (2013) Biochemistry , vol.52 , pp. 2536-2544
    • Schonhoft, J.D.1    Stivers, J.T.2
  • 25
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner, S.D., Norman, D.P. and Verdine, G.L. (2000) Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature, 403, 859-866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.2    Verdine, G.L.3
  • 26
    • 15844379169 scopus 로고    scopus 로고
    • Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA
    • Banerjee, A., Yang, W., Karplus, M. and Verdine, G.L. (2005) Structure of a repair enzyme interrogating undamaged DNA elucidates recognition of damaged DNA. Nature, 434, 612-618.
    • (2005) Nature , vol.434 , pp. 612-618
    • Banerjee, A.1    Yang, W.2    Karplus, M.3    Verdine, G.L.4
  • 27
    • 77951113170 scopus 로고    scopus 로고
    • Hopping enables a DNA repair glycosylase to search both strands and bypass a bound protein
    • Hedglin, M. and O'Brien, P.J. (2010) Hopping enables a DNA repair glycosylase to search both strands and bypass a bound protein. ACS Chem. Biol., 5, 427-436.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 427-436
    • Hedglin, M.1    O'Brien, P.J.2
  • 28
    • 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
  • 31
    • 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
  • 32
    • 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
  • 37
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • Hippel, P.H. and Berg, O.G. (1989) Facilitated target location in biological systems. J. Biol. Chem., 264, 675-678.
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • Hippel, P.H.1    Berg, O.G.2
  • 38
    • 0035098395 scopus 로고    scopus 로고
    • Rates of base excision repair are not solely dependent on levels of initiating enzymes
    • Cappelli, E. (2001) Rates of base excision repair are not solely dependent on levels of initiating enzymes. Carcinogenesis, 22, 387-393.
    • (2001) Carcinogenesis , vol.22 , pp. 387-393
    • Cappelli, E.1
  • 39
    • 65249099497 scopus 로고    scopus 로고
    • Fundamental aspects of protein-protein association kinetics
    • Schreiber, G., Haran, G. and Zhou, H.X. (2009) Fundamental aspects of protein-protein association kinetics. Chem. Rev., 109, 839-860.
    • (2009) Chem. Rev. , vol.109 , pp. 839-860
    • Schreiber, G.1    Haran, G.2    Zhou, H.X.3
  • 40
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • Zhou, H.X., Rivas, G. and Minton, A.P. (2008) Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu. Rev. Biophys., 37, 375-397.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 41
    • 0036009327 scopus 로고    scopus 로고
    • Direct visualization of a DNA glycosylase searching for damage
    • Chen, L., Haushalter, K.A., Lieber, C.M. and Verdine, G.L. (2002) Direct visualization of a DNA glycosylase searching for damage. Chem. Biol., 9, 345-350.
    • (2002) Chem. Biol. , vol.9 , pp. 345-350
    • Chen, L.1    Haushalter, K.A.2    Lieber, C.M.3    Verdine, G.L.4
  • 42
    • 33847057368 scopus 로고    scopus 로고
    • Interactions of human 8-oxoguanine-DNA glycosylase with singleand double-stranded DNA
    • Kirpota, O.O., Zharkov, D.O., Buneva, V.N. and Nevinskii, G.A. (2006) [Interactions of human 8-oxoguanine-DNA glycosylase with singleand double-stranded DNA]. Mol. Biol. (Mosk.), 40, 1055-1063.
    • (2006) Mol. Biol. (Mosk.) , vol.40 , pp. 1055-1063
    • Kirpota, O.O.1    Zharkov, D.O.2    Buneva, V.N.3    Nevinskii, G.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.