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Volumn 37, Issue 18, 2009, Pages 6161-6173

Mechanism of DNA substrate recognition by the mammalian DNA repair enzyme, Polynucleotide Kinase

Author keywords

[No Author keywords available]

Indexed keywords

POLYNUCLEOTIDE 5' HYDROXYL KINASE;

EID: 70350690563     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp597     Document Type: Article
Times cited : (47)

References (45)
  • 1
    • 0037133684 scopus 로고    scopus 로고
    • Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA
    • Hazra,T.K., Izumi,T., Boldogh,I., Imhoff,B., Kow,Y.W., Jaruga,P., Dizdaroglu,M. and Mitra,S. (2002) Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA. Proc. Natl Acad. Sci. USA, 99, 3523-3528.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3523-3528
    • Hazra, T.K.1    Izumi, T.2    Boldogh, I.3    Imhoff, B.4    Kow, Y.W.5    Jaruga, P.6    Dizdaroglu, M.7    Mitra, S.8
  • 2
    • 0344009629 scopus 로고    scopus 로고
    • DNase II: Genes, enzymes and function
    • Evans,C.J. and Aguilera,R.J. (2003) DNase II: Genes, enzymes and function. Gene, 322, 1-15.
    • (2003) Gene , vol.322 , pp. 1-15
    • Evans, C.J.1    Aguilera, R.J.2
  • 3
    • 0033569666 scopus 로고    scopus 로고
    • Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes
    • Pouliot,J.J., Yao,K.C., Robertson,C.A. and Nash,H.A. (1999) Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes. Science, 286, 552-555.
    • (1999) Science , vol.286 , pp. 552-555
    • Pouliot, J.J.1    Yao, K.C.2    Robertson, C.A.3    Nash, H.A.4
  • 4
    • 0037178839 scopus 로고    scopus 로고
    • Conversion of phosphoglycolate to phosphate termini on 3′ overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1
    • Inamdar,K.V., Pouliot,J.J., Zhou,T., Lees-Miller,S.P., Rasouli-Nia,A. and Povirk,L.F. (2002) Conversion of phosphoglycolate to phosphate termini on 3′ overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1. J. Biol. Chem., 277, 27162-27168.
    • (2002) J. Biol. Chem , vol.277 , pp. 27162-27168
    • Inamdar, K.V.1    Pouliot, J.J.2    Zhou, T.3    Lees-Miller, S.P.4    Rasouli-Nia, A.5    Povirk, L.F.6
  • 5
    • 0032189831 scopus 로고    scopus 로고
    • Repair of DNA strand gaps and nicks containing 3′-phosphate and 5′-hydroxyl termini by purified mammalian enzymes
    • Karimi-Busheri,F., Lee,J., Tomkinson,A.E. and Weinfeld,M. (1998) Repair of DNA strand gaps and nicks containing 3′-phosphate and 5′-hydroxyl termini by purified mammalian enzymes. Nucleic Acids Res., 26 4395-4400.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4395-4400
    • Karimi-Busheri, F.1    Lee, J.2    Tomkinson, A.E.3    Weinfeld, M.4
  • 9
    • 0037040191 scopus 로고    scopus 로고
    • Pnk1, a DNA kinase/phosphatase required for normal response to DNA damage by gamma-radiation or camptothecin in Schizosaccharomyces pombe
    • Meijer,M., Karimi-Busheri,F., Huang,T.Y., Weinfeld,M. and Young,D. (2002) Pnk1, a DNA kinase/phosphatase required for normal response to DNA damage by gamma-radiation or camptothecin in Schizosaccharomyces pombe. J. Biol. Chem., 277, 4050-4055.
    • (2002) J. Biol. Chem , vol.277 , pp. 4050-4055
    • Meijer, M.1    Karimi-Busheri, F.2    Huang, T.Y.3    Weinfeld, M.4    Young, D.5
  • 10
    • 2342541592 scopus 로고    scopus 로고
    • Stable down-regulation of human polynucleotide kinase enhances spontaneous mutation frequency and sensitizes cells to genotoxic agents
    • Rasouli-Nia,A., Karimi-Busheri,F. and Weinfeld,M. (2004) Stable down-regulation of human polynucleotide kinase enhances spontaneous mutation frequency and sensitizes cells to genotoxic agents. Proc. Natl Acad. Sci. USA, 101, 6905-6910.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 6905-6910
    • Rasouli-Nia, A.1    Karimi-Busheri, F.2    Weinfeld, M.3
  • 11
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • Hegde,M.L., Hazra,T.K. and Mitra,S. (2008) Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells. Cell Res., 18, 27-47.
    • (2008) Cell Res , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 12
    • 38049115657 scopus 로고    scopus 로고
    • The mechanism of human nonhomologous DNA end joining
    • Lieber,M.R. (2008) The mechanism of human nonhomologous DNA end joining. J. Biol. Chem., 283, 1-5.
    • (2008) J. Biol. Chem , vol.283 , pp. 1-5
    • Lieber, M.R.1
  • 15
    • 33744532390 scopus 로고    scopus 로고
    • The phosphatase activity of mammalian polynucleotide kinase takes precedence over its kinase activity in repair of single strand breaks
    • Dobson,C.J. and Allinson,S.L. (2006) The phosphatase activity of mammalian polynucleotide kinase takes precedence over its kinase activity in repair of single strand breaks. Nucleic Acids Res., 34, 2230-2237.
    • (2006) Nucleic Acids Res , vol.34 , pp. 2230-2237
    • Dobson, C.J.1    Allinson, S.L.2
  • 16
    • 0031031032 scopus 로고    scopus 로고
    • Purification and substrate specificity of polydeoxyribonucleotide kinases isolated from calf thymus and rat liver
    • Karimi-Busheri,F. and Weinfeld,M. (1997) Purification and substrate specificity of polydeoxyribonucleotide kinases isolated from calf thymus and rat liver. J. Cell Biochem., 64, 258-272.
    • (1997) J. Cell Biochem , vol.64 , pp. 258-272
    • Karimi-Busheri, F.1    Weinfeld, M.2
  • 18
    • 0037155703 scopus 로고    scopus 로고
    • Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination
    • Ma,Y., Pannicke,U., Schwarz,K. and Lieber,M.R. (2002) Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination. Cell 108, 781-794.
    • (2002) Cell , vol.108 , pp. 781-794
    • Ma, Y.1    Pannicke, U.2    Schwarz, K.3    Lieber, M.R.4
  • 19
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • Putnam,C.D., Hammel,M., Hura,G.L. and Tainer,J.A. (2007) X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys., 40, 191-285.
    • (2007) Q. Rev. Biophys , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 21
    • 34248397195 scopus 로고    scopus 로고
    • Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering
    • Mylonas,E. and Svergun,D.I. (2007) Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering. J. Appl. Cryst., 40, 245-249.
    • (2007) J. Appl. Cryst , vol.40 , pp. 245-249
    • Mylonas, E.1    Svergun, D.I.2
  • 22
    • 63449105726 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun,D. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystal., 28, 768-773.
    • (1992) J. Appl. Crystal , vol.28 , pp. 768-773
    • Svergun, D.1
  • 23
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun,D.I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J., 76, 2879-2886.
    • (1999) Biophys. J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 24
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov,V.V. and Svergun,D.I. (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystal., 36 860-864.
    • (2003) J. Appl. Crystal , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 25
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers,W., Milligan,R.A. and McCammon,J.A. (1999) Situs: A package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol., 125, 185-195.
    • (1999) J. Struct. Biol , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 26
    • 84986512474 scopus 로고    scopus 로고
    • Brooks,B.R., Bruccoleri,R.E., Olafson,B.D., States,D.J., Swaminathan,S. and Karplus,M. (1983) A program for macromolecular energy, minimization, and dynamics calculations. J. Comp. Chem., 4, 187-217.
    • Brooks,B.R., Bruccoleri,R.E., Olafson,B.D., States,D.J., Swaminathan,S. and Karplus,M. (1983) A program for macromolecular energy, minimization, and dynamics calculations. J. Comp. Chem., 4, 187-217.
  • 27
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun,D., Barberato,C. and Koch,M.H.J. (1995) CRYSOL - a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr., 28, 768-773.
    • (1995) J. Appl. Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 28
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle X-ray scattering
    • Pelikan,M., Hura,G.L. and Hammel,M. (2009) Structure and flexibility within proteins as identified through small angle X-ray scattering. Gen. Physiol. Biophys., 28, 174-189.
    • (2009) Gen. Physiol. Biophys , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 31
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • Bernado,P., Mylonas,E., Petoukhov,M.V., Blackledge,M. and Svergun,D.I. (2007) Structural characterization of flexible proteins using small-angle X-ray scattering. J. Am. Chem. Soc., 129, 5656-5664.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 32
    • 4344618856 scopus 로고    scopus 로고
    • 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: Head-to-head with a bifunctional enzyme that controls glycolysis
    • Rider,M.H., Bertrand,L., Vertommen,D., Michels,P.A., Rousseau,G.G. and Hue,L. (2004) 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis. Biochem. J., 381, 561-579.
    • (2004) Biochem. J , vol.381 , pp. 561-579
    • Rider, M.H.1    Bertrand, L.2    Vertommen, D.3    Michels, P.A.4    Rousseau, G.G.5    Hue, L.6
  • 33
    • 4043166269 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in human UMP/CMP kinase
    • Segura-Pena,D., Sekulic,N., Ort,S., Konrad,M. and Lavie,A. (2004) Substrate-induced conformational changes in human UMP/CMP kinase. J. Biol. Chem., 279, 33882-33889.
    • (2004) J. Biol. Chem , vol.279 , pp. 33882-33889
    • Segura-Pena, D.1    Sekulic, N.2    Ort, S.3    Konrad, M.4    Lavie, A.5
  • 35
    • 34248363563 scopus 로고    scopus 로고
    • Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography
    • Tsutakawa,S.E., Hura,G.L., Frankel,K.A., Cooper,P.K. and Tainer,J.A. (2007) Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography. J. Struct. Biol., 158, 214-223.
    • (2007) J. Struct. Biol , vol.158 , pp. 214-223
    • Tsutakawa, S.E.1    Hura, G.L.2    Frankel, K.A.3    Cooper, P.K.4    Tainer, J.A.5
  • 36
    • 0035980273 scopus 로고    scopus 로고
    • Physical properties of human polynucleotide kinase: Hydrodynamic and spectroscopic studies
    • Mani,R.S., Karimi-Busheri,F., Cass,C.E. and Weinfeld,M. (2001) Physical properties of human polynucleotide kinase: Hydrodynamic and spectroscopic studies. Biochemistry, 40, 12967-12973.
    • (2001) Biochemistry , vol.40 , pp. 12967-12973
    • Mani, R.S.1    Karimi-Busheri, F.2    Cass, C.E.3    Weinfeld, M.4
  • 37
    • 1342327713 scopus 로고    scopus 로고
    • Recognition of DNA substrates by T4 bacteriophage polynucleotide kinase
    • Eastberg,J.H., Pelletier,J. and Stoddard,B.L. (2004) Recognition of DNA substrates by T4 bacteriophage polynucleotide kinase. Nucleic Acids Res., 32, 653-660.
    • (2004) Nucleic Acids Res , vol.32 , pp. 653-660
    • Eastberg, J.H.1    Pelletier, J.2    Stoddard, B.L.3
  • 38
    • 63249109714 scopus 로고    scopus 로고
    • Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK
    • Ali,A.A., Jukes,R.M., Pearl,L.H. and Oliver,A.W. (2009) Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK. Nucleic Acids Res., 37, 1701-1712.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1701-1712
    • Ali, A.A.1    Jukes, R.M.2    Pearl, L.H.3    Oliver, A.W.4
  • 39
    • 28044453306 scopus 로고    scopus 로고
    • End-damage-specific proteins facilitate recruitment or stability of X-ray cross-complementing protein 1 at the sites of DNA single-strand break repair
    • Parsons,J.L., Dianova,II, Boswell,E., Weinfeld,M. and Dianov,G.L. (2005) End-damage-specific proteins facilitate recruitment or stability of X-ray cross-complementing protein 1 at the sites of DNA single-strand break repair. FEBS J., 272, 5753-5763.
    • (2005) FEBS J , vol.272 , pp. 5753-5763
    • Parsons1    Dianova II, J.L.2    Boswell, E.3    Weinfeld, M.4    Dianov, G.L.5
  • 40
    • 34948837443 scopus 로고    scopus 로고
    • XRCC1 stimulates polynucleotide kinase by enhancing its damage discrimination and displacement from DNA repair intermediates
    • Mani,R.S., Fanta,M., Karimi-Busheri,F., Silver,E., Virgen,C.A., Caldecott,K.W., Cass,C.E. and Weinfeld,M. (2007) XRCC1 stimulates polynucleotide kinase by enhancing its damage discrimination and displacement from DNA repair intermediates. J. Biol. Chem., 282 28004-28013.
    • (2007) J. Biol. Chem , vol.282 , pp. 28004-28013
    • Mani, R.S.1    Fanta, M.2    Karimi-Busheri, F.3    Silver, E.4    Virgen, C.A.5    Caldecott, K.W.6    Cass, C.E.7    Weinfeld, M.8
  • 41
    • 45549099011 scopus 로고    scopus 로고
    • Coordinate 5′ and 3′ endonucleolytic trimming of terminally blocked blunt DNA double-strand break ends by Artemis nuclease and DNA-dependent protein kinase
    • Yannone,S.M., Khan,I.S., Zhou,R.Z., Zhou,T., Valerie,K. and Povirk,L.F. (2008) Coordinate 5′ and 3′ endonucleolytic trimming of terminally blocked blunt DNA double-strand break ends by Artemis nuclease and DNA-dependent protein kinase. Nucleic Acids Res., 36, 3354-3365.
    • (2008) Nucleic Acids Res , vol.36 , pp. 3354-3365
    • Yannone, S.M.1    Khan, I.S.2    Zhou, R.Z.3    Zhou, T.4    Valerie, K.5    Povirk, L.F.6
  • 43
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]
    • Mol,C.D., Izumi,T., Mitra,S. and Tainer,J.A. (2000) DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]. Nature, 403, 451-456.
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 44
    • 0742321956 scopus 로고    scopus 로고
    • Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair
    • Chapados,B.R., Hosfield,D.J., Han,S., Qiu,J., Yelent,B., Shen,B. and Tainer,J.A. (2004) Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair. Cell, 116, 39-50.
    • (2004) Cell , vol.116 , pp. 39-50
    • Chapados, B.R.1    Hosfield, D.J.2    Han, S.3    Qiu, J.4    Yelent, B.5    Shen, B.6    Tainer, J.A.7


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