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Volumn 38, Issue 3, 2009, Pages 920-930

Dna2 is a structure-specific nuclease, with affinity for 5′-flap intermediates

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEASE I; DNA; DNA2; DOUBLE STRANDED DNA; HELICASE; NUCLEASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; DEOXYRIBONUCLEASE; OLIGONUCLEOTIDE;

EID: 77950363352     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp1055     Document Type: Article
Times cited : (34)

References (52)
  • 1
    • 39449096135 scopus 로고    scopus 로고
    • Genome instability: a mechanistic view of its causes and consequences
    • Aguilera, A. and Gomez-Gonzalez, B. (2008) Genome instability: a mechanistic view of its causes and consequences. Nat. Rev. Genet., 9, 204-217.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 204-217
    • Aguilera, A.1    Gomez-Gonzalez, B.2
  • 2
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell, S.P. and Dutta, A. (2002) DNA replication in eukaryotic cells. Annu. Rev. Biochem., 71, 333-374.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 333-374
    • Bell, S.P.1    Dutta, A.2
  • 3
    • 0028784285 scopus 로고
    • DNA2 encodes a DNA helicase essential for replication of eukaryotic chromosomes
    • Budd, M.E., Choe, W.C. and Campbell, J.L. (1995) DNA2 encodes a DNA helicase essential for replication of eukaryotic chromosomes. J. Biol. Chem., 270, 26766-26769.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26766-26769
    • Budd, M.E.1    Choe, W.C.2    Campbell, J.L.3
  • 4
    • 33749603235 scopus 로고    scopus 로고
    • A network of multi-tasking proteins at the DNA replication fork preserves genome stability
    • Budd, M.E., Tong, A.H., Polaczek, P., Peng, X., Boone, C. and Campbell, J.L. (2005) A network of multi-tasking proteins at the DNA replication fork preserves genome stability. PLoS Genet., 1, e61.
    • (2005) PLoS Genet. , vol.1
    • Budd, M.E.1    Tong, A.H.2    Polaczek, P.3    Peng, X.4    Boone, C.5    Campbell, J.L.6
  • 5
    • 0038604455 scopus 로고    scopus 로고
    • Dna2 helicase/nuclease causes replicative fork stalling and double-strand breaks in the ribosomal DNA of Saccharomyces cerevisiae
    • Weitao, T., Budd, M., Hoopes, L.L. and Campbell, J.L. (2003) Dna2 helicase/nuclease causes replicative fork stalling and double-strand breaks in the ribosomal DNA of Saccharomyces cerevisiae. J. Biol. Chem., 278, 22513-22522.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22513-22522
    • Weitao, T.1    Budd, M.2    Hoopes, L.L.3    Campbell, J.L.4
  • 6
    • 55049112210 scopus 로고    scopus 로고
    • Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates
    • Zheng, L., Zhou, M., Guo, Z., Lu, H., Qian, L., Dai, H., Qiu, J., Yakubovskaya, E., Bogenhagen, D.F., Demple, B. et al. (2008) Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates. Mol. Cell, 32, 325-336.
    • (2008) Mol. Cell , vol.32 , pp. 325-336
    • Zheng, L.1    Zhou, M.2    Guo, Z.3    Lu, H.4    Qian, L.5    Dai, H.6    Qiu, J.7    Yakubovskaya, E.8    Bogenhagen, D.F.9    Demple, B.10
  • 7
    • 51549095956 scopus 로고    scopus 로고
    • Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends
    • Zhu, Z., Chung, W.H., Shim, E.Y., Lee, S.E. and Ira, G. (2008) Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends. Cell, 134, 981-994.
    • (2008) Cell , vol.134 , pp. 981-994
    • Zhu, Z.1    Chung, W.H.2    Shim, E.Y.3    Lee, S.E.4    Ira, G.5
  • 8
    • 33646058609 scopus 로고    scopus 로고
    • Isolation of human Dna2 endonuclease and characterization of its enzymatic properties
    • Kim, J.H., Kim, H.D., Ryu, G.H., Kim, D.H., Hurwitz, J. and Seo, Y.S. (2006) Isolation of human Dna2 endonuclease and characterization of its enzymatic properties. Nucleic Acids Res., 34, 1854-1864.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1854-1864
    • Kim, J.H.1    Kim, H.D.2    Ryu, G.H.3    Kim, D.H.4    Hurwitz, J.5    Seo, Y.S.6
  • 10
    • 0032500542 scopus 로고    scopus 로고
    • Dna2 of Saccharomyces cerevisiae possesses a singlestranded DNA-specific endonuclease activity that is able to act on double-stranded DNA in the presence of ATP
    • Bae, S.H., Choi, E., Lee, K.H., Park, J.S., Lee, S.H. and Seo, Y.S. (1998) Dna2 of Saccharomyces cerevisiae possesses a singlestranded DNA-specific endonuclease activity that is able to act on double-stranded DNA in the presence of ATP. J. Biol. Chem., 273, 26880-26890.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26880-26890
    • Bae, S.H.1    Choi, E.2    Lee, K.H.3    Park, J.S.4    Lee, S.H.5    Seo, Y.S.6
  • 11
    • 0034596053 scopus 로고    scopus 로고
    • The nuclease activity of the yeast DNA2 protein, which is related to the RecB-like nucleases, is essential in vivo
    • Budd, M.E., Choe, W. and Campbell, J.L. (2000) The nuclease activity of the yeast DNA2 protein, which is related to the RecB-like nucleases, is essential in vivo. J. Biol. Chem., 275, 16518-16529.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16518-16529
    • Budd, M.E.1    Choe, W.2    Campbell, J.L.3
  • 12
    • 0029098312 scopus 로고
    • A yeast gene required for DNA replication encodes a protein with homology to DNA helicases
    • Budd, M.E. and Campbell, J.L. (1995) A yeast gene required for DNA replication encodes a protein with homology to DNA helicases. Proc. Natl Acad. Sci. USA, 92, 7642-7646.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7642-7646
    • Budd, M.E.1    Campbell, J.L.2
  • 13
    • 0034528196 scopus 로고    scopus 로고
    • Characterization of the enzymatic properties of the yeast dna2 Helicase/endonuclease suggests a new model for Okazaki fragment processing
    • Bae, S.H. and Seo, Y.S. (2000) Characterization of the enzymatic properties of the yeast dna2 Helicase/endonuclease suggests a new model for Okazaki fragment processing. J. Biol. Chem., 275, 38022-38031.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38022-38031
    • Bae, S.H.1    Seo, Y.S.2
  • 14
    • 33846030496 scopus 로고    scopus 로고
    • Single strand annealing and ATP-independent strand exchange activities of yeast and human DNA2: possible role in Okazaki fragment maturation
    • Masuda-Sasa, T., Polaczek, P. and Campbell, J.L. (2006) Single strand annealing and ATP-independent strand exchange activities of yeast and human DNA2: possible role in Okazaki fragment maturation. J. Biol. Chem., 281, 38555-38564.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38555-38564
    • Masuda-Sasa, T.1    Polaczek, P.2    Campbell, J.L.3
  • 16
    • 0037449738 scopus 로고    scopus 로고
    • Okazaki fragment maturation in yeast. I. Distribution of functions between FEN1 AND DNA2
    • Ayyagari, R., Gomes, X.V., Gordenin, D.A. and Burgers, P.M. (2003) Okazaki fragment maturation in yeast. I. Distribution of functions between FEN1 AND DNA2. J. Biol. Chem., 278, 1618-1625.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1618-1625
    • Ayyagari, R.1    Gomes, X.V.2    Gordenin, D.A.3    Burgers, P.M.4
  • 17
    • 8644285427 scopus 로고    scopus 로고
    • Idling by DNA polymerase delta maintains a ligatable nick during lagging-strand DNA replication
    • Garg, P., Stith, C.M., Sabouri, N., Johansson, E. and Burgers, P.M. (2004) Idling by DNA polymerase delta maintains a ligatable nick during lagging-strand DNA replication. Genes Dev., 18, 2764-2773.
    • (2004) Genes Dev. , vol.18 , pp. 2764-2773
    • Garg, P.1    Stith, C.M.2    Sabouri, N.3    Johansson, E.4    Burgers, P.M.5
  • 18
    • 3943086339 scopus 로고    scopus 로고
    • Flap endonuclease 1: a central component of DNA metabolism
    • Liu, Y., Kao, H.I. and Bambara, R.A. (2004) Flap endonuclease 1: a central component of DNA metabolism. Annu. Rev. Biochem., 73, 589-615.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 589-615
    • Liu, Y.1    Kao, H.I.2    Bambara, R.A.3
  • 19
    • 0028281443 scopus 로고
    • The characterization of a mammalian DNA structure-specific endonuclease
    • Harrington, J.J. and Lieber, M.R. (1994) The characterization of a mammalian DNA structure-specific endonuclease. EMBO J., 13, 1235-1246.
    • (1994) EMBO J. , vol.13 , pp. 1235-1246
    • Harrington, J.J.1    Lieber, M.R.2
  • 20
    • 0037177823 scopus 로고    scopus 로고
    • Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double-flap structure as the cellular substrate
    • Kao, H.I., Henricksen, L.A., Liu, Y. and Bambara, R.A. (2002) Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double-flap structure as the cellular substrate. J. Biol. Chem., 277, 14379-14389.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14379-14389
    • Kao, H.I.1    Henricksen, L.A.2    Liu, Y.3    Bambara, R.A.4
  • 21
    • 0035954737 scopus 로고    scopus 로고
    • RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes
    • Bae, S.H., Bae, K.H., Kim, J.A. and Seo, Y.S. (2001) RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes. Nature, 412, 456-461.
    • (2001) Nature , vol.412 , pp. 456-461
    • Bae, S.H.1    Bae, K.H.2    Kim, J.A.3    Seo, Y.S.4
  • 22
    • 2442601582 scopus 로고    scopus 로고
    • On the roles of Saccharomyces cerevisiae Dna2p and Flap endonuclease 1 in Okazaki fragment processing
    • Kao, H.I., Veeraraghavan, J., Polaczek, P., Campbell, J.L. and Bambara, R.A. (2004) On the roles of Saccharomyces cerevisiae Dna2p and Flap endonuclease 1 in Okazaki fragment processing. J. Biol. Chem., 279, 15014-15024.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15014-15024
    • Kao, H.I.1    Veeraraghavan, J.2    Polaczek, P.3    Campbell, J.L.4    Bambara, R.A.5
  • 23
    • 33846007720 scopus 로고    scopus 로고
    • Flap endonuclease disengages Dna2 helicase/nuclease from Okazaki fragment flaps
    • Stewart, J.A., Campbell, J.L. and Bambara, R.A. (2006) Flap endonuclease disengages Dna2 helicase/nuclease from Okazaki fragment flaps. J. Biol. Chem., 281, 38565-38572.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38565-38572
    • Stewart, J.A.1    Campbell, J.L.2    Bambara, R.A.3
  • 24
    • 67649768562 scopus 로고    scopus 로고
    • Significance of the dissociation of Dna2 by flap endonuclease 1 to Okazaki fragment processing in Saccharomyces cerevisiae
    • Stewart, J.A., Campbell, J.L. and Bambara, R.A. (2009) Significance of the dissociation of Dna2 by flap endonuclease 1 to Okazaki fragment processing in Saccharomyces cerevisiae. J. Biol. Chem., 284, 8283-8291.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8283-8291
    • Stewart, J.A.1    Campbell, J.L.2    Bambara, R.A.3
  • 25
    • 57649114600 scopus 로고    scopus 로고
    • Dynamic removal of replication protein A by Dna2 facilitates primer cleavage during Okazaki fragment processing in Saccharomyces cerevisiae
    • Stewart, J.A., Miller, A.S., Campbell, J.L. and Bambara, R.A. (2008) Dynamic removal of replication protein A by Dna2 facilitates primer cleavage during Okazaki fragment processing in Saccharomyces cerevisiae. J. Biol. Chem., 283, 31356-31365.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31356-31365
    • Stewart, J.A.1    Miller, A.S.2    Campbell, J.L.3    Bambara, R.A.4
  • 26
    • 0031000629 scopus 로고    scopus 로고
    • A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function
    • Budd, M.E. and Campbell, J.L. (1997) A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function. Mol. Cell. Biol., 17, 2136-2142.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2136-2142
    • Budd, M.E.1    Campbell, J.L.2
  • 27
    • 59249107930 scopus 로고    scopus 로고
    • Interplay of Mre11 nuclease with Dna2 plus Sgs1 in Rad51-dependent recombinational repair
    • Budd, M.E. and Campbell, J.L. (2009) Interplay of Mre11 nuclease with Dna2 plus Sgs1 in Rad51-dependent recombinational repair. PLoS ONE, 4, e4267.
    • (2009) PLoS ONE , vol.4
    • Budd, M.E.1    Campbell, J.L.2
  • 28
    • 56049111594 scopus 로고    scopus 로고
    • Identification of the Xenopus DNA2 protein as a major nuclease for the 5′->3′ strandspecific processing of DNA ends
    • Liao, S., Toczylowski, T. and Yan, H. (2008) Identification of the Xenopus DNA2 protein as a major nuclease for the 5′->3′ strandspecific processing of DNA ends. Nucleic Acids Res., 36, 6091-6100.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6091-6100
    • Liao, S.1    Toczylowski, T.2    Yan, H.3
  • 30
    • 10944271787 scopus 로고    scopus 로고
    • Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation
    • Kao, H.I., Campbell, J.L. and Bambara, R.A. (2004) Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation. J. Biol. Chem., 279, 50840-50849.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50840-50849
    • Kao, H.I.1    Campbell, J.L.2    Bambara, R.A.3
  • 31
    • 0029616338 scopus 로고
    • Calf 5′ to 3′ exo/endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage
    • Murante, R.S., Rust, L. and Bambara, R.A. (1995) Calf 5′ to 3′ exo/endonuclease must slide from a 5′ end of the substrate to perform structure-specific cleavage. J. Biol. Chem., 270, 30377-30383.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30377-30383
    • Murante, R.S.1    Rust, L.2    Bambara, R.A.3
  • 32
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews, D.H., Sabina, J., Zuker, M. and Turner, D.H. (1999) Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol., 288, 911-940.
    • (1999) J. Mol. Biol. , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 33
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res., 31, 3406-3415.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 35
    • 0001079085 scopus 로고
    • Artificial nucleosome positioning sequences
    • Shrader, T.E. and Crothers, D.M. (1989) Artificial nucleosome positioning sequences. Proc. Natl Acad. Sci. USA, 86, 7418-7422.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 7418-7422
    • Shrader, T.E.1    Crothers, D.M.2
  • 36
    • 67649342599 scopus 로고    scopus 로고
    • Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex
    • Balakrishnan, L., Brandt, P.D., Lindsey-Boltz, L.A., Sancar, A. and Bambara, R.A. (2009) Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex. J. Biol. Chem., 284, 15158-15172.
    • (2009) J. Biol. Chem. , vol.284 , pp. 15158-15172
    • Balakrishnan, L.1    Brandt, P.D.2    Lindsey-Boltz, L.A.3    Sancar, A.4    Bambara, R.A.5
  • 37
    • 62349120246 scopus 로고    scopus 로고
    • DNA repair in mammalian cells: base excision repair: the long and short of it
    • Robertson, A.B., Klungland, A., Rognes, T. and Leiros, I. (2009) DNA repair in mammalian cells: base excision repair: the long and short of it. Cell. Mol. Life Sci., 66, 981-993.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 981-993
    • Robertson, A.B.1    Klungland, A.2    Rognes, T.3    Leiros, I.4
  • 39
    • 55049124777 scopus 로고    scopus 로고
    • Long patch base excision repair in mammalian mitochondrial genomes
    • Szczesny, B., Tann, A.W., Longley, M.J., Copeland, W.C. and Mitra, S. (2008) Long patch base excision repair in mammalian mitochondrial genomes. J. Biol. Chem., 283, 26349-26356.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26349-26356
    • Szczesny, B.1    Tann, A.W.2    Longley, M.J.3    Copeland, W.C.4    Mitra, S.5
  • 40
    • 65449158366 scopus 로고    scopus 로고
    • Differential arrival of leading and lagging strand DNA polymerases at fission yeast telomeres
    • Moser, B.A., Subramanian, L., Chang, Y.T., Noguchi, C., Noguchi, E. and Nakamura, T.M. (2009) Differential arrival of leading and lagging strand DNA polymerases at fission yeast telomeres. EMBO J., 28, 810-820.
    • (2009) EMBO J. , vol.28 , pp. 810-820
    • Moser, B.A.1    Subramanian, L.2    Chang, Y.T.3    Noguchi, C.4    Noguchi, E.5    Nakamura, T.M.6
  • 41
    • 67649653968 scopus 로고    scopus 로고
    • Multiple pathways regulate 3′ overhang generation at S. cerevisiae telomeres
    • Bonetti, D., Martina, M., Clerici, M., Lucchini, G. and Longhese, M.P. (2009) Multiple pathways regulate 3′ overhang generation at S. cerevisiae telomeres. Mol. Cell, 35, 70-81.
    • (2009) Mol. Cell , vol.35 , pp. 70-81
    • Bonetti, D.1    Martina, M.2    Clerici, M.3    Lucchini, G.4    Longhese, M.P.5
  • 42
    • 0030002197 scopus 로고    scopus 로고
    • A helical arch allowing single-stranded DNA to thread through T5 5′-exonuclease
    • Ceska, T.A., Sayers, J.R., Stier, G. and Suck, D. (1996) A helical arch allowing single-stranded DNA to thread through T5 5′-exonuclease. Nature, 382, 90-93.
    • (1996) Nature , vol.382 , pp. 90-93
    • Ceska, T.A.1    Sayers, J.R.2    Stier, G.3    Suck, D.4
  • 43
    • 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
  • 44
    • 0037173092 scopus 로고    scopus 로고
    • Interactions of mutant and wildtype flap endonucleases with oligonucleotide substrates suggest an alternative model of DNA binding
    • Dervan, J.J., Feng, M., Patel, D., Grasby, J.A., Artymiuk, P.J., Ceska, T.A. and Sayers, J.R. (2002) Interactions of mutant and wildtype flap endonucleases with oligonucleotide substrates suggest an alternative model of DNA binding. Proc. Natl Acad. Sci. USA, 99, 8542-8547.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8542-8547
    • Dervan, J.J.1    Feng, M.2    Patel, D.3    Grasby, J.A.4    Artymiuk, P.J.5    Ceska, T.A.6    Sayers, J.R.7
  • 45
    • 35748936474 scopus 로고    scopus 로고
    • Crystal structure of bacteriophage T4 5′ nuclease in complex with a branched DNA reveals how flap endonuclease-1 family nucleases bind their substrates
    • Devos, J.M., Tomanicek, S.J., Jones, C.E., Nossal, N.G. and Mueser, T.C. (2007) Crystal structure of bacteriophage T4 5′ nuclease in complex with a branched DNA reveals how flap endonuclease-1 family nucleases bind their substrates. J. Biol. Chem., 282, 31713-31724.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31713-31724
    • Devos, J.M.1    Tomanicek, S.J.2    Jones, C.E.3    Nossal, N.G.4    Mueser, T.C.5
  • 46
    • 0032475933 scopus 로고    scopus 로고
    • Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity
    • Hosfield, D.J., Mol, C.D., Shen, B. and Tainer, J.A. (1998) Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity. Cell, 95, 135-146.
    • (1998) Cell , vol.95 , pp. 135-146
    • Hosfield, D.J.1    Mol, C.D.2    Shen, B.3    Tainer, J.A.4
  • 47
    • 0028983795 scopus 로고
    • Crystal structure of Thermus aquaticus DNA polymerase
    • Kim, Y., Eom, S.H., Wang, J., Lee, D.S., Suh, S.W. and Steitz, T.A. (1995) Crystal structure of Thermus aquaticus DNA polymerase. Nature, 376, 612-616.
    • (1995) Nature , vol.376 , pp. 612-616
    • Kim, Y.1    Eom, S.H.2    Wang, J.3    Lee, D.S.4    Suh, S.W.5    Steitz, T.A.6
  • 48
    • 33645823577 scopus 로고    scopus 로고
    • The DNA-protein interaction modes of FEN-1 with gap substrates and their implication in preventing duplication mutations
    • Liu, R., Qiu, J., Finger, L.D., Zheng, L. and Shen, B. (2006) The DNA-protein interaction modes of FEN-1 with gap substrates and their implication in preventing duplication mutations. Nucleic Acids Res., 34, 1772-1784.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1772-1784
    • Liu, R.1    Qiu, J.2    Finger, L.D.3    Zheng, L.4    Shen, B.5
  • 49
    • 2142860722 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 RNase H, a 5′ to 3′ RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic proteins
    • Mueser, T.C., Nossal, N.G. and Hyde, C.C. (1996) Structure of bacteriophage T4 RNase H, a 5′ to 3′ RNA-DNA and DNA-DNA exonuclease with sequence similarity to the RAD2 family of eukaryotic proteins. Cell, 85, 1101-1112.
    • (1996) Cell , vol.85 , pp. 1101-1112
    • Mueser, T.C.1    Nossal, N.G.2    Hyde, C.C.3
  • 50
    • 2642545719 scopus 로고    scopus 로고
    • Interaction interface of human flap endonuclease-1 with its DNA substrates
    • Qiu, J., Liu, R., Chapados, B.R., Sherman, M., Tainer, J.A. and Shen, B. (2004) Interaction interface of human flap endonuclease-1 with its DNA substrates. J. Biol. Chem., 279, 24394-24402.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24394-24402
    • Qiu, J.1    Liu, R.2    Chapados, B.R.3    Sherman, M.4    Tainer, J.A.5    Shen, B.6
  • 51
    • 0035839588 scopus 로고    scopus 로고
    • Contacts between the 5′ nuclease of DNA polymerase I and its DNA substrate
    • Xu, Y., Potapova, O., Leschziner, A.E., Grindley, N.D. and Joyce, C.M. (2001) Contacts between the 5′ nuclease of DNA polymerase I and its DNA substrate. J. Biol. Chem., 276, 30167-30177.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30167-30177
    • Xu, Y.1    Potapova, O.2    Leschziner, A.E.3    Grindley, N.D.4    Joyce, C.M.5


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