메뉴 건너뛰기




Volumn 110, Issue 22, 2013, Pages

Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity

Author keywords

DNA nuclease; Replication protein A; Sgs1

Indexed keywords

DNA; DNA2; HELICASE; NUCLEASE; REPLICATION FACTOR A; UNCLASSIFIED DRUG;

EID: 84878437546     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1300390110     Document Type: Article
Times cited : (50)

References (52)
  • 1
    • 0021026937 scopus 로고
    • Isolation of yeast DNA replication mutants in permeabilized cells
    • Kuo C, Nuang H, Campbell JL (1983) Isolation of yeast DNA replication mutants in permeabilized cells. Proc Natl Acad Sci USA 80(21):6465-6469.
    • (1983) Proc Natl Acad Sci USA , vol.80 , Issue.21 , pp. 6465-6469
    • Kuo, C.1    Nuang, H.2    Campbell, J.L.3
  • 2
    • 0029098312 scopus 로고
    • A yeast gene required for DNA replication encodes a protein with homology to DNA helicases
    • Budd ME, Campbell JL (1995) A yeast gene required for DNA replication encodes a protein with homology to DNA helicases. Proc Natl Acad Sci USA 92(17):7642-7646.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.17 , pp. 7642-7646
    • Budd, M.E.1    Campbell, J.L.2
  • 3
    • 0028784285 scopus 로고
    • DNA2 encodes a DNA helicase essential for replication of eukaryotic chromosomes
    • Budd ME, Choe WC, Campbell JL (1995) DNA2 encodes a DNA helicase essential for replication of eukaryotic chromosomes. J Biol Chem 270(45):26766-26769.
    • (1995) J Biol Chem , vol.270 , Issue.45 , pp. 26766-26769
    • Budd, M.E.1    Choe, W.C.2    Campbell, J.L.3
  • 4
    • 0032500542 scopus 로고    scopus 로고
    • Dna2 of Saccharomyces cerevisiae possesses a single-stranded DNA-specific endonuclease activity that is able to act on double-stranded DNA in the presence of ATP
    • Bae SH, et al. (1998) Dna2 of Saccharomyces cerevisiae possesses a single-stranded DNA-specific endonuclease activity that is able to act on double-stranded DNA in the presence of ATP. J Biol Chem 273(41):26880-26890.
    • (1998) J Biol Chem , vol.273 , Issue.41 , pp. 26880-26890
    • Bae, S.H.1
  • 5
    • 0031000629 scopus 로고    scopus 로고
    • A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function
    • Budd ME, Campbell JL (1997) A yeast replicative helicase, Dna2 helicase, interacts with yeast FEN-1 nuclease in carrying out its essential function. Mol Cell Biol 17(4): 2136-2142.
    • (1997) Mol Cell Biol , vol.17 , Issue.4 , pp. 2136-2142
    • Budd, M.E.1    Campbell, J.L.2
  • 6
    • 0035954737 scopus 로고    scopus 로고
    • RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes
    • Bae SH, Bae KH, Kim JA, Seo YS (2001) RPA governs endonuclease switching during processing of Okazaki fragments in eukaryotes. Nature 412(6845): 456-461.
    • (2001) Nature , vol.412 , Issue.6845 , pp. 456-461
    • Bae, S.H.1    Bae, K.H.2    Kim, J.A.3    Seo, Y.S.4
  • 7
    • 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 SH, Seo YS (2000) Characterization of the enzymatic properties of the yeast dna2 Helicase/endonuclease suggests a new model for Okazaki fragment processing. J Biol Chem 275(48):38022-38031.
    • (2000) J Biol Chem , vol.275 , Issue.48 , pp. 38022-38031
    • Bae, S.H.1    Seo, Y.S.2
  • 8
    • 2442601582 scopus 로고    scopus 로고
    • On the roles of Saccharomyces cerevisiae Dna2p and Flap endonuclease 1 in Okazaki fragment processing
    • Kao HI, Veeraraghavan J, Polaczek P, Campbell JL, Bambara RA (2004) On the roles of Saccharomyces cerevisiae Dna2p and Flap endonuclease 1 in Okazaki fragment processing. J Biol Chem 279(15):15014-15024.
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 15014-15024
    • Kao, H.I.1    Veeraraghavan, J.2    Polaczek, P.3    Campbell, J.L.4    Bambara, R.A.5
  • 9
    • 51549095956 scopus 로고    scopus 로고
    • Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends
    • Zhu Z, Chung WH, Shim EY, Lee SE, Ira G (2008) Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends. Cell 134(6):981-994.
    • (2008) Cell , vol.134 , Issue.6 , pp. 981-994
    • Zhu, Z.1    Chung, W.H.2    Shim, E.Y.3    Lee, S.E.4    Ira, G.5
  • 10
    • 53649104599 scopus 로고    scopus 로고
    • Sae2, Exo1 and Sgs1 collaborate in DNA doublestrand break processing
    • Mimitou EP, Symington LS (2008) Sae2, Exo1 and Sgs1 collaborate in DNA doublestrand break processing. Nature 455(7214):770-774.
    • (2008) Nature , vol.455 , Issue.7214 , pp. 770-774
    • Mimitou, E.P.1    Symington, L.S.2
  • 11
    • 53649090109 scopus 로고    scopus 로고
    • DNA helicases Sgs1 and BLM promote DNA double-strand break resection
    • Gravel S, Chapman JR, Magill C, Jackson SP (2008) DNA helicases Sgs1 and BLM promote DNA double-strand break resection. Genes Dev 22(20):2767-2772.
    • (2008) Genes Dev , vol.22 , Issue.20 , pp. 2767-2772
    • Gravel, S.1    Chapman, J.R.2    Magill, C.3    Jackson, S.P.4
  • 12
    • 77956325620 scopus 로고    scopus 로고
    • DNA end resection by Dna2-Sgs1-RPA and its stimulation by Top3-Rmi1 and Mre11-Rad50-Xrs2
    • Cejka P, et al. (2010) DNA end resection by Dna2-Sgs1-RPA and its stimulation by Top3-Rmi1 and Mre11-Rad50-Xrs2. Nature 467(7311):112-116.
    • (2010) Nature , vol.467 , Issue.7311 , pp. 112-116
    • Cejka, P.1
  • 13
    • 77956302112 scopus 로고    scopus 로고
    • Mechanism of the ATP-dependent DNA end-resection machinery from Saccharomyces cerevisiae
    • Niu H, et al. (2010) Mechanism of the ATP-dependent DNA end-resection machinery from Saccharomyces cerevisiae. Nature 467(7311):108-111.
    • (2010) Nature , vol.467 , Issue.7311 , pp. 108-111
    • Niu, H.1
  • 14
    • 79951688343 scopus 로고    scopus 로고
    • BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair
    • Nimonkar AV, et al. (2011) BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair. Genes Dev 25(4): 350-362.
    • (2011) Genes Dev , vol.25 , Issue.4 , pp. 350-362
    • Nimonkar, A.V.1
  • 15
    • 0036258214 scopus 로고    scopus 로고
    • Dynamic localization of an Okazaki fragment processing protein suggests a novel role in telomere replication
    • Choe W, Budd M, Imamura O, Hoopes L, Campbell JL (2002) Dynamic localization of an Okazaki fragment processing protein suggests a novel role in telomere replication. Mol Cell Biol 22(12):4202-4217.
    • (2002) Mol Cell Biol , vol.22 , Issue.12 , pp. 4202-4217
    • Choe, W.1    Budd, M.2    Imamura, O.3    Hoopes, L.4    Campbell, J.L.5
  • 16
    • 1542344026 scopus 로고    scopus 로고
    • The transcriptome of prematurely aging yeast cells is similar to that of telomerase-deficient cells
    • Lesur I, Campbell JL (2004) The transcriptome of prematurely aging yeast cells is similar to that of telomerase-deficient cells. Mol Biol Cell 15(3):1297-1312.
    • (2004) Mol Biol Cell , vol.15 , Issue.3 , pp. 1297-1312
    • Lesur, I.1    Campbell, J.L.2
  • 17
    • 55049112210 scopus 로고    scopus 로고
    • Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates
    • Zheng L, et al. (2008) Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates. Mol Cell 32(3):325-336.
    • (2008) Mol Cell , vol.32 , Issue.3 , pp. 325-336
    • Zheng, L.1
  • 18
    • 84861974796 scopus 로고    scopus 로고
    • The intra-S phase checkpoint targets Dna2 to prevent stalled replication forks from reversing
    • Hu J, et al. (2012) The intra-S phase checkpoint targets Dna2 to prevent stalled replication forks from reversing. Cell 149(6):1221-1232.
    • (2012) Cell , vol.149 , Issue.6 , pp. 1221-1232
    • Hu, J.1
  • 19
    • 84861880476 scopus 로고    scopus 로고
    • Human nuclease/helicase DNA2 alleviates replication stress by promoting DNA end resection
    • Peng G, et al. (2012) Human nuclease/helicase DNA2 alleviates replication stress by promoting DNA end resection. Cancer Res 72(11):2802-2813.
    • (2012) Cancer Res , vol.72 , Issue.11 , pp. 2802-2813
    • Peng, G.1
  • 20
    • 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 ME, Choe Wc, Campbell JL (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(22):16518-16529.
    • (2000) J Biol Chem , vol.275 , Issue.22 , pp. 16518-16529
    • Budd, M.E.1    Choe, W.C.2    Campbell, J.L.3
  • 21
    • 10944271787 scopus 로고    scopus 로고
    • Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation
    • Kao HI, Campbell JL, Bambara RA (2004) Dna2p helicase/nuclease is a tracking protein, like FEN1, for flap cleavage during Okazaki fragment maturation. J Biol Chem 279(49):50840-50849.
    • (2004) J Biol Chem , vol.279 , Issue.49 , pp. 50840-50849
    • Kao, H.I.1    Campbell, J.L.2    Bambara, R.A.3
  • 23
    • 0037135632 scopus 로고    scopus 로고
    • Coupling of DNA helicase and endonuclease activities of yeast Dna2 facilitates Okazaki fragment processing
    • Bae SH, et al. (2002) Coupling of DNA helicase and endonuclease activities of yeast Dna2 facilitates Okazaki fragment processing. J Biol Chem 277(29):26632-26641.
    • (2002) J Biol Chem , vol.277 , Issue.29 , pp. 26632-26641
    • Bae, S.H.1
  • 24
    • 33646058609 scopus 로고    scopus 로고
    • Isolation of human Dna2 endonuclease and characterization of its enzymatic properties
    • Kim JH, et al. (2006) Isolation of human Dna2 endonuclease and characterization of its enzymatic properties. Nucleic Acids Res 34(6):1854-1864.
    • (2006) Nucleic Acids Res , vol.34 , Issue.6 , pp. 1854-1864
    • Kim, J.H.1
  • 25
    • 33846030496 scopus 로고    scopus 로고
    • Single strand annealing and ATPindependent strand exchange activities of yeast and human DNA2: Possible role in Okazaki fragment maturation
    • Masuda-Sasa T, Polaczek P, Campbell JL (2006) Single strand annealing and ATPindependent strand exchange activities of yeast and human DNA2: Possible role in Okazaki fragment maturation. J Biol Chem 281(50):38555-38564.
    • (2006) J Biol Chem , vol.281 , Issue.50 , pp. 38555-38564
    • Masuda-Sasa, T.1    Polaczek, P.2    Campbell, J.L.3
  • 26
    • 0034695597 scopus 로고    scopus 로고
    • Identification of the Xenopus laevis homolog of Saccharomyces cerevisiae DNA2 and its role in DNA replication
    • Liu Q, Choe W, Campbell JL (2000) Identification of the Xenopus laevis homolog of Saccharomyces cerevisiae DNA2 and its role in DNA replication. J Biol Chem 275(3): 1615-1624.
    • (2000) J Biol Chem , vol.275 , Issue.3 , pp. 1615-1624
    • Liu, Q.1    Choe, W.2    Campbell, J.L.3
  • 28
    • 0034724750 scopus 로고    scopus 로고
    • The pattern of sensitivity of yeast dna2 mutants to DNA damaging agents suggests a role in DSB and postreplication repair pathways
    • Budd ME, Campbell JL (2000) The pattern of sensitivity of yeast dna2 mutants to DNA damaging agents suggests a role in DSB and postreplication repair pathways. Mutat Res 459(3):173-186.
    • (2000) Mutat Res , vol.459 , Issue.3 , pp. 173-186
    • Budd, M.E.1    Campbell, J.L.2
  • 29
    • 0032943760 scopus 로고    scopus 로고
    • Dna2 mutants reveal interactions with Dna polymerase alpha and Ctf4, a Pol alpha accessory factor, and show that full Dna2 helicase activity is not essential for growth
    • Formosa T, Nittis T (1999) Dna2 mutants reveal interactions with Dna polymerase alpha and Ctf4, a Pol alpha accessory factor, and show that full Dna2 helicase activity is not essential for growth. Genetics 151(4):1459-1470.
    • (1999) Genetics , vol.151 , Issue.4 , pp. 1459-1470
    • Formosa, T.1    Nittis, T.2
  • 30
    • 65549136266 scopus 로고    scopus 로고
    • An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases
    • Yeeles JT, Cammack R, Dillingham MS (2009) An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases. J Biol Chem 284(12): 7746-7755.
    • (2009) J Biol Chem , vol.284 , Issue.12 , pp. 7746-7755
    • Yeeles, J.T.1    Cammack, R.2    Dillingham, M.S.3
  • 31
    • 84867289116 scopus 로고    scopus 로고
    • Cross talk between the nuclease and helicase activities of Dna2: Role of an essential iron-sulfur cluster domain
    • Pokharel S, Campbell JL (2012) Cross talk between the nuclease and helicase activities of Dna2: Role of an essential iron-sulfur cluster domain. Nucleic Acids Res 40(16): 7821-7830.
    • (2012) Nucleic Acids Res , vol.40 , Issue.16 , pp. 7821-7830
    • Pokharel, S.1    Campbell, J.L.2
  • 32
    • 77950900571 scopus 로고    scopus 로고
    • The full-length Saccharomyces cerevisiae Sgs1 protein is a vigorous DNA helicase that preferentially unwinds holliday junctions
    • Cejka P, Kowalczykowski SC (2010) The full-length Saccharomyces cerevisiae Sgs1 protein is a vigorous DNA helicase that preferentially unwinds holliday junctions. J Biol Chem 285(11):8290-8301.
    • (2010) J Biol Chem , vol.285 , Issue.11 , pp. 8290-8301
    • Cejka, P.1    Kowalczykowski, S.C.2
  • 33
    • 59149096327 scopus 로고    scopus 로고
    • Torsional stiffness of single superparamagnetic microspheres in an external magnetic field
    • Klaue D, Seidel R (2009) Torsional stiffness of single superparamagnetic microspheres in an external magnetic field. Phys Rev Lett 102(2):028302.
    • (2009) Phys Rev Lett , vol.102 , Issue.2 , pp. 028302
    • Klaue, D.1    Seidel, R.2
  • 34
    • 77955063955 scopus 로고    scopus 로고
    • Torsional regulation of hRPA-induced unwinding of double-stranded DNA
    • De Vlaminck I, et al. (2010) Torsional regulation of hRPA-induced unwinding of double-stranded DNA. Nucleic Acids Res 38(12):4133-4142.
    • (2010) Nucleic Acids Res , vol.38 , Issue.12 , pp. 4133-4142
    • De Vlaminck, I.1
  • 35
    • 2342598305 scopus 로고    scopus 로고
    • Single-molecule assay reveals strand switching and enhanced processivity of UvrD
    • Dessinges MN, Lionnet T, Xi XG, Bensimon D, Croquette V (2004) Single-molecule assay reveals strand switching and enhanced processivity of UvrD. Proc Natl Acad Sci USA 101(17):6439-6444.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.17 , pp. 6439-6444
    • Dessinges, M.N.1    Lionnet, T.2    Xi, X.G.3    Bensimon, D.4    Croquette, V.5
  • 36
    • 36749028241 scopus 로고    scopus 로고
    • Single phage T4 DNA packaging motors exhibit large force generation, high velocity, and dynamic variability
    • Fuller DN, Raymer DM, Kottadiel VI, Rao VB, Smith DE (2007) Single phage T4 DNA packaging motors exhibit large force generation, high velocity, and dynamic variability. Proc Natl Acad Sci USA 104(43):16868-16873.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.43 , pp. 16868-16873
    • Fuller, D.N.1    Raymer, D.M.2    Kottadiel, V.I.3    Rao, V.B.4    Smith, D.E.5
  • 37
    • 0020971304 scopus 로고
    • Escherichia coli phage T4 topoisomerase
    • Kreuzer KN, Jongeneel CV (1983) Escherichia coli phage T4 topoisomerase. Methods Enzymol 100:144-160.
    • (1983) Methods Enzymol , vol.100 , pp. 144-160
    • Kreuzer, K.N.1    Jongeneel, C.V.2
  • 38
    • 0023135142 scopus 로고
    • Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein: Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA
    • Kowalczykowski SC, Krupp RA (1987) Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein: Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA. J Mol Biol 193(1):97-113.
    • (1987) J Mol Biol , vol.193 , Issue.1 , pp. 97-113
    • Kowalczykowski, S.C.1    Krupp, R.A.2
  • 39
    • 77949557756 scopus 로고    scopus 로고
    • Dna2 on the road to Okazaki fragment processing and genome stability in eukaryotes
    • Kang YH, Lee CH, Seo YS (2010) Dna2 on the road to Okazaki fragment processing and genome stability in eukaryotes. Crit Rev Biochem Mol Biol 45(2):71-96.
    • (2010) Crit Rev Biochem Mol Biol , vol.45 , Issue.2 , pp. 71-96
    • Kang, Y.H.1    Lee, C.H.2    Seo, Y.S.3
  • 40
    • 84862688195 scopus 로고    scopus 로고
    • Okazaki fragment processing-independent role for human Dna2 enzyme during DNA replication
    • Duxin JP, et al. (2012) Okazaki fragment processing-independent role for human Dna2 enzyme during DNA replication. J Biol Chem 287(26):21980-21991.
    • (2012) J Biol Chem , vol.287 , Issue.26 , pp. 21980-21991
    • Duxin, J.P.1
  • 41
    • 77951191213 scopus 로고    scopus 로고
    • Acetylation of Dna2 endonuclease/helicase and flap endonuclease 1 by p300 promotes DNA stability by creating long flap intermediates
    • Balakrishnan L, Stewart J, Polaczek P, Campbell JL, Bambara RA (2010) Acetylation of Dna2 endonuclease/helicase and flap endonuclease 1 by p300 promotes DNA stability by creating long flap intermediates. J Biol Chem 285(7):4398-4404.
    • (2010) J Biol Chem , vol.285 , Issue.7 , pp. 4398-4404
    • Balakrishnan, L.1    Stewart, J.2    Polaczek, P.3    Campbell, J.L.4    Bambara, R.A.5
  • 42
    • 80052492286 scopus 로고    scopus 로고
    • Cell cycle regulation of DNA double-strand break end resection by Cdk1-dependent Dna2 phosphorylation
    • Chen X, et al. (2011) Cell cycle regulation of DNA double-strand break end resection by Cdk1-dependent Dna2 phosphorylation. Nat Struct Mol Biol 18(9):1015-1019.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.9 , pp. 1015-1019
    • Chen, X.1
  • 43
    • 0035878722 scopus 로고    scopus 로고
    • Tripartite structure of Saccharomyces cerevisiae Dna2 helicase/ endonuclease
    • Bae SH, et al. (2001) Tripartite structure of Saccharomyces cerevisiae Dna2 helicase/ endonuclease. Nucleic Acids Res 29(14):3069-3079.
    • (2001) Nucleic Acids Res , vol.29 , Issue.14 , pp. 3069-3079
    • Bae, S.H.1
  • 44
    • 57349157777 scopus 로고    scopus 로고
    • RecBCD enzyme and the repair of doublestranded DNA breaks
    • Dillingham MS, Kowalczykowski SC (2008) RecBCD enzyme and the repair of doublestranded DNA breaks. Microbiol Mol Biol Rev 72(4):642-671.
    • (2008) Microbiol Mol Biol Rev , vol.72 , Issue.4 , pp. 642-671
    • Dillingham, M.S.1    Kowalczykowski, S.C.2
  • 45
    • 23944518444 scopus 로고    scopus 로고
    • An inactivated nuclease-like domain in RecC with novel function: Implications for evolution
    • Rigden DJ (2005) An inactivated nuclease-like domain in RecC with novel function: Implications for evolution. BMC Struct Biol 5:9.
    • (2005) BMC Struct Biol , vol.5 , pp. 9
    • Rigden, D.J.1
  • 46
  • 47
    • 79953177394 scopus 로고    scopus 로고
    • The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain
    • Yeeles JT, Gwynn EJ, Webb MR, Dillingham MS (2011) The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain. Nucleic Acids Res 39(6):2271-2285.
    • (2011) Nucleic Acids Res , vol.39 , Issue.6 , pp. 2271-2285
    • Yeeles, J.T.1    Gwynn, E.J.2    Webb, M.R.3    Dillingham, M.S.4
  • 48
    • 84858796420 scopus 로고    scopus 로고
    • Insights into Chi recognition from the structure of an AddAB-type helicase-nuclease complex
    • Saikrishnan K, et al. (2012) Insights into Chi recognition from the structure of an AddAB-type helicase-nuclease complex. EMBO J 31(6):1568-1578.
    • (2012) EMBO J , vol.31 , Issue.6 , pp. 1568-1578
    • Saikrishnan, K.1
  • 49
    • 0037931365 scopus 로고    scopus 로고
    • The recombinationdeficient mutant RPA (rfa1-t11) is displaced slowly from single-stranded DNA by Rad51 protein
    • Kantake N, Sugiyama T, Kolodner RD, Kowalczykowski SC (2003) The recombinationdeficient mutant RPA (rfa1-t11) is displaced slowly from single-stranded DNA by Rad51 protein. J Biol Chem 278(26):23410-23417.
    • (2003) J Biol Chem , vol.278 , Issue.26 , pp. 23410-23417
    • Kantake, N.1    Sugiyama, T.2    Kolodner, R.D.3    Kowalczykowski, S.C.4
  • 50
    • 0035853277 scopus 로고    scopus 로고
    • Rad54 protein stimulates heteroduplex DNA formation in the synaptic phase of DNA strand exchange via specific interactions with the presynaptic Rad51 nucleoprotein filament
    • Solinger JA, Lutz G, Sugiyama T, Kowalczykowski SC, Heyer WD (2001) Rad54 protein stimulates heteroduplex DNA formation in the synaptic phase of DNA strand exchange via specific interactions with the presynaptic Rad51 nucleoprotein filament. J Mol Biol 307(5):1207-1221.
    • (2001) J Mol Biol , vol.307 , Issue.5 , pp. 1207-1221
    • Solinger, J.A.1    Lutz, G.2    Sugiyama, T.3    Kowalczykowski, S.C.4    Heyer, W.D.5
  • 51
    • 84855795597 scopus 로고    scopus 로고
    • Nicking enzyme-based internal labeling of DNA at multiple loci
    • Luzzietti N, Knappe S, Richter I, Seidel R (2012) Nicking enzyme-based internal labeling of DNA at multiple loci. Nat Protoc 7(4):643-653.
    • (2012) Nat Protoc , vol.7 , Issue.4 , pp. 643-653
    • Luzzietti, N.1    Knappe, S.2    Richter, I.3    Seidel, R.4
  • 52
    • 79951565667 scopus 로고    scopus 로고
    • Efficient preparation of internally modified single-molecule constructs using nicking enzymes
    • Luzzietti N, et al. (2011) Efficient preparation of internally modified single-molecule constructs using nicking enzymes. Nucleic Acids Res 39(3):e15.
    • (2011) Nucleic Acids Res , vol.39 , Issue.3
    • Luzzietti, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.