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Volumn 5, Issue 2, 2013, Pages

Okazaki fragment metabolism

Author keywords

[No Author keywords available]

Indexed keywords

DNA; OKAZAKI FRAGMENTS;

EID: 84875134308     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a010173     Document Type: Article
Times cited : (118)

References (74)
  • 2
    • 0037449738 scopus 로고    scopus 로고
    • Okazaki fragment maturation in yeast. I. Distribution of functions between FEN1 AND DNA2
    • Ayyagari R, Gomes XV, Gordenin DA, Burgers PM. 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
  • 3
    • 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: 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
  • 4
  • 5
    • 79953207705 scopus 로고    scopus 로고
    • Eukaryotic lagging strand DNA replication employs a multi-pathway mechanism that protects genome integrity
    • Balakrishnan L, Bambara RA. 2011b. Eukaryotic lagging strand DNA replication employs a multi-pathway mechanism that protects genome integrity. J Biol Chem 286: 6865-6870.
    • (2011) J Biol Chem , vol.286 , pp. 6865-6870
    • Balakrishnan, L.1    Bambara, R.A.2
  • 6
    • 67649342599 scopus 로고    scopus 로고
    • Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex
    • Balakrishnan L, Brandt PD, Lindsey-Boltz LA, Sancar A, Bambara RA. 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
  • 7
    • 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: 4398-4404.
    • (2010) J Biol Chem , vol.285 , pp. 4398-4404
    • Balakrishnan, L.1    Stewart, J.2    Polaczek, P.3    Campbell, J.L.4    Bambara, R.A.5
  • 8
    • 0031054051 scopus 로고    scopus 로고
    • Enzymes and reactions at the eukaryotic DNA replication fork
    • Bambara RA, Murante RS, Henricksen LA. 1997. Enzymes and reactions at the eukaryotic DNA replication fork. J Biol Chem 272: 4647-4650.
    • (1997) J Biol Chem , vol.272 , pp. 4647-4650
    • Bambara, R.A.1    Murante, R.S.2    Henricksen, L.A.3
  • 9
    • 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 92: 7642-7646.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 7642-7646
    • Budd, M.E.1    Campbell, J.L.2
  • 10
    • 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: 2136-2142.
    • (1997) Mol Cell Biol , vol.17 , pp. 2136-2142
    • Budd, M.E.1    Campbell, J.L.2
  • 11
    • 33749603235 scopus 로고    scopus 로고
    • A network of multi-tasking proteins at the DNA replication fork preserves genome stability
    • Budd ME, Tong AH, Polaczek P, Peng X, Boone C, Campbell JL. 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
  • 12
    • 33645215616 scopus 로고    scopus 로고
    • Evidence suggesting that Pif1 helicase functions in DNA replication with the Dna2 helicase/nuclease and DNA polymerase delta
    • Budd ME, Reis CC, Smith S, Myung K, Campbell JL. 2006. Evidence suggesting that Pif1 helicase functions in DNA replication with the Dna2 helicase/nuclease and DNA polymerase delta. Mol Cell Biol 26: 2490-2500.
    • (2006) Mol Cell Biol , vol.26 , pp. 2490-2500
    • Budd, M.E.1    Reis, C.C.2    Smith, S.3    Myung, K.4    Campbell, J.L.5
  • 13
    • 79955999320 scopus 로고    scopus 로고
    • Inviability of a DNA2 deletion mutant is due to the DNA damage checkpoint
    • Budd ME, Antoshechkin IA, Reis C, Wold BJ, Campbell JL. 2011. Inviability of a DNA2 deletion mutant is due to the DNA damage checkpoint. Cell Cycle 10: 1690-1698.
    • (2011) Cell Cycle , vol.10 , pp. 1690-1698
    • Budd, M.E.1    Antoshechkin, I.A.2    Reis, C.3    Wold, B.J.4    Campbell, J.L.5
  • 14
    • 63249130106 scopus 로고    scopus 로고
    • Polymerase dynamics at the eukaryotic DNA replication fork
    • Burgers PM. 2009. Polymerase dynamics at the eukaryotic DNA replication fork. J Biol Chem 284: 4041-4045.
    • (2009) J Biol Chem , vol.284 , pp. 4041-4045
    • Burgers, P.M.1
  • 15
    • 61349102407 scopus 로고    scopus 로고
    • Ribonuclease H: The enzymes in eukaryotes
    • Cerritelli SM, Crouch RJ. 2009. Ribonuclease H: The enzymes in eukaryotes. FEBS J 276: 1494-1505.
    • (2009) FEBS J , vol.276 , pp. 1494-1505
    • Cerritelli, S.M.1    Crouch, R.J.2
  • 18
    • 0027379095 scopus 로고
    • Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication
    • Copeland WC, Wang TS. 1993. Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication. J Biol Chem 268: 26179-26189.
    • (1993) J Biol Chem , vol.268 , pp. 26179-26189
    • Copeland, W.C.1    Wang, T.S.2
  • 19
    • 0026770783 scopus 로고
    • The simian virus 40 Tantigen double hexamer assembles around the DNA at the replication origin
    • Dean FB, Borowiec JA, Eki T, Hurwitz J. 1992. The simian virus 40 Tantigen double hexamer assembles around the DNA at the replication origin. J Biol Chem 267: 14129-14137.
    • (1992) J Biol Chem , vol.267 , pp. 14129-14137
    • Dean, F.B.1    Borowiec, J.A.2    Eki, T.3    Hurwitz, J.4
  • 20
    • 0026726156 scopus 로고
    • The replication of DNA containing the simian virus 40 origin by the monopolymerase and dipolymerase systems
    • Eki T, Matsumoto T, Murakami Y, Hurwitz J. 1992. The replication of DNA containing the simian virus 40 origin by the monopolymerase and dipolymerase systems. J Biol Chem 267: 7284-7294.
    • (1992) J Biol Chem , vol.267 , pp. 7284-7294
    • Eki, T.1    Matsumoto, T.2    Murakami, Y.3    Hurwitz, J.4
  • 21
    • 0032484140 scopus 로고    scopus 로고
    • Partial functional deficiency of E160D flap endonuclease-1 mutant in vitro and in vivo is due to defective cleavage of DNA substrates
    • Frank G, Qiu J, Somsouk M, Weng Y, Somsouk L, Nolan JP, Shen B. 1998. Partial functional deficiency of E160D flap endonuclease-1 mutant in vitro and in vivo is due to defective cleavage of DNA substrates. J Biol Chem 273: 33064-33072.
    • (1998) J Biol Chem , vol.273 , pp. 33064-33072
    • Frank, G.1    Qiu, J.2    Somsouk, M.3    Weng, Y.4    Somsouk, L.5    Nolan, J.P.6    Shen, B.7
  • 22
    • 18044384092 scopus 로고    scopus 로고
    • DNA polymerases that propagate the eukaryotic DNA replication fork
    • Garg P, Burgers PM. 2005a. DNA polymerases that propagate the eukaryotic DNA replication fork. Crit Rev Biochem Mol Biol 40: 115-128.
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , pp. 115-128
    • Garg, P.1    Burgers, P.M.2
  • 23
    • 25444484099 scopus 로고    scopus 로고
    • How the cell deals with DNA nicks
    • Garg P, Burgers PM. 2005b. How the cell deals with DNA nicks. Cell Cycle 4: 221-224.
    • (2005) Cell Cycle , vol.4 , pp. 221-224
    • Garg, P.1    Burgers, P.M.2
  • 24
    • 78049375876 scopus 로고    scopus 로고
    • Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading
    • Gloor JW, Balakrishnan L, Bambara RA. 2010. Flap endonuclease 1 mechanism analysis indicates flap base binding prior to threading. J Biol Chem 285: 34922-34931.
    • (2010) J Biol Chem , vol.285 , pp. 34922-34931
    • Gloor, J.W.1    Balakrishnan, L.2    Bambara, R.A.3
  • 26
    • 0034969453 scopus 로고    scopus 로고
    • Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300
    • Hasan S, Stucki M, Hassa PO, Imhof R, Gehrig P, Hunziker P, Hubscher U, Hottiger MO. 2001. Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300. Mol Cell 7: 1221-1231.
    • (2001) Mol Cell , vol.7 , pp. 1221-1231
    • Hasan, S.1    Stucki, M.2    Hassa, P.O.3    Imhof, R.4    Gehrig, P.5    Hunziker, P.6    Hubscher, U.7    Hottiger, M.O.8
  • 27
    • 0015718863 scopus 로고
    • Analysis of nucleotide pools in animal cells
    • Hauschka PV. 1973. Analysis of nucleotide pools in animal cells. Methods Cell Biol 7: 361-462.
    • (1973) Methods Cell Biol , vol.7 , pp. 361-462
    • Hauschka, P.V.1
  • 28
    • 77956525557 scopus 로고    scopus 로고
    • Components of the secondary pathway stimulate the primary pathwayof eukaryotic Okazaki fragment processing
    • Henry RA, Balakrishnan L, Ying-Lin ST, Campbell JL, Bambara RA. 2010. Components of the secondary pathway stimulate the primary pathwayof eukaryotic Okazaki fragment processing. J Biol Chem 285: 28496-28505.
    • (2010) J Biol Chem , vol.285 , pp. 28496-28505
    • Henry, R.A.1    Balakrishnan, L.2    Ying-Lin, S.T.3    Campbell, J.L.4    Bambara, R.A.5
  • 29
    • 0022180425 scopus 로고
    • Initiation of DNA synthesis by the calf thymus DNA polymerase-primase complex
    • Holmes AM, Cheriathundam E, Bollum FJ, Chang LM. 1985. Initiation of DNA synthesis by the calf thymus DNA polymerase-primase complex. J Biol Chem 260: 10840-10846.
    • (1985) J Biol Chem , vol.260 , pp. 10840-10846
    • Holmes, A.M.1    Cheriathundam, E.2    Bollum, F.J.3    Chang, L.M.4
  • 30
    • 0027448984 scopus 로고
    • Absence of a direct role for RNase HI in initiation of DNA replication at the oriC site on the Escherichia coli chromosome
    • Hong X, Kogoma T. 1993. Absence of a direct role for RNase HI in initiation of DNA replication at the oriC site on the Escherichia coli chromosome. J Bacteriol 175: 6731-6734.
    • (1993) J Bacteriol , vol.175 , pp. 6731-6734
    • Hong, X.1    Kogoma, T.2
  • 32
    • 0026544211 scopus 로고
    • Topoisomerase II plays an essential role as a swivelase in the late stage of SV40 chromosome replication in vitro
    • Ishimi Y, Sugasawa K, Hanaoka F, Eki T, Hurwitz J. 1992. Topoisomerase II plays an essential role as a swivelase in the late stage of SV40 chromosome replication in vitro. J Biol Chem 267: 462-466.
    • (1992) J Biol Chem , vol.267 , pp. 462-466
    • Ishimi, Y.1    Sugasawa, K.2    Hanaoka, F.3    Eki, T.4    Hurwitz, J.5
  • 33
    • 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: 71-96.
    • (2010) Crit Rev Biochem Mol Biol , vol.45 , pp. 71-96
    • Kang, Y.H.1    Lee, C.H.2    Seo, Y.S.3
  • 34
    • 1642545486 scopus 로고    scopus 로고
    • The protein components and mechanism of eukaryotic Okazaki fragment maturation
    • Kao HI, Bambara RA. 2003. The protein components and mechanism of eukaryotic Okazaki fragment maturation. Crit Rev Biochem Mol Biol 38: 433-452.
    • (2003) Crit Rev Biochem Mol Biol , vol.38 , pp. 433-452
    • Kao, H.I.1    Bambara, R.A.2
  • 37
    • 77949570959 scopus 로고    scopus 로고
    • Mechanism and evolution of DNA primases
    • Kuchta RD, Stengel G. 2010. Mechanism and evolution of DNA primases. Biochim Biophys Acta 1804: 1180-1189.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1180-1189
    • Kuchta, R.D.1    Stengel, G.2
  • 38
    • 0031104841 scopus 로고    scopus 로고
    • The FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair
    • Lieber MR. 1997. The FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair. Bioessays 19: 233-240.
    • (1997) Bioessays , vol.19 , pp. 233-240
    • Lieber, M.R.1
  • 39
    • 0029616338 scopus 로고
    • 0 end of the substrate to perform structure-specific cleavage
    • 0 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
  • 40
    • 0032478084 scopus 로고    scopus 로고
    • Junction ribonuclease: An activity in Okazaki fragment processing
    • Murante RS, Henricksen LA, Bambara RA. 1998. Junction ribonuclease: An activity in Okazaki fragment processing. Proc Natl Acad Sci 95: 2244-2249.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 2244-2249
    • Murante, R.S.1    Henricksen, L.A.2    Bambara, R.A.3
  • 41
    • 2442431498 scopus 로고    scopus 로고
    • The post-translational modifications of proliferating cell nuclear antigen: Acetylation, not phosphorylation, plays an important role in the regulation of its function
    • Naryzhny SN, Lee H. 2004. The post-translational modifications of proliferating cell nuclear antigen: Acetylation, not phosphorylation, plays an important role in the regulation of its function. J Biol Chem 279: 20194-20199.
    • (2004) J Biol Chem , vol.279 , pp. 20194-20199
    • Naryzhny, S.N.1    Lee, H.2
  • 42
    • 0018895114 scopus 로고
    • Discontinuous DNA replication
    • Ogawa T, Okazaki T. 1980. Discontinuous DNA replication. Annu Rev Biochem 49: 421-457.
    • (1980) Annu Rev Biochem , vol.49 , pp. 421-457
    • Ogawa, T.1    Okazaki, T.2
  • 43
    • 0014251791 scopus 로고
    • Mechanism of DNA chain growth. I. Possible discontinuity and unusual secondary structureof newly synthesized chains
    • Okazaki R, Okazaki T, Sakabe K, Sugimoto K, Sugino A. 1968. Mechanism of DNA chain growth. I. Possible discontinuity and unusual secondary structureof newly synthesized chains. Proc Natl Acad Sci 59: 598-605.
    • (1968) Proc Natl Acad Sci , vol.59 , pp. 598-605
    • Okazaki, R.1    Okazaki, T.2    Sakabe, K.3    Sugimoto, K.4    Sugino, A.5
  • 44
    • 72449204579 scopus 로고    scopus 로고
    • Coordinating DNA replication by means of priming loop and differential synthesis rate
    • Pandey M, Syed S, Donmez I, Patel G, Ha T, Patel SS. 2009. Coordinating DNA replication by means of priming loop and differential synthesis rate. Nature 462: 940-943.
    • (2009) Nature , vol.462 , pp. 940-943
    • Pandey, M.1    Syed, S.2    Donmez, I.3    Patel, G.4    Ha, T.5    Patel, S.S.6
  • 45
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli E, Chen S, Davies AA, Huttner D, Krejci L, Sung P, Ulrich HD. 2005. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol Cell 19: 123-133.
    • (2005) Mol Cell , vol.19 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 47
    • 78650630757 scopus 로고    scopus 로고
    • An alternative pathway for Okazaki fragment processing: Resolution of fold-back flaps by Pif1 helicase
    • Pike JE, Henry RA, Burgers PM, Campbell JL, Bambara RA. 2010. An alternative pathway for Okazaki fragment processing: Resolution of fold-back flaps by Pif1 helicase. J Biol Chem 285: 41712-41723.
    • (2010) J Biol Chem , vol.285 , pp. 41712-41723
    • Pike, J.E.1    Henry, R.A.2    Burgers, P.M.3    Campbell, J.L.4    Bambara, R.A.5
  • 48
    • 0037040170 scopus 로고    scopus 로고
    • Reconstitution of human DNA polymerase d using recombinant baculoviruses: The p12 subunit potentiates DNA polymerizing activity of the four-subunit enzyme
    • Podust VN, Chang LS, Ott R, Dianov GL, Fanning E. 2002. Reconstitution of human DNA polymerase d using recombinant baculoviruses: The p12 subunit potentiates DNA polymerizing activity of the four-subunit enzyme. J Biol Chem 277: 3894-3901.
    • (2002) J Biol Chem , vol.277 , pp. 3894-3901
    • Podust, V.N.1    Chang, L.S.2    Ott, R.3    Dianov, G.L.4    Fanning, E.5
  • 49
    • 34447336941 scopus 로고    scopus 로고
    • Yeast DNA polymerase epsilon participates in leading-strand DNA replication
    • Pursell ZF, Isoz I, Lundstrom EB, Johansson E, Kunkel TA. 2007. Yeast DNA polymerase epsilon participates in leading-strand DNA replication. Science 317: 127-130.
    • (2007) Science , vol.317 , pp. 127-130
    • Pursell, Z.F.1    Isoz, I.2    Lundstrom, E.B.3    Johansson, E.4    Kunkel, T.A.5
  • 50
    • 33646759589 scopus 로고    scopus 로고
    • Primer initiation and extension by T7 DNA primase
    • Qimron U, Lee SJ, Hamdan SM, Richardson CC. 2006. Primer initiation and extension by T7 DNA primase. EMBO J 25: 2199-2208.
    • (2006) EMBO J , vol.25 , pp. 2199-2208
    • Qimron, U.1    Lee, S.J.2    Hamdan, S.M.3    Richardson, C.C.4
  • 51
    • 0033512305 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease
    • Qiu J, Qian Y, Frank P, Wintersberger U, Shen B. 1999. Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease. Mol Cell Biol 19: 8361-8371.
    • (1999) Mol Cell Biol , vol.19 , pp. 8361-8371
    • Qiu, J.1    Qian, Y.2    Frank, P.3    Wintersberger, U.4    Shen, B.5
  • 52
    • 84863012802 scopus 로고    scopus 로고
    • Phosphorylation of the p68 subunit of Pol d acts as a molecular switch to regulate its interaction with PCNA
    • Rahmeh AA, Zhou Y, Xie B, Li H, Lee EY, Lee MY. 2012. Phosphorylation of the p68 subunit of Pol d acts as a molecular switch to regulate its interaction with PCNA. Biochemistry 51: 416-424.
    • (2012) Biochemistry , vol.51 , pp. 416-424
    • Rahmeh, A.A.1    Zhou, Y.2    Xie, B.3    Li, H.4    Lee, E.Y.5    Lee, M.Y.6
  • 53
    • 33748755119 scopus 로고    scopus 로고
    • Reconstituted Okazaki fragment processing indicates two pathways of primer removal
    • Rossi ML, Bambara RA. 2006. Reconstituted Okazaki fragment processing indicates two pathways of primer removal. J Biol Chem 281: 26051-26061.
    • (2006) J Biol Chem , vol.281 , pp. 26051-26061
    • Rossi, M.L.1    Bambara, R.A.2
  • 54
    • 33644633822 scopus 로고    scopus 로고
    • Lagging strand replication proteins in genome stability and DNA repair
    • Rossi ML, Purohit V, Brandt PD, Bambara RA. 2006. Lagging strand replication proteins in genome stability and DNA repair. Chem Rev 106: 453-473.
    • (2006) Chem Rev , vol.106 , pp. 453-473
    • Rossi, M.L.1    Purohit, V.2    Brandt, P.D.3    Bambara, R.A.4
  • 56
    • 0014024498 scopus 로고
    • A unique property of the replicating region of chromosomal DNA
    • Sakabe K, Okazaki R. 1966. A unique property of the replicating region of chromosomal DNA. Biochem Biophys Acta 129: 651-654.
    • (1966) Biochem Biophys Acta , vol.129 , pp. 651-654
    • Sakabe, K.1    Okazaki, R.2
  • 57
    • 0027513148 scopus 로고
    • Mechanismofcalf thymus DNA primase: Slow initiation, rapid polymerization, and intelligent termination
    • Sheaff RJ, Kuchta RD. 1993. Mechanismofcalf thymus DNA primase: Slow initiation, rapid polymerization, and intelligent termination. Biochemistry 32: 3027-3037.
    • (1993) Biochemistry , vol.32 , pp. 3027-3037
    • Sheaff, R.J.1    Kuchta, R.D.2
  • 58
    • 0028331879 scopus 로고
    • Calf thymus DNA polymerase a-primase: "Communication" and primertemplate movement between the two active sites
    • Sheaff RJ, Kuchta RD, Ilsley D. 1994. Calf thymus DNA polymerase a-primase: "Communication" and primertemplate movement between the two active sites. Biochemistry 33: 2247-2254.
    • (1994) Biochemistry , vol.33 , pp. 2247-2254
    • Sheaff, R.J.1    Kuchta, R.D.2    Ilsley, D.3
  • 59
    • 84862776917 scopus 로고    scopus 로고
    • Intrinsic coupling of lagging strand synthesis to chromatin assembly
    • Smith D, Whitehouse I. 2012. Intrinsic coupling of lagging strand synthesis to chromatin assembly. Nature 483: 434-438.
    • (2012) Nature , vol.483 , pp. 434-438
    • Smith, D.1    Whitehouse, I.2
  • 60
    • 57649114600 scopus 로고    scopus 로고
    • Dynamic removal of replication protein A by Dna2 facilitates primer cleavage during Okazaki fragment processing in Saccharomyces cerevisiae
    • Stewart JA, Miller AS, Campbell JL, Bambara RA. 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
  • 62
    • 0003914464 scopus 로고
    • 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Tooze J. 1981. DNA tumor viruses, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1981) DNA Tumor Viruses
    • Tooze, J.1
  • 63
    • 0025189911 scopus 로고
    • Functions of replication factor C and proliferating-cell nuclear antigen: Functional similarity of DNA polymerase accessory proteins from human cells and bacteriophage T4
    • Tsurimoto T, Stillman B. 1990. Functions of replication factor C and proliferating-cell nuclear antigen: Functional similarity of DNA polymerase accessory proteins from human cells and bacteriophage T4. Proc Natl Acad Sci 87: 1023-1027.
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 1023-1027
    • Tsurimoto, T.1    Stillman, B.2
  • 64
    • 0025328320 scopus 로고
    • Sequential initiation of lagging and leading strand synthesis by two different polymerase complexes at the SV40 DNA replication origin
    • Tsurimoto T, Melendy T, Stillman B. 1990. Sequential initiation of lagging and leading strand synthesis by two different polymerase complexes at the SV40 DNA replication origin. Nature 346: 534-539.
    • (1990) Nature , vol.346 , pp. 534-539
    • Tsurimoto, T.1    Melendy, T.2    Stillman, B.3
  • 67
    • 0031663505 scopus 로고    scopus 로고
    • The DNA replication fork in eukaryotic cells
    • Waga S, Stillman B. 1998. The DNA replication fork in eukaryotic cells. Annu Rev Biochem 67: 721-751.
    • (1998) Annu Rev Biochem , vol.67 , pp. 721-751
    • Waga, S.1    Stillman, B.2
  • 68
    • 0028363546 scopus 로고
    • Reconstitution of complete SV40 DNA replication with purified replication factors
    • Waga S, Bauer G, Stillman B. 1994. Reconstitution of complete SV40 DNA replication with purified replication factors. J Biol Chem 269: 10923-10934.
    • (1994) J Biol Chem , vol.269 , pp. 10923-10934
    • Waga, S.1    Bauer, G.2    Stillman, B.3
  • 70
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold MS. 1997. Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. AnnuRev Biochem 66:61-92.
    • (1997) AnnuRev Biochem , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 71
    • 0033534380 scopus 로고    scopus 로고
    • Trading places on DNA-A three-point switch underlies primer handoff from primase to the replicative DNA polymerase
    • Yuzhakov A, Kelman Z, O'Donnell M. 1999. Trading places on DNA-A three-point switch underlies primer handoff from primase to the replicative DNA polymerase. Cell 96: 153-163.
    • (1999) Cell , vol.96 , pp. 153-163
    • Yuzhakov, A.1    Kelman, Z.2    O'Donnell, M.3
  • 72
    • 0025640874 scopus 로고
    • Accuracyof DNA primase
    • Zhang SS, Grosse F. 1990. Accuracyof DNA primase. J Molec Biol 216: 475-479.
    • (1990) J Molec Biol , vol.216 , pp. 475-479
    • Zhang, S.S.1    Grosse, F.2
  • 73
    • 79951500316 scopus 로고    scopus 로고
    • Okazaki fragment maturation: Nucleases take centre stage
    • Zheng L, Shen B. 2011. Okazaki fragment maturation: Nucleases take centre stage. J Mol Cell Biol 3: 23-30.
    • (2011) J Mol Cell Biol , vol.3 , pp. 23-30
    • Zheng, L.1    Shen, B.2
  • 74
    • 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 DF, 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


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