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Volumn 6, Issue 6, 2014, Pages 1129-1138

Helicase and Polymerase Move Together Close to the Fork Junction and Copy DNA in One-Nucleotide Steps

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSINE; DNA; DNA HELICASE; DNA POLYMERASE; GUANINE; NUCLEOTIDE; NUCLEOTIDE TRIPHOSPHATE; SINGLE STRANDED DNA; T7 DNA POLYMERASE; T7 GP4 HELICASE; UNCLASSIFIED DRUG; GP4 HELICASE; HELICASE; DNA BINDING PROTEIN; DNA DIRECTED DNA POLYMERASE;

EID: 84897057195     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2014.02.025     Document Type: Article
Times cited : (41)

References (53)
  • 2
    • 18244371925 scopus 로고    scopus 로고
    • Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint
    • Byun T.S., Pacek M., Yee M.C., Walter J.C., Cimprich K.A. Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint. Genes Dev. 2005, 19:1040-1052.
    • (2005) Genes Dev. , vol.19 , pp. 1040-1052
    • Byun, T.S.1    Pacek, M.2    Yee, M.C.3    Walter, J.C.4    Cimprich, K.A.5
  • 3
    • 0024362231 scopus 로고
    • The bacteriophage T4 DNA replication fork. Only DNA helicase is required for leading strand DNA synthesis by the DNA polymerase holoenzyme
    • Cha T.A., Alberts B.M. The bacteriophage T4 DNA replication fork. Only DNA helicase is required for leading strand DNA synthesis by the DNA polymerase holoenzyme. J.Biol. Chem. 1989, 264:12220-12225.
    • (1989) J.Biol. Chem. , vol.264 , pp. 12220-12225
    • Cha, T.A.1    Alberts, B.M.2
  • 4
    • 0028128913 scopus 로고
    • DNA double helix promotes a linkage isomerization reaction in trans-diamminedichloroplatinum(II)-modified DNA
    • Dalbiès R., Payet D., Leng M. DNA double helix promotes a linkage isomerization reaction in trans-diamminedichloroplatinum(II)-modified DNA. Proc. Natl. Acad. Sci. USA 1994, 91:8147-8151.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8147-8151
    • Dalbiès, R.1    Payet, D.2    Leng, M.3
  • 5
    • 0028938409 scopus 로고
    • Linkage isomerization reaction of intrastrand cross-links in trans-diamminedichloroplatinum(II)-modified single-stranded oligonucleotides
    • Dalbiès R., Boudvillain M., Leng M. Linkage isomerization reaction of intrastrand cross-links in trans-diamminedichloroplatinum(II)-modified single-stranded oligonucleotides. Nucleic Acids Res. 1995, 23:949-953.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 949-953
    • Dalbiès, R.1    Boudvillain, M.2    Leng, M.3
  • 6
    • 0035836479 scopus 로고    scopus 로고
    • Molecular mechanisms of the functional coupling of the helicase (gp41) and polymerase (gp43) of bacteriophage T4 within the DNA replication fork
    • Delagoutte E., von Hippel P.H. Molecular mechanisms of the functional coupling of the helicase (gp41) and polymerase (gp43) of bacteriophage T4 within the DNA replication fork. Biochemistry 2001, 40:4459-4477.
    • (2001) Biochemistry , vol.40 , pp. 4459-4477
    • Delagoutte, E.1    von Hippel, P.H.2
  • 7
    • 0029905072 scopus 로고    scopus 로고
    • A coupled complex of T4 DNA replication helicase (gp41) and polymerase (gp43) can perform rapid and processive DNA strand-displacement synthesis
    • Dong F., Weitzel S.E., von Hippel P.H. A coupled complex of T4 DNA replication helicase (gp41) and polymerase (gp43) can perform rapid and processive DNA strand-displacement synthesis. Proc. Natl. Acad. Sci. USA 1996, 93:14456-14461.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14456-14461
    • Dong, F.1    Weitzel, S.E.2    von Hippel, P.H.3
  • 8
    • 47049093279 scopus 로고    scopus 로고
    • Coupling of DNA unwinding to nucleotide hydrolysis in a ring-shaped helicase
    • Donmez I., Patel S.S. Coupling of DNA unwinding to nucleotide hydrolysis in a ring-shaped helicase. EMBO J. 2008, 27:1718-1726.
    • (2008) EMBO J. , vol.27 , pp. 1718-1726
    • Donmez, I.1    Patel, S.S.2
  • 9
    • 34547118809 scopus 로고    scopus 로고
    • Nucleic acid unwinding by hepatitis C virus and bacteriophage T7 helicases is sensitive to base pair stability
    • Donmez I., Rajagopal V., Jeong Y.J., Patel S.S. Nucleic acid unwinding by hepatitis C virus and bacteriophage T7 helicases is sensitive to base pair stability. J.Biol. Chem. 2007, 282:21116-21123.
    • (2007) J.Biol. Chem. , vol.282 , pp. 21116-21123
    • Donmez, I.1    Rajagopal, V.2    Jeong, Y.J.3    Patel, S.S.4
  • 10
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • Doublié S., Tabor S., Long A.M., Richardson C.C., Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution. Nature 1998, 391:251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublié, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 11
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • Enemark E.J., Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 2006, 442:270-275.
    • (2006) Nature , vol.442 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 12
    • 4644261530 scopus 로고    scopus 로고
    • Unzipping mechanism of the double-stranded DNA unwinding by a hexameric helicase: quantitative analysis of the rate of the dsDNA unwinding, processivity and kinetic step-size of the Escherichia coli DnaB helicase using rapid quench-flow method
    • Galletto R., Jezewska M.J., Bujalowski W. Unzipping mechanism of the double-stranded DNA unwinding by a hexameric helicase: quantitative analysis of the rate of the dsDNA unwinding, processivity and kinetic step-size of the Escherichia coli DnaB helicase using rapid quench-flow method. J.Mol. Biol. 2004, 343:83-99.
    • (2004) J.Mol. Biol. , vol.343 , pp. 83-99
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 13
    • 67650741773 scopus 로고    scopus 로고
    • Motors, switches, and contacts in the replisome
    • Hamdan S.M., Richardson C.C. Motors, switches, and contacts in the replisome. Annu. Rev. Biochem. 2009, 78:205-243.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 205-243
    • Hamdan, S.M.1    Richardson, C.C.2
  • 14
    • 0030045742 scopus 로고    scopus 로고
    • Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases
    • Hingorani M.M., Patel S.S. Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases. Biochemistry 1996, 35:2218-2228.
    • (1996) Biochemistry , vol.35 , pp. 2218-2228
    • Hingorani, M.M.1    Patel, S.S.2
  • 15
    • 65549153598 scopus 로고    scopus 로고
    • Translesion DNA polymerases remodel the replisome and alter the speed of the replicative helicase
    • Indiani C., Langston L.D., Yurieva O., Goodman M.F., O'Donnell M. Translesion DNA polymerases remodel the replisome and alter the speed of the replicative helicase. Proc. Natl. Acad. Sci. USA 2009, 106:6031-6038.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 6031-6038
    • Indiani, C.1    Langston, L.D.2    Yurieva, O.3    Goodman, M.F.4    O'Donnell, M.5
  • 16
    • 84867538324 scopus 로고    scopus 로고
    • The hexameric helicase DnaB adopts a nonplanar conformation during translocation
    • Itsathitphaisarn O., Wing R.A., Eliason W.K., Wang J., Steitz T.A. The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell 2012, 151:267-277.
    • (2012) Cell , vol.151 , pp. 267-277
    • Itsathitphaisarn, O.1    Wing, R.A.2    Eliason, W.K.3    Wang, J.4    Steitz, T.A.5
  • 17
    • 2442513338 scopus 로고    scopus 로고
    • The DNA-unwinding mechanism of the ring helicase of bacteriophage T7
    • Jeong Y.J., Levin M.K., Patel S.S. The DNA-unwinding mechanism of the ring helicase of bacteriophage T7. Proc. Natl. Acad. Sci. USA 2004, 101:7264-7269.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7264-7269
    • Jeong, Y.J.1    Levin, M.K.2    Patel, S.S.3
  • 18
    • 34250766751 scopus 로고    scopus 로고
    • Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase
    • Johnson D.S., Bai L., Smith B.Y., Patel S.S., Wang M.D. Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase. Cell 2007, 129:1299-1309.
    • (2007) Cell , vol.129 , pp. 1299-1309
    • Johnson, D.S.1    Bai, L.2    Smith, B.Y.3    Patel, S.S.4    Wang, M.D.5
  • 19
    • 84865989446 scopus 로고    scopus 로고
    • Breathing fluctuations in position-specific DNA base pairs are involved in regulating helicase movement into the replication fork
    • Jose D., Weitzel S.E., von Hippel P.H. Breathing fluctuations in position-specific DNA base pairs are involved in regulating helicase movement into the replication fork. Proc. Natl. Acad. Sci. USA 2012, 109:14428-14433.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 14428-14433
    • Jose, D.1    Weitzel, S.E.2    von Hippel, P.H.3
  • 20
    • 84859980381 scopus 로고    scopus 로고
    • Properties of the human Cdc45/Mcm2-7/GINS helicase complex and its action with DNA polymerase epsilon in rolling circle DNA synthesis
    • Kang Y.H., Galal W.C., Farina A., Tappin I., Hurwitz J. Properties of the human Cdc45/Mcm2-7/GINS helicase complex and its action with DNA polymerase epsilon in rolling circle DNA synthesis. Proc. Natl. Acad. Sci. USA 2012, 109:6042-6047.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6042-6047
    • Kang, Y.H.1    Galal, W.C.2    Farina, A.3    Tappin, I.4    Hurwitz, J.5
  • 22
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement
    • Kim S., Dallmann H.G., McHenry C.S., Marians K.J. Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement. Cell 1996, 84:643-650.
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 23
    • 0036382873 scopus 로고    scopus 로고
    • T7 DNA helicase: a molecular motor that processively and unidirectionally translocates along single-stranded DNA
    • Kim D.E., Narayan M., Patel S.S. T7 DNA helicase: a molecular motor that processively and unidirectionally translocates along single-stranded DNA. J.Mol. Biol. 2002, 321:807-819.
    • (2002) J.Mol. Biol. , vol.321 , pp. 807-819
    • Kim, D.E.1    Narayan, M.2    Patel, S.S.3
  • 25
    • 84869049993 scopus 로고    scopus 로고
    • An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome
    • Kulczyk A.W., Akabayov B., Lee S.J., Bostina M., Berkowitz S.A., Richardson C.C. An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome. J.Biol. Chem. 2012, 287:39050-39060.
    • (2012) J.Biol. Chem. , vol.287 , pp. 39050-39060
    • Kulczyk, A.W.1    Akabayov, B.2    Lee, S.J.3    Bostina, M.4    Berkowitz, S.A.5    Richardson, C.C.6
  • 27
    • 84875884170 scopus 로고    scopus 로고
    • Structure of the PolIIIα-τc-DNA complex suggests an atomic model of the replisome
    • Liu B., Lin J., Steitz T.A. Structure of the PolIIIα-τc-DNA complex suggests an atomic model of the replisome. Structure 2013, 21:658-664.
    • (2013) Structure , vol.21 , pp. 658-664
    • Liu, B.1    Lin, J.2    Steitz, T.A.3
  • 28
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: mechanisms and regulation
    • Lohman T.M., Tomko E.J., Wu C.G. Non-hexameric DNA helicases and translocases: mechanisms and regulation. Nat. Rev. Mol. Cell Biol. 2008, 9:391-401.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 391-401
    • Lohman, T.M.1    Tomko, E.J.2    Wu, C.G.3
  • 30
    • 84864447544 scopus 로고    scopus 로고
    • Collaborative coupling between polymerase and helicase for leading-strand synthesis
    • Manosas M., Spiering M.M., Ding F., Croquette V., Benkovic S.J. Collaborative coupling between polymerase and helicase for leading-strand synthesis. Nucleic Acids Res. 2012, 40:6187-6198.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 6187-6198
    • Manosas, M.1    Spiering, M.M.2    Ding, F.3    Croquette, V.4    Benkovic, S.J.5
  • 31
    • 0021046123 scopus 로고
    • DNA-dependent nucleoside 5'-triphosphatase activity of the gene 4 protein of bacteriophage T7
    • Matson S.W., Richardson C.C. DNA-dependent nucleoside 5'-triphosphatase activity of the gene 4 protein of bacteriophage T7. J.Biol. Chem. 1983, 258:14009-14016.
    • (1983) J.Biol. Chem. , vol.258 , pp. 14009-14016
    • Matson, S.W.1    Richardson, C.C.2
  • 32
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • Meyer R.R., Laine P.S. The single-stranded DNA-binding protein of Escherichia coli. Microbiol. Rev. 1990, 54:342-380.
    • (1990) Microbiol. Rev. , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 33
    • 0023726250 scopus 로고
    • The effect of the T7 and Escherichia coli DNA-binding proteins at the replication fork of bacteriophage T7
    • Nakai H., Richardson C.C. The effect of the T7 and Escherichia coli DNA-binding proteins at the replication fork of bacteriophage T7. J.Biol. Chem. 1988, 263:9831-9839.
    • (1988) J.Biol. Chem. , vol.263 , pp. 9831-9839
    • Nakai, H.1    Richardson, C.C.2
  • 34
    • 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 S.S. Coordinating DNA replication by means of priming loop and differential synthesis rate. Nature 2009, 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
  • 35
    • 77952995507 scopus 로고    scopus 로고
    • Experimental and computational analysis of DNA unwinding and polymerization kinetics
    • Pandey M., Levin M.K., Patel S.S. Experimental and computational analysis of DNA unwinding and polymerization kinetics. Methods Mol. Biol. 2010, 587:57-83.
    • (2010) Methods Mol. Biol. , vol.587 , pp. 57-83
    • Pandey, M.1    Levin, M.K.2    Patel, S.S.3
  • 36
    • 0033230823 scopus 로고    scopus 로고
    • NMR solution structure of a DNA dodecamer containing a transplatin interstrand GN7-CN3 cross-link
    • Paquet F., Boudvillain M., Lancelot G., Leng M. NMR solution structure of a DNA dodecamer containing a transplatin interstrand GN7-CN3 cross-link. Nucleic Acids Res. 1999, 27:4261-4268.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4261-4268
    • Paquet, F.1    Boudvillain, M.2    Lancelot, G.3    Leng, M.4
  • 37
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel S.S., Picha K.M. Structure and function of hexameric helicases. Annu. Rev. Biochem. 2000, 69:651-697.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 38
    • 33745823112 scopus 로고    scopus 로고
    • Mechanisms of helicases
    • Patel S.S., Donmez I. Mechanisms of helicases. J.Biol. Chem. 2006, 281:18265-18268.
    • (2006) J.Biol. Chem. , vol.281 , pp. 18265-18268
    • Patel, S.S.1    Donmez, I.2
  • 39
    • 0026033193 scopus 로고
    • Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant
    • Patel S.S., Wong I., Johnson K.A. Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. Biochemistry 1991, 30:511-525.
    • (1991) Biochemistry , vol.30 , pp. 511-525
    • Patel, S.S.1    Wong, I.2    Johnson, K.A.3
  • 40
    • 0026651756 scopus 로고
    • Large scale purification and biochemical characterization of T7 primase/helicase proteins. Evidence for homodimer and heterodimer formation
    • Patel S.S., Rosenberg A.H., Studier F.W., Johnson K.A. Large scale purification and biochemical characterization of T7 primase/helicase proteins. Evidence for homodimer and heterodimer formation. J.Biol. Chem. 1992, 267:15013-15021.
    • (1992) J.Biol. Chem. , vol.267 , pp. 15013-15021
    • Patel, S.S.1    Rosenberg, A.H.2    Studier, F.W.3    Johnson, K.A.4
  • 41
    • 79958004688 scopus 로고    scopus 로고
    • A257T linker region mutant of T7 helicase-primase protein is defective in DNA loading and rescued by T7 DNA polymerase
    • Patel G., Johnson D.S., Sun B., Pandey M., Yu X., Egelman E.H., Wang M.D., Patel S.S. A257T linker region mutant of T7 helicase-primase protein is defective in DNA loading and rescued by T7 DNA polymerase. J.Biol. Chem. 2011, 286:20490-20499.
    • (2011) J.Biol. Chem. , vol.286 , pp. 20490-20499
    • Patel, G.1    Johnson, D.S.2    Sun, B.3    Pandey, M.4    Yu, X.5    Egelman, E.H.6    Wang, M.D.7    Patel, S.S.8
  • 42
    • 80053575452 scopus 로고    scopus 로고
    • Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase
    • Patel S.S., Pandey M., Nandakumar D. Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase. Curr. Opin. Chem. Biol. 2011, 15:595-605.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 595-605
    • Patel, S.S.1    Pandey, M.2    Nandakumar, D.3
  • 43
    • 0037184944 scopus 로고    scopus 로고
    • Essential amino acid residues in the single-stranded DNA-binding protein of bacteriophage T7. Identification of the dimer interface
    • Rezende L.F., Hollis T., Ellenberger T., Richardson C.C. Essential amino acid residues in the single-stranded DNA-binding protein of bacteriophage T7. Identification of the dimer interface. J.Biol. Chem. 2002, 277:50643-50653.
    • (2002) J.Biol. Chem. , vol.277 , pp. 50643-50653
    • Rezende, L.F.1    Hollis, T.2    Ellenberger, T.3    Richardson, C.C.4
  • 44
    • 77958475756 scopus 로고    scopus 로고
    • DnaB helicase activity is modulated by DNA geometry and force
    • Ribeck N., Kaplan D.L., Bruck I., Saleh O.A. DnaB helicase activity is modulated by DNA geometry and force. Biophys. J. 2010, 99:2170-2179.
    • (2010) Biophys. J. , vol.99 , pp. 2170-2179
    • Ribeck, N.1    Kaplan, D.L.2    Bruck, I.3    Saleh, O.A.4
  • 45
    • 0028972546 scopus 로고
    • Helix-destabilizing activity of phi 29 single-stranded DNA binding protein: effect on the elongation rate during strand displacement DNA replication
    • Soengas M.S., Gutiérrez C., Salas M. Helix-destabilizing activity of phi 29 single-stranded DNA binding protein: effect on the elongation rate during strand displacement DNA replication. J.Mol. Biol. 1995, 253:517-529.
    • (1995) J.Mol. Biol. , vol.253 , pp. 517-529
    • Soengas, M.S.1    Gutiérrez, C.2    Salas, M.3
  • 46
    • 19644399070 scopus 로고    scopus 로고
    • DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase
    • Stano N.M., Jeong Y.J., Donmez I., Tummalapalli P., Levin M.K., Patel S.S. DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase. Nature 2005, 435:370-373.
    • (2005) Nature , vol.435 , pp. 370-373
    • Stano, N.M.1    Jeong, Y.J.2    Donmez, I.3    Tummalapalli, P.4    Levin, M.K.5    Patel, S.S.6
  • 48
    • 84897037131 scopus 로고    scopus 로고
    • Single molecule fluorescence reveals the unwinding stepping mechanism of replicative helicase
    • Published online March 13, 2014
    • Syed S., Pandey M., Patel S.S., Ha T. Single molecule fluorescence reveals the unwinding stepping mechanism of replicative helicase. Cell Rep. 2014, 6. Published online March 13, 2014. 10.1016/j.celrep.2014.02.022.
    • (2014) Cell Rep. , vol.6
    • Syed, S.1    Pandey, M.2    Patel, S.S.3    Ha, T.4
  • 49
    • 70350344051 scopus 로고    scopus 로고
    • Running in reverse: the structural basis for translocation polarity in hexameric helicases
    • Thomsen N.D., Berger J.M. Running in reverse: the structural basis for translocation polarity in hexameric helicases. Cell 2009, 139:523-534.
    • (2009) Cell , vol.139 , pp. 523-534
    • Thomsen, N.D.1    Berger, J.M.2
  • 50
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • Yin Y.W., Steitz T.A. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science 2002, 298:1387-1395.
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2
  • 51
    • 1342313235 scopus 로고    scopus 로고
    • The structural mechanism of translocation and helicase activity in T7 RNA polymerase
    • Yin Y.W., Steitz T.A. The structural mechanism of translocation and helicase activity in T7 RNA polymerase. Cell 2004, 116:393-404.
    • (2004) Cell , vol.116 , pp. 393-404
    • Yin, Y.W.1    Steitz, T.A.2
  • 52
    • 70450269266 scopus 로고    scopus 로고
    • Strand displacement by DNA polymerase III occurs through a tau-psi-chi link to single-stranded DNA-binding protein coating the lagging strand template
    • Yuan Q., McHenry C.S. Strand displacement by DNA polymerase III occurs through a tau-psi-chi link to single-stranded DNA-binding protein coating the lagging strand template. J.Biol. Chem. 2009, 284:31672-31679.
    • (2009) J.Biol. Chem. , vol.284 , pp. 31672-31679
    • Yuan, Q.1    McHenry, C.S.2
  • 53


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