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Volumn 4, Issue MAY, 2015, Pages

Cooperative base pair melting by helicase and polymerase positioned one nucleotide from each other

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; HELICASE; NUCLEOSIDE TRIPHOSPHATE; OLIGONUCLEOTIDE; 2 AMINOPURINE; DNA DIRECTED DNA POLYMERASE; DNA HELICASE; DNA PRIMASE;

EID: 84930635063     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.06562     Document Type: Article
Times cited : (30)

References (50)
  • 1
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • Ali JA, Lohman TM (1997) Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science 275: 377-380
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 3
    • 18244371925 scopus 로고    scopus 로고
    • Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint
    • Byun TS, Pacek M, Yee MC, Walter JC, Cimprich KA (2005) Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint. Genes & development 19: 1040-1052
    • (2005) Genes & development , vol.19 , pp. 1040-1052
    • Byun, T.S.1    Pacek, M.2    Yee, M.C.3    Walter, J.C.4    Cimprich, K.A.5
  • 5
    • 30744451401 scopus 로고    scopus 로고
    • DNA-induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase
    • Crampton DJ, Mukherjee S, Richardson CC (2006) DNA-induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase. Molecular cell 21: 165-174
    • (2006) Molecular cell , vol.21 , pp. 165-174
    • Crampton, D.J.1    Mukherjee, S.2    Richardson, C.C.3
  • 6
    • 84860271761 scopus 로고    scopus 로고
    • DNA polymerases: Mechanistic insight from biochemical and biophysical studies
    • Delagoutte E (2012) DNA polymerases: mechanistic insight from biochemical and biophysical studies. Frontiers in bioscience 17: 509-544
    • (2012) Frontiers in bioscience , vol.17 , pp. 509-544
    • Delagoutte, E.1
  • 7
    • 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 PH (2001) Molecular mechanisms of the functional coupling of the helicase (gp41) and polymerase (gp43) of bacteriophage T4 within the DNA replication fork. Biochemistry 40: 4459-4477
    • (2001) Biochemistry , vol.40 , pp. 4459-4477
    • Delagoutte, E.1    von Hippel, P.H.2
  • 8
    • 47049093279 scopus 로고    scopus 로고
    • Coupling of DNA unwinding to nucleotide hydrolysis in a ring shaped helicase
    • Donmez I, Patel SS (2008) Coupling of DNA unwinding to nucleotide hydrolysis in a ring shaped helicase. The EMBO journal 27: 1718-1726
    • (2008) The EMBO journal , vol.27 , pp. 1718-1726
    • Donmez, I.1    Patel, S.S.2
  • 9
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2 2 A resolution
    • Doublie S, Tabor S, Long AM, Richardson CC, Ellenberger T (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution. Nature 391: 251-258
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 10
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • Enemark EJ, Joshua-Tor L (2006) Mechanism of DNA translocation in a replicative hexameric helicase. Nature 442: 270-275
    • (2006) Nature , vol.442 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 11
    • 4644358568 scopus 로고    scopus 로고
    • Unzipping mechanism of the double-stranded DNA unwinding by a hexameric helicase: The effect of the 3' arm and the stability of the dsDNA on the unwinding activity of the Escherichia coli DnaB helicase
    • Galletto R, Jezewska MJ, Bujalowski W (2004) Unzipping mechanism of the double-stranded DNA unwinding by a hexameric helicase: the effect of the 3' arm and the stability of the dsDNA on the unwinding activity of the Escherichia coli DnaB helicase. Journal of molecular biology 343: 101-114
    • (2004) Journal of molecular biology , vol.343 , pp. 101-114
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 14
    • 0027373139 scopus 로고
    • Interactions of bacteriophage T7 DNA A primase/helicase protein with single-stranded and double-stranded DNAs
    • Hingorani MM, Patel SS (1993) Interactions of bacteriophage T7 DNA A primase/helicase protein with single-stranded and double-stranded DNAs. Biochemistry 32: 12478-12487
    • (1993) Biochemistry , vol.32 , pp. 12478-12487
    • Hingorani, M.M.1    Patel, S.S.2
  • 16
    • 34250766751 scopus 로고    scopus 로고
    • Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase
    • Johnson DS, Bai L, Smith BY, Patel SS, Wang MD (2007) Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase. Cell 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
  • 20
    • 0036382873 scopus 로고    scopus 로고
    • T7 DNA helicase: A molecular motor that processively and unidirectionally translocates along single-stranded DNA
    • Kim DE, Narayan M, Patel SS (2002) T7 DNA helicase: a molecular motor that processively and unidirectionally translocates along single-stranded DNA. Journal of molecular biology 321: 807-819
    • (2002) Journal of molecular biology , vol.321 , pp. 807-819
    • Kim, D.E.1    Narayan, M.2    Patel, S.S.3
  • 21
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: A tau-DnaB interaction mediates rapid replication fork movement
    • Kim S, Dallmann HG, McHenry CS, Marians KJ (1996) Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement. Cell 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
  • 30
    • 34548507222 scopus 로고    scopus 로고
    • Replisome fate upon encountering a leading strand block and clearance from DNA by recombination proteins
    • McInerney P, O'Donnell M (2007) Replisome fate upon encountering a leading strand block and clearance from DNA by recombination proteins. The Journal of biological chemistry 282: 25903-25916
    • (2007) The Journal of biological chemistry , vol.282 , pp. 25903-25916
    • McInerney, P.1    O'Donnell, M.2
  • 31
    • 0016707291 scopus 로고
    • Physical studies of the interaction between the Escherichia coli DNA binding protein and nucleic acids
    • Molineux IJ, Pauli A, Gefter ML (1975) Physical studies of the interaction between the Escherichia coli DNA binding protein and nucleic acids. Nucleic acids research 2: 1821-1837
    • (1975) Nucleic acids research , vol.2 , pp. 1821-1837
    • Molineux, I.J.1    Pauli, A.2    Gefter, M.L.3
  • 32
    • 0023700060 scopus 로고
    • Mechanism of stimulation of T7 DNA polymerase by Escherichia coli single-stranded DNA binding protein (SSB)
    • Myers TW, Romano LJ (1988) Mechanism of stimulation of T7 DNA polymerase by Escherichia coli single-stranded DNA binding protein (SSB). The Journal of biological chemistry 263: 17006-17015
    • (1988) The Journal of biological chemistry , vol.263 , pp. 17006-17015
    • Myers, T.W.1    Romano, L.J.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 CC (1988) The effect of the T7 and Escherichia coli DNA-binding proteins at the replication fork of bacteriophage T7. The Journal of biological chemistry 263: 9831-9839
    • (1988) The Journal of biological chemistry , vol.263 , pp. 9831-9839
    • Nakai, H.1    Richardson, C.C.2
  • 35
    • 77952995507 scopus 로고    scopus 로고
    • Experimental and computational analysis of DNA unwinding and polymerization kinetics
    • Pandey M, Levin MK, Patel SS (2010) Experimental and computational analysis of DNA unwinding and polymerization kinetics. Methods in molecular biology 587: 57-83
    • (2010) Methods in molecular biology , vol.587 , pp. 57-83
    • Pandey, M.1    Levin, M.K.2    Patel, S.S.3
  • 36
    • 84897057195 scopus 로고    scopus 로고
    • Helicase and polymerase move together close to the fork junction and copy DNA in one-nucleotide steps
    • Pandey M, Patel SS (2014) Helicase and polymerase move together close to the fork junction and copy DNA in one-nucleotide steps. Cell reports 6: 1129-1138
    • (2014) Cell reports , vol.6 , pp. 1129-1138
    • Pandey, M.1    Patel, S.S.2
  • 37
    • 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
  • 38
    • 80053575452 scopus 로고    scopus 로고
    • Dynamic coupling between the motors of DNA replication: Hexameric helicase, DNA polymerase, and primase
    • Patel SS, Pandey M, Nandakumar D (2011) Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase. Current opinion in chemical biology 15: 595-605
    • (2011) Current opinion in chemical biology , vol.15 , pp. 595-605
    • Patel, S.S.1    Pandey, M.2    Nandakumar, D.3
  • 40
    • 0026033193 scopus 로고
    • Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant
    • Patel SS, Wong I, Johnson KA (1991) Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. Biochemistry 30: 511-525
    • (1991) Biochemistry , vol.30 , pp. 511-525
    • Patel, S.S.1    Wong, I.2    Johnson, K.A.3
  • 41
    • 68349148711 scopus 로고    scopus 로고
    • The use of 2-aminopurine fluorescence to study DNA polymerase function
    • Reha-Krantz LJ (2009) The use of 2-aminopurine fluorescence to study DNA polymerase function. Methods in molecular biology 521: 381-396
    • (2009) Methods in molecular biology , vol.521 , pp. 381-396
    • Reha-Krantz, L.J.1
  • 43
    • 84876108565 scopus 로고    scopus 로고
    • Dpb2 integrates the leading-strand DNA polymerase into the eukaryotic replisome
    • Sengupta S, van Deursen F, de Piccoli G, Labib K (2013) Dpb2 integrates the leading-strand DNA polymerase into the eukaryotic replisome. Current biology: CB 23: 543-552
    • (2013) Current biology: CB , vol.23 , pp. 543-552
    • Sengupta, S.1    van Deursen, F.2    de Piccoli, G.3    Labib, K.4
  • 44
    • 19644399070 scopus 로고    scopus 로고
    • DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase
    • Stano NM, Jeong YJ, Donmez I, Tummalapalli P, Levin MK, Patel SS (2005) DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase. Nature 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
  • 46
    • 85056017495 scopus 로고    scopus 로고
    • Unravelling the mechanism of RNA-polymerase forward motion by using mechanical force
    • Thomen P, Lopez PJ, Heslot F (2005) Unravelling the mechanism of RNA-polymerase forward motion by using mechanical force. Physical review letters 94: 128102
    • (2005) Physical review letters , vol.94 , pp. 128102
    • Thomen, P.1    Lopez, P.J.2    Heslot, F.3
  • 47
    • 70350344051 scopus 로고    scopus 로고
    • Running in reverse: The structural basis for translocation polarity in hexameric helicases
    • Thomsen ND, Berger JM (2009) Running in reverse: the structural basis for translocation polarity in hexameric helicases. Cell 139: 523-534
    • (2009) Cell , vol.139 , pp. 523-534
    • Thomsen, N.D.1    Berger, J.M.2
  • 49
    • 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 CS (2009) Strand displacement by DNA polymerase III occurs through a tau-psi-chi link to single-stranded DNA-binding protein coating the lagging strand template. The Journal of biological chemistry 284: 31672-31679
    • (2009) The Journal of biological chemistry , vol.284 , pp. 31672-31679
    • Yuan, Q.1    McHenry, C.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.