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Volumn 44, Issue 51, 2005, Pages 16967-16976

Mechanism of translocation and kinetics of DNA unwinding by the helicase RecG

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYME KINETICS; ENZYMES; HYDROLYSIS; REACTION KINETICS;

EID: 29344449133     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0512851     Document Type: Article
Times cited : (35)

References (39)
  • 1
    • 0036211179 scopus 로고    scopus 로고
    • Modularity and specialization in superfamily 1 and 2 helicases
    • Singleton, M. R., and Wigley, D. B. (2002) Modularity and specialization in superfamily 1 and 2 helicases, J. Bacteriol. 184, 1819-1826.
    • (2002) J. Bacteriol. , vol.184 , pp. 1819-1826
    • Singleton, M.R.1    Wigley, D.B.2
  • 2
    • 2442676334 scopus 로고    scopus 로고
    • Prokaryotic and eukaryotic DNA helicases: Essential molecular motors for cellular machinery
    • Tuteja, N., and Tuteja, R. (2004) Prokaryotic and eukaryotic DNA helicases: Essential molecular motors for cellular machinery, Eur. J. Biochem. 271, 1835-1848.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1835-1848
    • Tuteja, N.1    Tuteja, R.2
  • 3
    • 0034737294 scopus 로고    scopus 로고
    • Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression
    • McGlynn, P., and Lloyd, R. G. (2000) Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression, Cell 101, 35-45.
    • (2000) Cell , vol.101 , pp. 35-45
    • McGlynn, P.1    Lloyd, R.G.2
  • 4
    • 0035902573 scopus 로고    scopus 로고
    • Formation of Holliday junctions by regression of nascent DNA in intermediates containing stalled replication forks: RecG stimulates regression even when the DNA is negatively supercoiled
    • McGlynn, P., Lloyd, R. G., and Marians, K. J. (2001) Formation of Holliday junctions by regression of nascent DNA in intermediates containing stalled replication forks: recG stimulates regression even when the DNA is negatively supercoiled, Proc. Natl. Acad. Sci. U.S.A. 98, 8235-8240.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8235-8240
    • McGlynn, P.1    Lloyd, R.G.2    Marians, K.J.3
  • 5
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • Singleton, M. R., Scaife, S., and Wigley, D. B. (2001) Structural analysis of DNA replication fork reversal by RecG, Cell 107, 79-89.
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 6
    • 0035902591 scopus 로고    scopus 로고
    • Rescue of stalled replication forks by recG: Simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation
    • McGlynn, P., and Lloyd, R. G. (2001) Rescue of stalled replication forks by recG: Simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation, Proc. Natl. Acad. Sci. U.S.A. 98, 8227-8234.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8227-8234
    • McGlynn, P.1    Lloyd, R.G.2
  • 7
    • 17144385089 scopus 로고    scopus 로고
    • DNA binding by the substrate specificity (Wedge) Domain of RecG helicase suggests a role in processivity
    • Briggs, G. S., Mahdi, A. A., Wen, Q., and Lloyd, R. G. (2005) DNA Binding by the Substrate Specificity (Wedge) Domain of RecG Helicase Suggests a Role in Processivity, J. Biol. Chem. 280, 13921-13927.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13921-13927
    • Briggs, G.S.1    Mahdi, A.A.2    Wen, Q.3    Lloyd, R.G.4
  • 8
    • 0032584598 scopus 로고    scopus 로고
    • Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli
    • Whitby, M. C., and Lloyd, R. G. (1998) Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli, J. Biol. Chem. 273, 19729-19739.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19729-19739
    • Whitby, M.C.1    Lloyd, R.G.2
  • 9
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • Ali, J. A., and Lohman, T. M. (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
  • 10
    • 0033527761 scopus 로고    scopus 로고
    • An oligomeric form of E. coli UvrD is required for optimal helicase activity
    • Ali, J. A., Maluf, N. K., and Lohman, T. M. (1999) An oligomeric form of E. coli UvrD is required for optimal helicase activity, J. Mol. Biol. 293, 815-833.
    • (1999) J. Mol. Biol. , vol.293 , pp. 815-833
    • Ali, J.A.1    Maluf, N.K.2    Lohman, T.M.3
  • 11
    • 0034719392 scopus 로고    scopus 로고
    • The DExH protein NPH-II is a processive and directional motor for unwinding RNA
    • Jankowsky, E., Gross, C. H., Shuman, S., and Pyle, A. M. (2000) The DExH protein NPH-II is a processive and directional motor for unwinding RNA, Nature 403, 447-451.
    • (2000) Nature , vol.403 , pp. 447-451
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 12
    • 0036447339 scopus 로고    scopus 로고
    • DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies
    • Lucius, A. L., Vindigni, A., Gregorian, R., Ali, J. A., Taylor, A. F., Smith, G. R., and Lohman, T. M. (2002) DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies, J. Mol. Biol. 324, 409-428.
    • (2002) J. Mol. Biol. , vol.324 , pp. 409-428
    • Lucius, A.L.1    Vindigni, A.2    Gregorian, R.3    Ali, J.A.4    Taylor, A.F.5    Smith, G.R.6    Lohman, T.M.7
  • 13
    • 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., and Bujalowski, W. (2004) 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. 343, 83-89.
    • (2004) J. Mol. Biol. , vol.343 , pp. 83-89
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 14
    • 2442513338 scopus 로고    scopus 로고
    • The DNA-unwinding mechanism of the ring helicase of bacteriophage T7
    • Jeong, Y. J., Levin, M. K., and Patel, S. S. (2004) The DNA-unwinding mechanism of the ring helicase of bacteriophage T7, Proc. Natl. Acad. Sci. U.S.A. 101, 7264-7269.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7264-7269
    • Jeong, Y.J.1    Levin, M.K.2    Patel, S.S.3
  • 15
    • 2542468381 scopus 로고    scopus 로고
    • The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity
    • Levin, M. K., Wang, Y. H., and Patel, S. S. (2004) The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity, J. Biol. Chem. 279, 26005-26012.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26005-26012
    • Levin, M.K.1    Wang, Y.H.2    Patel, S.S.3
  • 16
    • 0028138413 scopus 로고
    • Single-turnover kinetics of helicase-catalyzed DNA unwinding monitored continuously by fluorescence energy transfer
    • Bjornson, K. P., Amaratunga, M., Moore, K. J., and Lohman, T. M. (1994) Single-turnover kinetics of helicase-catalyzed DNA unwinding monitored continuously by fluorescence energy transfer, Biochemistry 33, 14306-14316.
    • (1994) Biochemistry , vol.33 , pp. 14306-14316
    • Bjornson, K.P.1    Amaratunga, M.2    Moore, K.J.3    Lohman, T.M.4
  • 17
    • 0028301341 scopus 로고
    • Spectrophotometric assay for enzyme-mediated unwinding of double-stranded DNA
    • Houston, P., and Kodadek, T. (1994) Spectrophotometric assay for enzyme-mediated unwinding of double-stranded DNA, Proc. Natl. Acad. Sci. U.S.A. 91, 5471-5474.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5471-5474
    • Houston, P.1    Kodadek, T.2
  • 18
    • 0035816217 scopus 로고    scopus 로고
    • E. coli Rep oligomers are required to initiate DNA unwinding in vitro
    • Cheng, W., Hsieh, J., Brendza, K. M., and Lohman, T. M. (2001) E. coli Rep oligomers are required to initiate DNA unwinding in vitro, J. Mol. Biol. 310, 327-350.
    • (2001) J. Mol. Biol. , vol.310 , pp. 327-350
    • Cheng, W.1    Hsieh, J.2    Brendza, K.M.3    Lohman, T.M.4
  • 19
    • 2542430217 scopus 로고    scopus 로고
    • Fluorescence stopped-flow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding
    • Lucius, A. L., Wong, C. J., and Lohman, T. M. (2004) Fluorescence stopped-flow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding, J. Mol. Biol. 339, 731-750.
    • (2004) J. Mol. Biol. , vol.339 , pp. 731-750
    • Lucius, A.L.1    Wong, C.J.2    Lohman, T.M.3
  • 20
    • 4544295237 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of the DNA helicase and exonuclease activities of Werner syndrome protein
    • Choudhary, S., Sommers, J. A., and Brosh, R. M., Jr. (2004) Biochemical and kinetic characterization of the DNA helicase and exonuclease activities of Werner syndrome protein, J. Biol. Chem. 279, 34603-34613.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34603-34613
    • Choudhary, S.1    Sommers, J.A.2    Brosh Jr., R.M.3
  • 21
    • 0032555184 scopus 로고    scopus 로고
    • Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli
    • Brune, M., Hunter, J. L., Howell, S. A., Martin, S. R., Hazlett, T. L., Corrie, J. E. T., and Webb, M. R. (1998) Mechanism of inorganic phosphate interaction with phosphate binding protein from Escherichia coli, Biochemistry 37, 10370-10380.
    • (1998) Biochemistry , vol.37 , pp. 10370-10380
    • Brune, M.1    Hunter, J.L.2    Howell, S.A.3    Martin, S.R.4    Hazlett, T.L.5    Corrie, J.E.T.6    Webb, M.R.7
  • 22
    • 9244235535 scopus 로고    scopus 로고
    • Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA
    • Fischer, C. J., Maluf, N. K., and Lohman, T. M. (2004) Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA, J. Mol Biol. 344, 1287-1309.
    • (2004) J. Mol Biol. , vol.344 , pp. 1287-1309
    • Fischer, C.J.1    Maluf, N.K.2    Lohman, T.M.3
  • 23
    • 0034682407 scopus 로고    scopus 로고
    • Translocation step size and mechanism of the RecBC DNA helicase
    • Bianco, P. R., and Kowalczykowski, S. C. (2000) Translocation step size and mechanism of the RecBC DNA helicase, Nature 405, 368-372.
    • (2000) Nature , vol.405 , pp. 368-372
    • Bianco, P.R.1    Kowalczykowski, S.C.2
  • 24
    • 0034054773 scopus 로고    scopus 로고
    • Enzymatic properties of hepatitis C virus NS3-associated helicase
    • Paolini, C., De Francesco, R., and Gallinari, P. (2000) Enzymatic properties of hepatitis C virus NS3-associated helicase, J. Gen. Virol. 81, 1335-1345.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1335-1345
    • Paolini, C.1    De Francesco, R.2    Gallinari, P.3
  • 25
    • 26944479924 scopus 로고    scopus 로고
    • A fluorescent sensor to assay inorganic phosphate
    • (Johnson, K. A., Ed.), Oxford University Press, Oxford, U.K.
    • Webb, M. R. (2003) A fluorescent sensor to assay inorganic phosphate, in Kinetic analysis: A practical approach (Johnson, K. A., Ed.) pp 131-152, Oxford University Press, Oxford, U.K.
    • (2003) Kinetic Analysis: A Practical Approach , pp. 131-152
    • Webb, M.R.1
  • 28
    • 0029670262 scopus 로고    scopus 로고
    • Molecular beacons: Probes that fluoresce upon hybridization
    • Tyagi, S., and Kramer, F. R. (1996) Molecular beacons: Probes that fluoresce upon hybridization, Nat. Biotechnol. 14, 303-308.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 303-308
    • Tyagi, S.1    Kramer, F.R.2
  • 29
    • 0031983834 scopus 로고    scopus 로고
    • Multicolor molecular beacons for allele discrimination
    • Tyagi, S., Bratu, D. P., and Kramer, F. R. (1998) Multicolor molecular beacons for allele discrimination, Nat. Biotechnol. 16, 49-53.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 49-53
    • Tyagi, S.1    Bratu, D.P.2    Kramer, F.R.3
  • 30
    • 0036835759 scopus 로고    scopus 로고
    • Efficiencies of fluorescence resonance energy transfer and contact-mediated quenching in oligonucleotide probes
    • Marras, S. A., Kramer, F. R., and Tyagi, S. (2002) Efficiencies of fluorescence resonance energy transfer and contact-mediated quenching in oligonucleotide probes, Nucleic Acids Res. 30, e122.
    • (2002) Nucleic Acids Res. , vol.30
    • Marras, S.A.1    Kramer, F.R.2    Tyagi, S.3
  • 31
    • 0027261429 scopus 로고
    • Kinetics of ATP hydrolysis during the DNA helicase II-promoted unwinding of duplex DNA
    • Yodh, J. G., and Bryant, F. R. (1993) Kinetics of ATP hydrolysis during the DNA helicase II-promoted unwinding of duplex DNA, Biochemistry 32, 7765-7771.
    • (1993) Biochemistry , vol.32 , pp. 7765-7771
    • Yodh, J.G.1    Bryant, F.R.2
  • 32
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of unidirectional single-stranded DNA translocation by pcrA helicase: Measurement of step size and translocation speed
    • Dillingham, M. S., Wigley, D. B., and Webb, M. R. (2000) Demonstration of unidirectional single-stranded DNA translocation by pcrA helicase: Measurement of step size and translocation speed, Biochemistry 39, 205-212.
    • (2000) Biochemistry , vol.39 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 33
    • 0030885346 scopus 로고    scopus 로고
    • DNA binding and helicase domains of the Escherichia coll recombination protein RecG
    • Mahdi, A., McGlynn, P., Levett, S., and Lloyd, R. (1997) DNA binding and helicase domains of the Escherichia coll recombination protein RecG, Nucleic Acids Res. 25, 3875-3880.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3875-3880
    • Mahdi, A.1    McGlynn, P.2    Levett, S.3    Lloyd, R.4
  • 34
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in pcrA: Direct evidence for an active mechanism
    • Soultanas, P., Dillingham, M., Wiley, P., Webb, M. R., and Wigley, D. B. (2000) Uncoupling DNA translocation and helicase activity in pcrA: Direct evidence for an active mechanism, EMBO J. 19, 3799-3810.
    • (2000) EMBO J. , vol.19 , pp. 3799-3810
    • Soultanas, P.1    Dillingham, M.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 35
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of pcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar, S. S., Soultanas, P., Dillingham, M. S., Subramanya, H. S., and Wigley, D. B. (1999) Crystal structures of complexes of pcrA DNA helicase with a DNA substrate indicate an inchworm mechanism, Cell 97, 75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 38
    • 0024512057 scopus 로고
    • Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay
    • Roman, L. J., and Kowalczykowski, S. C. (1989) Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay, Biochemistry 28, 2863-2873.
    • (1989) Biochemistry , vol.28 , pp. 2863-2873
    • Roman, L.J.1    Kowalczykowski, S.C.2
  • 39
    • 0035951425 scopus 로고    scopus 로고
    • A general model for nucleic acid helicases and their "coupling" within macromolecular machines
    • von Hippel, P. H., and Delagoutte, E. (2001) A general model for nucleic acid helicases and their "coupling" within macromolecular machines, Cell 104, 177-190.
    • (2001) Cell , vol.104 , pp. 177-190
    • Hippel, P.H.1    Delagoutte, E.2


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