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Volumn 38, Issue 13, 2010, Pages 4404-4414

Processive translocation mechanism of the human Bloom's syndrome helicase along single-stranded DNA

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; HELICASE;

EID: 77955247067     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq145     Document Type: Article
Times cited : (37)

References (59)
  • 1
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M.R., Dillingham, M.S. and Wigley, D.B. (2007) Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem., 76, 23-50.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 2
    • 33751426143 scopus 로고    scopus 로고
    • DNA helicases required for homologous recombination and repair of damaged replication forks
    • Wu, L. and Hickson, I.D. (2006) DNA helicases required for homologous recombination and repair of damaged replication forks. Annu. Rev. Genet., 40, 279-306.
    • (2006) Annu. Rev. Genet. , vol.40 , pp. 279-306
    • Wu, L.1    Hickson, I.D.2
  • 3
    • 56449090762 scopus 로고    scopus 로고
    • Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance
    • Bohr, V.A. (2008) Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance. Trends Biochem. Sci., 33, 609-620.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 609-620
    • Bohr, V.A.1
  • 4
    • 34447536139 scopus 로고    scopus 로고
    • BLM ortholog, Sgs1, prevents aberrant crossing-over by suppressing formation of multichromatid joint molecules
    • Oh, S.D., Lao, J.P., Hwang, P.Y., Taylor, A.F., Smith, G.R. and Hunter, N. (2007) BLM ortholog, Sgs1, prevents aberrant crossing-over by suppressing formation of multichromatid joint molecules. Cell, 130, 259-272.
    • (2007) Cell , vol.130 , pp. 259-272
    • Oh, S.D.1    Lao, J.P.2    Hwang, P.Y.3    Taylor, A.F.4    Smith, G.R.5    Hunter, N.6
  • 5
    • 0027331383 scopus 로고
    • Bloom syndrome: a mendelian prototype of somatic mutational disease
    • German, J. (1993) Bloom syndrome: a mendelian prototype of somatic mutational disease. Medicine (Baltimore), 72, 393-406.
    • (1993) Medicine (Baltimore) , vol.72 , pp. 393-406
    • German, J.1
  • 6
    • 0030686496 scopus 로고    scopus 로고
    • The Bloom's syndrome gene product is a 3'-5' DNA helicase
    • Karow, J.K., Chakraverty, R.K. and Hickson, I.D. (1997) The Bloom's syndrome gene product is a 3'-5' DNA helicase. J. Biol. Chem., 272, 30611-30614.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30611-30614
    • Karow, J.K.1    Chakraverty, R.K.2    Hickson, I.D.3
  • 7
    • 36849029846 scopus 로고    scopus 로고
    • Novel pro- and anti-recombination activities of the Bloom's syndrome helicase
    • Bugreev, D.V., Yu, X., Egelman, E.H. and Mazin, A.V. (2007) Novel pro- and anti-recombination activities of the Bloom's syndrome helicase. Genes Dev., 21, 3085-3094.
    • (2007) Genes Dev , vol.21 , pp. 3085-3094
    • Bugreev, D.V.1    Yu, X.2    Egelman, E.H.3    Mazin, A.V.4
  • 8
    • 3142544243 scopus 로고
    • Evidence for increased in vivo mutation and somatic recombination in Bloom's syndrome
    • Langlois, R.G., Bigbee, W.L., Jensen, R.H. and German, J. (1989) Evidence for increased in vivo mutation and somatic recombination in Bloom's syndrome. Proc. Natl Acad. Sci. USA, 86, 670-674.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 670-674
    • Langlois, R.G.1    Bigbee, W.L.2    Jensen, R.H.3    German, J.4
  • 9
    • 0037428069 scopus 로고    scopus 로고
    • Drosophila BLM in double-strand break repair by synthesis-dependent strand annealing
    • Adams, M.D., McVey, M. and Sekelsky, J.J. (2003) Drosophila BLM in double-strand break repair by synthesis-dependent strand annealing. Science, 299, 265-267.
    • (2003) Science , vol.299 , pp. 265-267
    • Adams, M.D.1    McVey, M.2    Sekelsky, J.J.3
  • 11
    • 0347987856 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase suppresses crossing over during homologous recombination
    • Wu, L. and Hickson, I.D. (2003) The Bloom's syndrome helicase suppresses crossing over during homologous recombination. Nature, 426, 870-874.
    • (2003) Nature , vol.426 , pp. 870-874
    • Wu, L.1    Hickson, I.D.2
  • 12
    • 33646843592 scopus 로고    scopus 로고
    • Mobile D-loops are a preferred substrate for the Bloom's syndrome helicase
    • Bachrati, C.Z., Borts, R.H. and Hickson, I.D. (2006) Mobile D-loops are a preferred substrate for the Bloom's syndrome helicase. Nucleic Acids Res., 34, 2269-2279.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2269-2279
    • Bachrati, C.Z.1    Borts, R.H.2    Hickson, I.D.3
  • 14
    • 43049162175 scopus 로고    scopus 로고
    • RecQ helicases: guardian angels of the DNA replication fork
    • Bachrati, C.Z. and Hickson, I.D. (2008) RecQ helicases: guardian angels of the DNA replication fork. Chromosoma, 117, 219-233.
    • (2008) Chromosoma , vol.117 , pp. 219-233
    • Bachrati, C.Z.1    Hickson, I.D.2
  • 15
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle, A.M. (2008) Translocation and unwinding mechanisms of RNA and DNA helicases. Annu. Rev. Biophys., 37, 317-336.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 16
    • 67649637509 scopus 로고    scopus 로고
    • Srs2 disassembles Rad51 filaments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA
    • Antony, E., Tomko, E.J., Xiao, Q., Krejci, L., Lohman, T.M. and Ellenberger, T. (2009) Srs2 disassembles Rad51 filaments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA. Mol. Cell, 35, 105-115.
    • (2009) Mol. Cell , vol.35 , pp. 105-115
    • Antony, E.1    Tomko, E.J.2    Xiao, Q.3    Krejci, L.4    Lohman, T.M.5    Ellenberger, T.6
  • 17
    • 28444470501 scopus 로고    scopus 로고
    • Human DNA polymerase eta promotes DNA synthesis from strand invasion intermediates of homologous recombination
    • McIlwraith, M.J., Vaisman, A., Liu, Y., Fanning, E., Woodgate, R. and West, S.C. (2005) Human DNA polymerase eta promotes DNA synthesis from strand invasion intermediates of homologous recombination. Mol. Cell, 20, 783-792.
    • (2005) Mol. Cell , vol.20 , pp. 783-792
    • McIlwraith, M.J.1    Vaisman, A.2    Liu, Y.3    Fanning, E.4    Woodgate, R.5    West, S.C.6
  • 18
    • 45449110194 scopus 로고    scopus 로고
    • Homologous recombination and maintenance of genome integrity: cancer and aging through the prism of human RecQ helicases
    • Ouyang, K.J., Woo, L.L. and Ellis, N.A. (2008) Homologous recombination and maintenance of genome integrity: cancer and aging through the prism of human RecQ helicases. Mech. Ageing Dev., 129, 425-440.
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 425-440
    • Ouyang, K.J.1    Woo, L.L.2    Ellis, N.A.3
  • 19
    • 33845657428 scopus 로고    scopus 로고
    • UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke
    • Lee, J.Y. and Yang, W. (2006) UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Cell, 127, 1349-1360.
    • (2006) Cell , vol.127 , pp. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 20
    • 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
  • 21
    • 0037474547 scopus 로고    scopus 로고
    • A dimer of Escherichia coli UvrD is the active form of the helicase in vitro
    • Maluf, N.K., Fischer, C.J. and Lohman, T.M. (2003) A dimer of Escherichia coli UvrD is the active form of the helicase in vitro. J. Mol. Biol., 325, 913-935.
    • (2003) J. Mol. Biol. , vol.325 , pp. 913-935
    • Maluf, N.K.1    Fischer, C.J.2    Lohman, T.M.3
  • 22
    • 33947393189 scopus 로고    scopus 로고
    • Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD
    • Curti, E., Smerdon, S.J. and Davis, E.O. (2007) Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD. J. Bacteriol., 189, 1542-1555.
    • (2007) J. Bacteriol. , vol.189 , pp. 1542-1555
    • Curti, E.1    Smerdon, S.J.2    Davis, E.O.3
  • 23
    • 0033617191 scopus 로고    scopus 로고
    • Escherichia coli DNA helicase II is active as a monomer
    • Mechanic, L.E., Hall, M.C. and Matson, S.W. (1999) Escherichia coli DNA helicase II is active as a monomer. J. Biol. Chem., 274, 12488-12498.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12488-12498
    • Mechanic, L.E.1    Hall, M.C.2    Matson, S.W.3
  • 24
    • 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
  • 25
    • 34848840105 scopus 로고    scopus 로고
    • Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro
    • Niedziela-Majka, A., Chesnik, M.A., Tomko, E.J. and Lohman, T.M. (2007) Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro. J. Biol. Chem., 282, 27076-27085.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27076-27085
    • Niedziela-Majka, A.1    Chesnik, M.A.2    Tomko, E.J.3    Lohman, T.M.4
  • 27
    • 75149165723 scopus 로고    scopus 로고
    • Kinetic mechanism of DNA unwinding by the BLM helicase core and molecular basis for its low processivity
    • Yang, Y., Dou, S.X., Xu, Y.N., Bazeille, N., Wang, P.Y., Rigolet, P., Xu, H.Q. and Xi, X.G. (2010) Kinetic mechanism of DNA unwinding by the BLM helicase core and molecular basis for its low processivity. Biochemistry, 49, 656-668.
    • (2010) Biochemistry , vol.49 , pp. 656-668
    • Yang, Y.1    Dou, S.X.2    Xu, Y.N.3    Bazeille, N.4    Wang, P.Y.5    Rigolet, P.6    Xu, H.Q.7    Xi, X.G.8
  • 28
    • 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
  • 29
    • 20444440763 scopus 로고    scopus 로고
    • A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase
    • Levin, M.K., Gurjar, M. and Patel, S.S. (2005) A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase. Nat. Struct. Mol. Biol., 12, 429-435.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 429-435
    • Levin, M.K.1    Gurjar, M.2    Patel, S.S.3
  • 30
    • 34247602963 scopus 로고    scopus 로고
    • A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA
    • Tomko, E.J., Fischer, C.J., Niedziela-Majka, A. and Lohman, T.M. (2007) A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA. Mol. Cell, 26, 335-347.
    • (2007) Mol. Cell , vol.26 , pp. 335-347
    • Tomko, E.J.1    Fischer, C.J.2    Niedziela-Majka, A.3    Lohman, T.M.4
  • 31
    • 2542475076 scopus 로고    scopus 로고
    • Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E. coli RecBCD helicase-catalyzed DNA unwinding
    • Lucius, A.L. and Lohman, T.M. (2004) Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E. coli RecBCD helicase-catalyzed DNA unwinding. J. Mol. Biol., 339, 751-771.
    • (2004) J. Mol. Biol. , vol.339 , pp. 751-771
    • Lucius, A.L.1    Lohman, T.M.2
  • 32
    • 30144436268 scopus 로고    scopus 로고
    • RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP
    • Dumont, S., Cheng, W., Serebrov, V., Beran, R.K., Tinoco, I. Jr, Pyle, A.M. and Bustamante, C. (2006) RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP. Nature, 439, 105-108.
    • (2006) Nature , vol.439 , pp. 105-108
    • Dumont, S.1    Cheng, W.2    Serebrov, V.3    Beran, R.K.4    Tinoco I., Jr.5    Pyle, A.M.6    Bustamante, C.7
  • 33
    • 39649096274 scopus 로고    scopus 로고
    • The ATPase cycle mechanism of the DEAD-box rRNA helicase
    • Henn, A., Cao, W., Hackney, D.D. and De La Cruz, E.M. (2008) The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA. J. Mol. Biol., 377, 193-205.
    • (2008) DbpA. J. Mol. Biol. , vol.377 , pp. 193-205
    • Henn, A.1    Cao, W.2    Hackney, D.D.3    De La Cruz, E.M.4
  • 34
    • 0028098798 scopus 로고
    • Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase
    • Brune, M., Hunter, J.L., Corrie, J.E. and Webb, M.R. (1994) Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry, 33, 8262-8271.
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, J.E.3    Webb, M.R.4
  • 35
    • 0031872841 scopus 로고    scopus 로고
    • ATPase kinetics of the Dictyostelium discoideum myosin II motor domain
    • Kuhlman, P.A. and Bagshaw, C.R. (1998) ATPase kinetics of the Dictyostelium discoideum myosin II motor domain. J. Muscle. Res. Cell Motil., 19, 491-504.
    • (1998) J. Muscle. Res. Cell Motil. , vol.19 , pp. 491-504
    • Kuhlman, P.A.1    Bagshaw, C.R.2
  • 36
    • 0027267667 scopus 로고
    • Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum
    • Ritchie, M.D., Geeves, M.A., Woodward, S.K. and Manstein, D.J. (1993) Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum. Proc. Natl Acad. Sci. USA, 90, 8619-8623.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8619-8623
    • Ritchie, M.D.1    Geeves, M.A.2    Woodward, S.K.3    Manstein, D.J.4
  • 37
    • 0028785981 scopus 로고
    • Kinetic characterization of the catalytic domain of Dictyostelium discoideum myosin
    • Woodward, S.K., Geeves, M.A. and Manstein, D.J. (1995) Kinetic characterization of the catalytic domain of Dictyostelium discoideum myosin. Biochemistry, 34, 16056-16064.
    • (1995) Biochemistry , vol.34 , pp. 16056-16064
    • Woodward, S.K.1    Geeves, M.A.2    Manstein, D.J.3
  • 38
    • 69749114267 scopus 로고    scopus 로고
    • The ATPase cycle of PcrA helicase and its coupling to translocation on DNA
    • Toseland, C.P., Martinez-Senac, M.M., Slatter, A.F. and Webb, M.R. (2009) The ATPase cycle of PcrA helicase and its coupling to translocation on DNA. J. Mol. Biol., 392, 1020-1032.
    • (2009) J. Mol. Biol. , vol.392 , pp. 1020-1032
    • Toseland, C.P.1    Martinez-Senac, M.M.2    Slatter, A.F.3    Webb, M.R.4
  • 40
    • 77954133346 scopus 로고    scopus 로고
    • Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities
    • [31 January 2010, date last accessed]
    • Gyimesi, M., Sarlós, K., Derényi, I. and Kovács, M. (2010) Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities. Nucleic Acids Res., [31 January 2010, date last accessed].
    • (2010) Nucleic Acids Res.
    • Gyimesi, M.1    Sarlós, K.2    Derényi, I.3    Kovács, M.4
  • 41
    • 33744951869 scopus 로고    scopus 로고
    • Escherichia coli RecQ is a rapid, efficient, and monomeric helicase
    • Zhang, X.D., Dou, S.X., Xie, P., Hu, J.S., Wang, P.Y. and Xi, X.G. (2006) Escherichia coli RecQ is a rapid, efficient, and monomeric helicase. J. Biol. Chem., 281, 12655-12663.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12655-12663
    • Zhang, X.D.1    Dou, S.X.2    Xie, P.3    Hu, J.S.4    Wang, P.Y.5    Xi, X.G.6
  • 42
    • 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
  • 43
    • 65249083349 scopus 로고    scopus 로고
    • Kinetic Mechanism for Single stranded DNA binding and Translocation by S. cerevisiae Isw2
    • Fischer, C., Fitzgerald, D. and Yamada, K. (2009) Kinetic Mechanism for Single stranded DNA binding and Translocation by S. cerevisiae Isw2. Biochemistry, 48, 2960-2968.
    • (2009) Biochemistry , vol.48 , pp. 2960-2968
    • Fischer, C.1    Fitzgerald, D.2    Yamada, K.3
  • 44
    • 29344449133 scopus 로고    scopus 로고
    • Mechanism of translocation and kinetics of DNA unwinding by the helicase RecG
    • Martinez-Senac, M.M. and Webb, M.R. (2005) Mechanism of translocation and kinetics of DNA unwinding by the helicase RecG. Biochemistry, 44, 16967-16976.
    • (2005) Biochemistry , vol.44 , pp. 16967-16976
    • Martinez-Senac, M.M.1    Webb, M.R.2
  • 45
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev, S., Hsieh, J., Gauss, G.H., Lohman, T.M. and Waksman, G. (1997) Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell, 90, 635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 46
    • 34447132375 scopus 로고    scopus 로고
    • Structural basis for DNA duplex separation by a superfamily-2 helicase
    • Buttner, K., Nehring, S. and Hopfner, K.P. (2007) Structural basis for DNA duplex separation by a superfamily-2 helicase. Nat. Struct. Mol. Biol., 14, 647-652.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 647-652
    • Buttner, K.1    Nehring, S.2    Hopfner, K.P.3
  • 47
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding
    • Kim, J.L., Morgenstern, K.A., Griffith, J.P., Dwyer, M.D., Thomson, J.A., Murcko, M.A., Lin, C. and Caron, P.R. (1998) Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure, 6, 89-100.
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 49
    • 33747182255 scopus 로고    scopus 로고
    • The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA
    • Bono, F., Ebert, J., Lorentzen, E. and Conti, E. (2006) The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell, 126, 713-725.
    • (2006) Cell , vol.126 , pp. 713-725
    • Bono, F.1    Ebert, J.2    Lorentzen, E.3    Conti, E.4
  • 50
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku, T., Nureki, O., Nakamura, A., Kobayashi, S. and Yokoyama, S. (2006) Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell, 125, 287-300.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 51
    • 76249111702 scopus 로고    scopus 로고
    • Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism
    • Gu, M. and Rice, C.M. (2010) Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism. Proc. Natl Acad. Sci. USA, 107, 521-528.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 521-528
    • Gu, M.1    Rice, C.M.2
  • 52
    • 66149148295 scopus 로고    scopus 로고
    • Mechanistic basis of 5'-3' translocation in SF1B helicases
    • Saikrishnan, K., Powell, B., Cook, N.J., Webb, M.R. and Wigley, D.B. (2009) Mechanistic basis of 50-30 translocation in SF1B helicases. Cell, 137, 849-859.
    • (2009) Cell , vol.137 , pp. 849-859
    • Saikrishnan, K.1    Powell, B.2    Cook, N.J.3    Webb, M.R.4    Wigley, D.B.5
  • 53
    • 77950361633 scopus 로고    scopus 로고
    • Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase
    • Wang, Q., Arnold, J.J., Uchida, A., Raney, K.D. and Cameron, C.E. (2009) Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase. Nucleic Acids Res., 37, 7151-7162.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 7151-7162
    • Wang, Q.1    Arnold, J.J.2    Uchida, A.3    Raney, K.D.4    Cameron, C.E.5
  • 54
    • 70449584733 scopus 로고    scopus 로고
    • The DEAD box helicase YxiN maintains a closed conformation during ATP hydrolysis
    • Aregger, R. and Klostermeier, D. (2009) The DEAD box helicase YxiN maintains a closed conformation during ATP hydrolysis. Biochemistry, 48, 10679-10681.
    • (2009) Biochemistry , vol.48 , pp. 10679-10681
    • Aregger, R.1    Klostermeier, D.2
  • 56
    • 0141865522 scopus 로고    scopus 로고
    • High-resolution structure of the E.coli RecQ helicase catalytic core
    • Bernstein, D.A., Zittel, M.C. and Keck, J.L. (2003) High-resolution structure of the E.coli RecQ helicase catalytic core. EMBO J., 22, 4910-4921.
    • (2003) EMBO J , vol.22 , pp. 4910-4921
    • Bernstein, D.A.1    Zittel, M.C.2    Keck, J.L.3
  • 57
    • 41349092240 scopus 로고    scopus 로고
    • Opening of nucleic-acid double strands by helicases: active versus passive opening
    • Betterton, M.D. and Julicher, F. (2005) Opening of nucleic-acid double strands by helicases: active versus passive opening. Phys. Rev. E Stat. Nonlin. Soft Matter Phys., 71, 011904.
    • (2005) Phys. Rev. E Stat. Nonlin. Soft Matter Phys. , vol.71 , pp. 011904
    • Betterton, M.D.1    Julicher, F.2
  • 58
    • 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. and Wang, M.D. (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
  • 59
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman, T.M. and Bjornson, K.P. (1996) Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem., 65, 169-214.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.