메뉴 건너뛰기




Volumn 430, Issue 6998, 2004, Pages 476-480

Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINS; STOICHIOMETRY; SUBSTRATES; VIRUSES;

EID: 3342896727     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02704     Document Type: Article
Times cited : (120)

References (30)
  • 1
    • 0344012048 scopus 로고    scopus 로고
    • Membrane association of hepatitis C virus nonstructural proteins and identification of the membrane alteration that harbors the viral replication complex
    • Moradpour, D. et al. Membrane association of hepatitis C virus nonstructural proteins and identification of the membrane alteration that harbors the viral replication complex. Antiviral Res. 60, 103-109 (2003).
    • (2003) Antiviral Res. , vol.60 , pp. 103-109
    • Moradpour, D.1
  • 2
    • 0037404536 scopus 로고    scopus 로고
    • Protein-protein interactions between hepatitis C virus nonstructural proteins
    • Dimitrova, M., Imbert, I., Kieny, M. P. & Schuster, C. Protein-protein interactions between hepatitis C virus nonstructural proteins. J. Virol. 77, 5401-5414 (2003).
    • (2003) J. Virol. , vol.77 , pp. 5401-5414
    • Dimitrova, M.1    Imbert, I.2    Kieny, M.P.3    Schuster, C.4
  • 3
    • 0347457077 scopus 로고    scopus 로고
    • Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein
    • Piccininni, S. et al. Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein. J. Biol. Chem. 277, 45670-45679 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 45670-45679
    • Piccininni, S.1
  • 4
    • 0033609061 scopus 로고    scopus 로고
    • Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A
    • Gallinari, P. et al. Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A. Biochemistry 38, 5620-5632 (1999).
    • (1999) Biochemistry , vol.38 , pp. 5620-5632
    • Gallinari, P.1
  • 6
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: Motors, clocks, springs, and things
    • Staley, J. P. & Guthrie, C. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 92, 315-326 (1998).
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 8
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with abound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim, J. L. et al. Hepatitis C virus NS3 RNA helicase domain with abound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 6, 89-100 (1998).
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1
  • 9
    • 0013627747 scopus 로고    scopus 로고
    • Mutational analysis of the hepatitis C virus RNA helicase
    • Kim, D. W., Kim, J., Gwack, Y., Han, J. H. & Choe, J. Mutational analysis of the hepatitis C virus RNA helicase. J. Virol. 71, 9400-9409 (1997).
    • (1997) J. Virol. , vol.71 , pp. 9400-9409
    • Kim, D.W.1    Kim, J.2    Gwack, Y.3    Han, J.H.4    Choe, J.5
  • 10
    • 0032510963 scopus 로고    scopus 로고
    • Crystal structure of RNA helicase from genotype lb hepatitis C virus. A feasible-mechanism of unwinding duplex RNA
    • Cho, H.-S. et al. Crystal structure of RNA helicase from genotype lb hepatitis C virus. A feasible-mechanism of unwinding duplex RNA. J. Biol. Chem. 273, 15045-15052 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15045-15052
    • Cho, H.-S.1
  • 11
    • 0031911760 scopus 로고    scopus 로고
    • Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases
    • Korolev, S., Yao, N., Lohman, T. M., Weber, P. C. & Waksman, G. Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases. Protein Sci. 7, 605-610 (1998).
    • (1998) Protein Sci. , vol.7 , pp. 605-610
    • Korolev, S.1    Yao, N.2    Lohman, T.M.3    Weber, P.C.4    Waksman, G.5
  • 12
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale, R. D. & Milligan, R. A. The way things move: looking under the hood of molecular motor proteins. Science 288, 88-95 (2000).
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 13
    • 0032974384 scopus 로고    scopus 로고
    • The NS3/4A proteinase of the hepatitis C virus: Unravelling structure and function of an unusual enzyme and a prime target for antiviral therapy
    • Bartenschlager, R. The NS3/4A proteinase of the hepatitis C virus: unravelling structure and function of an unusual enzyme and a prime target for antiviral therapy. J. Viral Hepat. 6, 165-181 (1999).
    • (1999) J. Viral Hepat. , vol.6 , pp. 165-181
    • Bartenschlager, R.1
  • 14
    • 0031902992 scopus 로고    scopus 로고
    • Multiple enzymatic activities associated with recombinant NS3 protein of hepatitis C virus
    • Gallinari, P. et al. Multiple enzymatic activities associated with recombinant NS3 protein of hepatitis C virus. J. Virol. 72, 6758-6769 (1998).
    • (1998) J. Virol. , vol.72 , pp. 6758-6769
    • Gallinari, P.1
  • 15
    • 0036500976 scopus 로고    scopus 로고
    • The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding
    • Pang, F. S., Jankowsky, E., Planet, P. J. & Pyle, A. M. The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding. EMBO J. 21, 1168-1176 (2002).
    • (2002) EMBO J. , vol.21 , pp. 1168-1176
    • Pang, F.S.1    Jankowsky, E.2    Planet, P.J.3    Pyle, A.M.4
  • 16
    • 0034054773 scopus 로고    scopus 로고
    • Enzymatic properties of hepatitis C virus NS3-associated helicase
    • Paolini, C., De Francesco, R. & Gallinari, P. Enzymatic properties of hepatitis C virus NS3-associated helicase. J. Gen. Virol. 81, 1335-1345 (2000).
    • (2000) J. Gen. Virol. , vol.81 , pp. 1335-1345
    • Paolini, C.1    De Francesco, R.2    Gallinari, P.3
  • 17
    • 0141865611 scopus 로고    scopus 로고
    • General methods for analysis of sequential "n-step" kinetic mechanisms: Application to single turnover kinetics of helicase-catalyzed DNA unwinding
    • Lucius, A. L., Maluf, N. K., Fischer, C. J. & Lohman, T. M. General methods for analysis of sequential "n-step" kinetic mechanisms: application to single turnover kinetics of helicase-catalyzed DNA unwinding. Biophys. J. 85, 2224-2239 (2003).
    • (2003) Biophys. J. , vol.85 , pp. 2224-2239
    • Lucius, A.L.1    Maluf, N.K.2    Fischer, C.J.3    Lohman, T.M.4
  • 18
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • Ali, J. A. & Lohman, T. M. Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science 275, 377-380 (1997).
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 19
    • 0034682407 scopus 로고    scopus 로고
    • Translocation step size and mechanism of the RecBC DNA helicase
    • Bianco, P. R. & Kowalczykowski, S. C. Translocation step size and mechanism of the RecBC DNA helicase. Nature 405, 368-372 (2000).
    • (2000) Nature , vol.405 , pp. 368-372
    • Bianco, P.R.1    Kowalczykowski, S.C.2
  • 20
    • 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. & Pyle, A. M. The DExH protein NPH-II is a processive and directional motor for unwinding RNA. Nature 403, 447-451 (2000).
    • (2000) Nature , vol.403 , pp. 447-451
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 21
    • 0035905687 scopus 로고    scopus 로고
    • Processive translocation and DNA unwinding by individual RecBCD enzyme molecules
    • Bianco, P. R. et al. Processive translocation and DNA unwinding by individual RecBCD enzyme molecules. Nature 409, 374-378 (2001).
    • (2001) Nature , vol.409 , pp. 374-378
    • Bianco, P.R.1
  • 22
    • 0037057630 scopus 로고    scopus 로고
    • Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase
    • Ha, T. et al. Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase. Nature 419, 638-641 (2002).
    • (2002) Nature , vol.419 , pp. 638-641
    • Ha, T.1
  • 23
    • 0141540814 scopus 로고    scopus 로고
    • A molecular throttle: The recombination hotspot chi controls DNA translocation by the RecBCD helicase
    • Spies, M. et al. A molecular throttle: the recombination hotspot chi controls DNA translocation by the RecBCD helicase. Cell 114, 647-654 (2003).
    • (2003) Cell , vol.114 , pp. 647-654
    • Spies, M.1
  • 25
    • 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. et al. 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).
    • (2002) J. Mol. Biol. , vol.324 , pp. 409-428
    • Lucius, A.L.1
  • 26
    • 0033527562 scopus 로고    scopus 로고
    • The helicase from hepatitis C virus is active as an oligomer
    • Levin, M. K. & Patel, S. S. The helicase from hepatitis C virus is active as an oligomer. J. Biol. Chem. 274, 31839-31846 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31839-31846
    • Levin, M.K.1    Patel, S.S.2
  • 27
    • 0037072271 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 ATPase/helicase: An ATP switch regulates the cooperativity among the different substrate binding sites
    • Locatelli, G. A., Spadari, S. & Maga, G. Hepatitis C virus NS3 ATPase/helicase: an ATP switch regulates the cooperativity among the different substrate binding sites. Biochemistry 41, 10332-10342 (2002).
    • (2002) Biochemistry , vol.41 , pp. 10332-10342
    • Locatelli, G.A.1    Spadari, S.2    Maga, G.3
  • 28
    • 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. & Patel, S. S. The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity. J. Biol. Chem. 279, 26005-26012 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 26005-26012
    • Levin, M.K.1    Wang, Y.H.2    Patel, S.S.3
  • 30
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem. 237, 260-273 (1996).
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.