메뉴 건너뛰기




Volumn 19, Issue 6, 2009, Pages 752-758

Structural insights into replication initiation and elongation processes by the FMDV RNA-dependent RNA polymerase

Author keywords

[No Author keywords available]

Indexed keywords

RNA DIRECTED RNA POLYMERASE; TYROSINE; URIDINE PHOSPHATE;

EID: 70549097349     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2009.10.016     Document Type: Review
Times cited : (55)

References (30)
  • 1
    • 40649100793 scopus 로고    scopus 로고
    • Structure-function relationships among RNA-dependent RNA polymerases
    • Ng K.K., Arnold J.J., and Cameron C.E. Structure-function relationships among RNA-dependent RNA polymerases. Curr Top Microbiol Immunol 320 (2008) 137-156
    • (2008) Curr Top Microbiol Immunol , vol.320 , pp. 137-156
    • Ng, K.K.1    Arnold, J.J.2    Cameron, C.E.3
  • 3
    • 33644519317 scopus 로고    scopus 로고
    • The structure of a protein primer-polymerase complex in the initiation of genome replication
    • The structure of the FMDV RdRP in complex with the protein primer VPg providing insights into the replication initiation process in picornavirus. The product of the uridylylation reaction VPg-UMP was observed in the crystal structure.
    • Ferrer-Orta C., Arias A., Agudo R., Perez-Luque R., Escarmis C., Domingo E., and Verdaguer N. The structure of a protein primer-polymerase complex in the initiation of genome replication. EMBO J 25 (2006) 880-888. The structure of the FMDV RdRP in complex with the protein primer VPg providing insights into the replication initiation process in picornavirus. The product of the uridylylation reaction VPg-UMP was observed in the crystal structure.
    • (2006) EMBO J , vol.25 , pp. 880-888
    • Ferrer-Orta, C.1    Arias, A.2    Agudo, R.3    Perez-Luque, R.4    Escarmis, C.5    Domingo, E.6    Verdaguer, N.7
  • 4
    • 8744222695 scopus 로고    scopus 로고
    • Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA
    • Ferrer-Orta C., Arias A., Perez-Luque R., Escarmis C., Domingo E., and Verdaguer N. Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA. J Biol Chem 279 (2004) 47212-47221
    • (2004) J Biol Chem , vol.279 , pp. 47212-47221
    • Ferrer-Orta, C.1    Arias, A.2    Perez-Luque, R.3    Escarmis, C.4    Domingo, E.5    Verdaguer, N.6
  • 5
    • 34547178347 scopus 로고    scopus 로고
    • Sequential structures provide insights into the fidelity of RNA replication
    • The structure of four FMDV RdRP catalytic complexes showing different events of the RNA elongation process.
    • Ferrer-Orta C., Arias A., Perez-Luque R., Escarmis C., Domingo E., and Verdaguer N. Sequential structures provide insights into the fidelity of RNA replication. Proc Natl Acad Sci U S A 104 (2007) 9463-9468. The structure of four FMDV RdRP catalytic complexes showing different events of the RNA elongation process.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9463-9468
    • Ferrer-Orta, C.1    Arias, A.2    Perez-Luque, R.3    Escarmis, C.4    Domingo, E.5    Verdaguer, N.6
  • 6
    • 0242415195 scopus 로고    scopus 로고
    • A "slide-back" mechanism for the initiation of protein-primed RNA synthesis by the RNA polymerase of poliovirus
    • Paul A.V., Yin J., Mugavero J., Rieder E., Liu Y., and Wimmer E. A "slide-back" mechanism for the initiation of protein-primed RNA synthesis by the RNA polymerase of poliovirus. J Biol Chem 278 (2003) 43951-43960
    • (2003) J Biol Chem , vol.278 , pp. 43951-43960
    • Paul, A.V.1    Yin, J.2    Mugavero, J.3    Rieder, E.4    Liu, Y.5    Wimmer, E.6
  • 7
    • 0032554886 scopus 로고    scopus 로고
    • Protein-primed RNA synthesis by purified poliovirus RNA polymerase
    • Paul A.V., van Boom J.H., Filippov D., and Wimmer E. Protein-primed RNA synthesis by purified poliovirus RNA polymerase. Nature 393 (1998) 280-284
    • (1998) Nature , vol.393 , pp. 280-284
    • Paul, A.V.1    van Boom, J.H.2    Filippov, D.3    Wimmer, E.4
  • 8
    • 57649219466 scopus 로고    scopus 로고
    • Picornavirus genome replication: roles of precursor proteins and rate-limiting steps in oriI-dependent VPg uridylylation
    • Pathak H.B., Oh H.S., Goodfellow I.G., Arnold J.J., and Cameron C.E. Picornavirus genome replication: roles of precursor proteins and rate-limiting steps in oriI-dependent VPg uridylylation. J Biol Chem 283 (2008) 30677-30688
    • (2008) J Biol Chem , vol.283 , pp. 30677-30688
    • Pathak, H.B.1    Oh, H.S.2    Goodfellow, I.G.3    Arnold, J.J.4    Cameron, C.E.5
  • 10
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz T.A., and Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proc Natl Acad Sci U S A 90 (1993) 6498-6502
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 11
    • 50149100514 scopus 로고    scopus 로고
    • Molecular characterization of a dual inhibitory and mutagenic activity of 5-fluorouridine triphosphate on viral RNA synthesis. Implications for lethal mutagenesis
    • Agudo R., Arias A., Pariente N., Perales C., Escarmis C., Jorge A., Marina A., and Domingo E. Molecular characterization of a dual inhibitory and mutagenic activity of 5-fluorouridine triphosphate on viral RNA synthesis. Implications for lethal mutagenesis. J Mol Biol 382 (2008) 652-666
    • (2008) J Mol Biol , vol.382 , pp. 652-666
    • Agudo, R.1    Arias, A.2    Pariente, N.3    Perales, C.4    Escarmis, C.5    Jorge, A.6    Marina, A.7    Domingo, E.8
  • 12
    • 34447517120 scopus 로고    scopus 로고
    • Structure-function relationships of the viral RNA-dependent RNA polymerase: fidelity, replication speed, and initiation mechanism determined by a residue in the ribose-binding pocket
    • Korneeva V.S., and Cameron C.E. Structure-function relationships of the viral RNA-dependent RNA polymerase: fidelity, replication speed, and initiation mechanism determined by a residue in the ribose-binding pocket. J Biol Chem 282 (2007) 16135-16145
    • (2007) J Biol Chem , vol.282 , pp. 16135-16145
    • Korneeva, V.S.1    Cameron, C.E.2
  • 13
    • 33947386595 scopus 로고    scopus 로고
    • Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase
    • Marcotte L.L., Wass A.B., Gohara D.W., Pathak H.B., Arnold J.J., Filman D.J., Cameron C.E., and Hogle J.M. Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. J Virol 81 (2007) 3583-3596
    • (2007) J Virol , vol.81 , pp. 3583-3596
    • Marcotte, L.L.1    Wass, A.B.2    Gohara, D.W.3    Pathak, H.B.4    Arnold, J.J.5    Filman, D.J.6    Cameron, C.E.7    Hogle, J.M.8
  • 14
    • 52649173300 scopus 로고    scopus 로고
    • The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases
    • The structure of the coxsackievirus polymerase providing evidences of a second binding site for the primer protein VPg.
    • Gruez A., Selisko B., Roberts M., Bricogne G., Bussetta C., Jabafi I., Coutard B., De Palma A.M., Neyts J., and Canard B. The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases. J Virol 82 (2008) 9577-9590. The structure of the coxsackievirus polymerase providing evidences of a second binding site for the primer protein VPg.
    • (2008) J Virol , vol.82 , pp. 9577-9590
    • Gruez, A.1    Selisko, B.2    Roberts, M.3    Bricogne, G.4    Bussetta, C.5    Jabafi, I.6    Coutard, B.7    De Palma, A.M.8    Neyts, J.9    Canard, B.10
  • 15
    • 38149020712 scopus 로고    scopus 로고
    • Picornavirus genome replication. Identification of the surface of the poliovirus (PV) 3C dimer that interacts with PV 3Dpol during VPg uridylylation and construction of a structural model for the PV 3C2-3Dpol complex
    • Shen M., Reitman Z.J., Zhao Y., Moustafa I., Wang Q., Arnold J.J., Pathak H.B., and Cameron C.E. Picornavirus genome replication. Identification of the surface of the poliovirus (PV) 3C dimer that interacts with PV 3Dpol during VPg uridylylation and construction of a structural model for the PV 3C2-3Dpol complex. J Biol Chem 283 (2008) 875-888
    • (2008) J Biol Chem , vol.283 , pp. 875-888
    • Shen, M.1    Reitman, Z.J.2    Zhao, Y.3    Moustafa, I.4    Wang, Q.5    Arnold, J.J.6    Pathak, H.B.7    Cameron, C.E.8
  • 17
    • 0025743809 scopus 로고
    • The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses
    • Koonin E.V. The phylogeny of RNA-dependent RNA polymerases of positive-strand RNA viruses. J Gen Virol 72 (1991) 2197-2206
    • (1991) J Gen Virol , vol.72 , pp. 2197-2206
    • Koonin, E.V.1
  • 18
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen J.L., Long A.M., and Schultz S.C. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 5 (1997) 1109-1122
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 19
    • 2442461170 scopus 로고    scopus 로고
    • Poliovirus RNA-dependent RNA polymerase (3Dpol): kinetic, thermodynamic, and structural analysis of ribonucleotide selection
    • Gohara D.W., Arnold J.J., and Cameron C.E. Poliovirus RNA-dependent RNA polymerase (3Dpol): kinetic, thermodynamic, and structural analysis of ribonucleotide selection. Biochemistry 43 (2004) 5149-5158
    • (2004) Biochemistry , vol.43 , pp. 5149-5158
    • Gohara, D.W.1    Arnold, J.J.2    Cameron, C.E.3
  • 21
    • 0037388383 scopus 로고    scopus 로고
    • Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations
    • Johnson S.J., Taylor J.S., and Beese L.S. Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proc Natl Acad Sci U S A 100 (2003) 3895-3900
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3895-3900
    • Johnson, S.J.1    Taylor, J.S.2    Beese, L.S.3
  • 22
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • Doublie S., Tabor S., Long A.M., Richardson C.C., and Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution. Nature 391 (1998) 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
  • 23
    • 0037112082 scopus 로고    scopus 로고
    • Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase
    • Yin Y.W., and Steitz T.A. Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase. Science 298 (2002) 1387-1395
    • (2002) Science , vol.298 , pp. 1387-1395
    • Yin, Y.W.1    Steitz, T.A.2
  • 24
    • 31144445870 scopus 로고    scopus 로고
    • Mechanisms of action of ribavirin against distinct viruses
    • Graci J.D., and Cameron C.E. Mechanisms of action of ribavirin against distinct viruses. Rev Med Virol 16 (2006) 37-48
    • (2006) Rev Med Virol , vol.16 , pp. 37-48
    • Graci, J.D.1    Cameron, C.E.2
  • 25
    • 11844282166 scopus 로고    scopus 로고
    • Metabolism and antiviral activity of ribavirin
    • Parker W.B. Metabolism and antiviral activity of ribavirin. Virus Res 107 (2005) 165-171
    • (2005) Virus Res , vol.107 , pp. 165-171
    • Parker, W.B.1
  • 26
    • 11844256382 scopus 로고    scopus 로고
    • Virus entry into error catastrophe as a new antiviral strategy
    • Domingo E.E. Virus entry into error catastrophe as a new antiviral strategy. Virus Res 107 (2005) 115-228
    • (2005) Virus Res , vol.107 , pp. 115-228
    • Domingo, E.E.1
  • 27
    • 33846813925 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus mutant with decreased sensitivity to ribavirin: implications for error catastrophe
    • Sierra M., Airaksinen A., Gonzalez-Lopez C., Agudo R., Arias A., and Domingo E. Foot-and-mouth disease virus mutant with decreased sensitivity to ribavirin: implications for error catastrophe. J Virol 81 (2007) 2012-2024
    • (2007) J Virol , vol.81 , pp. 2012-2024
    • Sierra, M.1    Airaksinen, A.2    Gonzalez-Lopez, C.3    Agudo, R.4    Arias, A.5    Domingo, E.6
  • 28
    • 57349131683 scopus 로고    scopus 로고
    • Determinants of RNA-dependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin
    • The first kinetic analysis of FMDV RdRP providing the first direct comparison of the kinetic mechanism and fidelity of two picornaviral polymerases those of PV and FMDV.
    • Arias A., Arnold J.J., Sierra M., Smidansky E.D., Domingo E., and Cameron C.E. Determinants of RNA-dependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin. J Virol 82 (2008) 12346-12355. The first kinetic analysis of FMDV RdRP providing the first direct comparison of the kinetic mechanism and fidelity of two picornaviral polymerases those of PV and FMDV.
    • (2008) J Virol , vol.82 , pp. 12346-12355
    • Arias, A.1    Arnold, J.J.2    Sierra, M.3    Smidansky, E.D.4    Domingo, E.5    Cameron, C.E.6
  • 29
    • 0033621167 scopus 로고    scopus 로고
    • Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric hindrance with beta-branched amino acids
    • Sarafianos S.G., Das K., Clark Jr. A.D., Ding J., Boyer P.L., Hughes S.H., and Arnold E. Lamivudine (3TC) resistance in HIV-1 reverse transcriptase involves steric hindrance with beta-branched amino acids. Proc Natl Acad Sci U S A 96 (1999) 10027-10032
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 10027-10032
    • Sarafianos, S.G.1    Das, K.2    Clark Jr., A.D.3    Ding, J.4    Boyer, P.L.5    Hughes, S.H.6    Arnold, E.7
  • 30
    • 0035041976 scopus 로고    scopus 로고
    • Molecular modeling and biochemical characterization reveal the mechanism of hepatitis B virus polymerase resistance to lamivudine (3TC) and emtricitabine (FTC)
    • Das K., Xiong X., Yang H., Westland C.E., Gibbs C.S., Sarafianos S.G., and Arnold E. Molecular modeling and biochemical characterization reveal the mechanism of hepatitis B virus polymerase resistance to lamivudine (3TC) and emtricitabine (FTC). J Virol 75 (2001) 4771-4779
    • (2001) J Virol , vol.75 , pp. 4771-4779
    • Das, K.1    Xiong, X.2    Yang, H.3    Westland, C.E.4    Gibbs, C.S.5    Sarafianos, S.G.6    Arnold, E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.