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Volumn 15, Issue 5, 2008, Pages 500-506

The structural basis for cap binding by influenza virus polymerase subunit PB2

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; CAP BINDING PROTEIN; CAPPED RNA; GUANOSINE TRIPHOSPHATE; MESSENGER RNA PRECURSOR; NUCLEOTIDE; PROTEIN PB2; RNA POLYMERASE;

EID: 43249128376     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1421     Document Type: Article
Times cited : (431)

References (44)
  • 1
    • 33646033777 scopus 로고    scopus 로고
    • Global patterns of influenza a virus in wild birds
    • Olsen, B. et al. Global patterns of influenza a virus in wild birds. Science 312, 384-388 (2006).
    • (2006) Science , vol.312 , pp. 384-388
    • Olsen, B.1
  • 2
    • 22944457912 scopus 로고    scopus 로고
    • Influenza: Lessons from past pandemics, warnings from current incidents
    • Horimoto, T. & Kawaoka, Y. Influenza: lessons from past pandemics, warnings from current incidents. Nat. Rev. Microbiol. 3, 591-600 (2005).
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 591-600
    • Horimoto, T.1    Kawaoka, Y.2
  • 3
    • 33748455689 scopus 로고    scopus 로고
    • Structure and function of the influenza virus RNP
    • ed. Kawaoka, Y, Horizon Scientific, Norfolk
    • Elton, D., Digard, P., Tiley, L. & Ortín, J. Structure and function of the influenza virus RNP. in Current Topics in Influenza Virology (ed. Kawaoka, Y.) (Horizon Scientific, Norfolk, 2005).
    • (2005) Current Topics in Influenza Virology
    • Elton, D.1    Digard, P.2    Tiley, L.3    Ortín, J.4
  • 4
    • 0019394947 scopus 로고
    • A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription
    • Plotch, S.J., Bouloy, M., Ulmanen, I. & Krug, R.M. A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription. Cell 23, 847-858 (1981).
    • (1981) Cell , vol.23 , pp. 847-858
    • Plotch, S.J.1    Bouloy, M.2    Ulmanen, I.3    Krug, R.M.4
  • 5
    • 0035901509 scopus 로고    scopus 로고
    • The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits
    • Li, M.L., Rao, P. & Krug, R.M. The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits. EMBO J. 20, 2078-2086 (2001).
    • (2001) EMBO J , vol.20 , pp. 2078-2086
    • Li, M.L.1    Rao, P.2    Krug, R.M.3
  • 6
    • 0033015827 scopus 로고    scopus 로고
    • Direct evidence that the poly(A) tail of influenza A virus mRNA is synthesized by reiterative copying of a U track in the virion RNA template
    • Poon, L.L., Pritlove, D.C., Fodor, E. & Brownlee, G.G. Direct evidence that the poly(A) tail of influenza A virus mRNA is synthesized by reiterative copying of a U track in the virion RNA template. J. Virol. 73, 3473-3476 (1999).
    • (1999) J. Virol , vol.73 , pp. 3473-3476
    • Poon, L.L.1    Pritlove, D.C.2    Fodor, E.3    Brownlee, G.G.4
  • 7
    • 0029048936 scopus 로고
    • Differential activation of the influenza virus polymerase via template RNA binding
    • Cianci, C., Tiley, L. & Krystal, M. Differential activation of the influenza virus polymerase via template RNA binding. J. Virol. 69, 3995-3999 (1995).
    • (1995) J. Virol , vol.69 , pp. 3995-3999
    • Cianci, C.1    Tiley, L.2    Krystal, M.3
  • 8
    • 0032731217 scopus 로고    scopus 로고
    • Two separate sequences of PB2 subunit constitute the RNA cap-binding site of influenza virus RNA polymerase
    • Honda, A., Mizumoto, K. & Ishihama, A. Two separate sequences of PB2 subunit constitute the RNA cap-binding site of influenza virus RNA polymerase. Genes Cells 4, 475-485 (1999).
    • (1999) Genes Cells , vol.4 , pp. 475-485
    • Honda, A.1    Mizumoto, K.2    Ishihama, A.3
  • 9
    • 0037827745 scopus 로고    scopus 로고
    • Two aromatic residues in the PB2 subunit of influenza A RNA polymerase are crucial for cap binding
    • Fechter, P. et al. Two aromatic residues in the PB2 subunit of influenza A RNA polymerase are crucial for cap binding. J. Biol. Chem. 278, 20381-20388 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 20381-20388
    • Fechter, P.1
  • 10
    • 18144398494 scopus 로고    scopus 로고
    • Recognition of mRNA cap structures by viral and cellular proteins
    • Fechter, P. & Brownlee, G.G. Recognition of mRNA cap structures by viral and cellular proteins. J. Gen. Virol. 86, 1239-1249 (2005).
    • (2005) J. Gen. Virol , vol.86 , pp. 1239-1249
    • Fechter, P.1    Brownlee, G.G.2
  • 11
    • 0347719363 scopus 로고    scopus 로고
    • 3D structure of the influenza virus polymerase complex: Localization of subunit domains
    • Area, E. et al. 3D structure of the influenza virus polymerase complex: localization of subunit domains. Proc. Natl. Acad. Sci. USA 101, 308-313 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 308-313
    • Area, E.1
  • 12
    • 34547137695 scopus 로고    scopus 로고
    • Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer
    • Torreira, E. et al. Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer. Nucleic Acids Res. 35, 3774-3783 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. 3774-3783
    • Torreira, E.1
  • 13
    • 33847624936 scopus 로고    scopus 로고
    • Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit
    • Tarendeau, F. et al. Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat. Struct. Mol. Biol. 14, 229-233 (2007).
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 229-233
    • Tarendeau, F.1
  • 14
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 15
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano, J., Gingras, A.C., Sonenberg, N. & Burley, S.K. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 89, 951-961 (1997).
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 16
    • 0037107401 scopus 로고    scopus 로고
    • Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex
    • Mazza, C., Segref, A., Mattaj, I.W. & Cusack, S. Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex. EMBO J. 21, 5548-5557 (2002).
    • (2002) EMBO J , vol.21 , pp. 5548-5557
    • Mazza, C.1    Segref, A.2    Mattaj, I.W.3    Cusack, S.4
  • 17
    • 0031993338 scopus 로고    scopus 로고
    • Structural basis for sequence-nonspecific recognition of 5′-capped mRNA by a cap-modifying enzyme
    • Hodel, A.E., Gershon, P.D. & Quiocho, F.A. Structural basis for sequence-nonspecific recognition of 5′-capped mRNA by a cap-modifying enzyme. Mol. Cell 1, 443-447 (1998).
    • (1998) Mol. Cell , vol.1 , pp. 443-447
    • Hodel, A.E.1    Gershon, P.D.2    Quiocho, F.A.3
  • 18
    • 0036307897 scopus 로고    scopus 로고
    • Biophysical studies of eIF4E cap-binding protein: Recognition of mRNA 5′ cap structure and synthetic fragments of eIF4G and 4E-BP1 proteins
    • Niedzwiecka, A. et al. Biophysical studies of eIF4E cap-binding protein: recognition of mRNA 5′ cap structure and synthetic fragments of eIF4G and 4E-BP1 proteins. J. Mol. Biol. 319, 615-635 (2002).
    • (2002) J. Mol. Biol , vol.319 , pp. 615-635
    • Niedzwiecka, A.1
  • 19
    • 0035033091 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle
    • 313-317
    • Martin-Benito, J. et al. Three-dimensional reconstruction of a recombinant influenza virus ribonucleoprotein particle. EMBO Rep. 2, 313-317 (2001).
    • (2001) EMBO Rep , vol.2
    • Martin-Benito, J.1
  • 20
    • 17644443084 scopus 로고    scopus 로고
    • Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification
    • Ortega, J. et al. Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification. J. Virol. 74, 156-163 (2000).
    • (2000) J. Virol , vol.74 , pp. 156-163
    • Ortega, J.1
  • 21
    • 24044465540 scopus 로고    scopus 로고
    • Specificity of recognition of mRNA 5′ cap by human nuclear capbinding complex
    • Worch, R. et al. Specificity of recognition of mRNA 5′ cap by human nuclear capbinding complex. RNA 11, 1355-1363 (2005).
    • (2005) RNA , vol.11 , pp. 1355-1363
    • Worch, R.1
  • 22
    • 0038182864 scopus 로고    scopus 로고
    • Quantitative analysis of influenza virus RNP interaction with RNA cap structures and comparison to human cap binding protein eIF4E
    • Hooker, L. et al. Quantitative analysis of influenza virus RNP interaction with RNA cap structures and comparison to human cap binding protein eIF4E. Biochemistry 42, 6234-6240 (2003).
    • (2003) Biochemistry , vol.42 , pp. 6234-6240
    • Hooker, L.1
  • 23
    • 0003396513 scopus 로고
    • Both the 7-methyl and the 2′-O-methyl groups in the cap of mRNA strongly influence its ability to act as primer for influenza virus RNA transcription
    • Bouloy, M., Plotch, S.J. & Krug, R.M. Both the 7-methyl and the 2′-O-methyl groups in the cap of mRNA strongly influence its ability to act as primer for influenza virus RNA transcription. Proc. Natl. Acad. Sci. USA 77, 3952-3956 (1980).
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3952-3956
    • Bouloy, M.1    Plotch, S.J.2    Krug, R.M.3
  • 24
    • 0036720769 scopus 로고    scopus 로고
    • A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs
    • Fodor, E. et al. A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs. J. Virol. 76, 8989-9001 (2002).
    • (2002) J. Virol , vol.76 , pp. 8989-9001
    • Fodor, E.1
  • 25
    • 33746815630 scopus 로고    scopus 로고
    • Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding
    • Hara, K., Schmidt, F.I., Crow, M. & Brownlee, G.G. Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding. J. Virol. 80, 7789-7798 (2006).
    • (2006) J. Virol , vol.80 , pp. 7789-7798
    • Hara, K.1    Schmidt, F.I.2    Crow, M.3    Brownlee, G.G.4
  • 26
    • 0021243308 scopus 로고
    • Capped mRNAs may stimulate the influenza virion polymerase by allosteric modulation
    • Penn, C.R. & Mahy, B.W. Capped mRNAs may stimulate the influenza virion polymerase by allosteric modulation. Virus Res. 1, 1-13 (1984).
    • (1984) Virus Res , vol.1 , pp. 1-13
    • Penn, C.R.1    Mahy, B.W.2
  • 27
    • 0022021473 scopus 로고
    • Activation of influenza virus-associated RNA polymerase by cap-1 structure (m7GpppNm)
    • Kawakami, K., Mizumoto, K., Ishihama, A., Shinozaki-Yamaguchi, K. & Miura, K. Activation of influenza virus-associated RNA polymerase by cap-1 structure (m7GpppNm). J. Biochem. 97, 655-661 (1985).
    • (1985) J. Biochem , vol.97 , pp. 655-661
    • Kawakami, K.1    Mizumoto, K.2    Ishihama, A.3    Shinozaki-Yamaguchi, K.4    Miura, K.5
  • 28
    • 0030785703 scopus 로고    scopus 로고
    • Differential effect of modified capped RNA substrates on influenza virus transcription
    • Cianci, C., Colonno, R.J. & Krystal, M. Differential effect of modified capped RNA substrates on influenza virus transcription. Virus Res. 50, 65-75 (1997).
    • (1997) Virus Res , vol.50 , pp. 65-75
    • Cianci, C.1    Colonno, R.J.2    Krystal, M.3
  • 29
    • 0032189818 scopus 로고    scopus 로고
    • RNA-dependent activation of primer RNA production by influenza virus polymerase: Different regions of the same protein subunit constitute the two required RNA-binding sites
    • Li, M.L., Ramirez, B.C. & Krug, R.M. RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding sites. EMBO J. 17, 5844-5852 (1998).
    • (1998) EMBO J , vol.17 , pp. 5844-5852
    • Li, M.L.1    Ramirez, B.C.2    Krug, R.M.3
  • 30
    • 0020665686 scopus 로고
    • Influenza virus temperature-sensitive cap (m7GpppNm)-dependent endonuclease
    • Ulmanen, I., Broni, B. & Krug, R.M. Influenza virus temperature-sensitive cap (m7GpppNm)-dependent endonuclease. J. Virol. 45, 27-35 (1983).
    • (1983) J. Virol , vol.45 , pp. 27-35
    • Ulmanen, I.1    Broni, B.2    Krug, R.M.3
  • 31
    • 0025083454 scopus 로고
    • Characterization of a temperature-sensitive mutant in the RNA polymerase PB2 subunit gene of influenza A/WSN/33 virus
    • Yamanaka, K. et al. Characterization of a temperature-sensitive mutant in the RNA polymerase PB2 subunit gene of influenza A/WSN/33 virus. Arch. Virol. 114, 65-73 (1990).
    • (1990) Arch. Virol , vol.114 , pp. 65-73
    • Yamanaka, K.1
  • 32
    • 0030886052 scopus 로고    scopus 로고
    • Inhibition of influenza viral polymerases by minimal viral RNA decoys
    • Luo, G., Danetz, S. & Krystal, M. Inhibition of influenza viral polymerases by minimal viral RNA decoys. J. Gen. Virol. 78, 2329-2333 (1997).
    • (1997) J. Gen. Virol , vol.78 , pp. 2329-2333
    • Luo, G.1    Danetz, S.2    Krystal, M.3
  • 33
    • 33751517736 scopus 로고    scopus 로고
    • Antiviral agents active against influenza A viruses
    • De Clercq, E. Antiviral agents active against influenza A viruses. Nat. Rev. Drug Discov. 5, 1015-1025 (2006).
    • (2006) Nat. Rev. Drug Discov , vol.5 , pp. 1015-1025
    • De Clercq, E.1
  • 34
    • 0023084783 scopus 로고
    • Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
    • DuBridge, R.B. et al. Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system. Mol. Cell. Biol. 7, 379-387 (1987).
    • (1987) Mol. Cell. Biol , vol.7 , pp. 379-387
    • DuBridge, R.B.1
  • 35
    • 0019198905 scopus 로고
    • Genetic variability of Hong Kong (H3N2) influenza viruses: Spontaneous mutations and their location in the viral genome
    • Ortin, J., Najera, R., Lopez, C., Davila, M. & Domingo, E. Genetic variability of Hong Kong (H3N2) influenza viruses: spontaneous mutations and their location in the viral genome. Gene 11, 319-331 (1980).
    • (1980) Gene , vol.11 , pp. 319-331
    • Ortin, J.1    Najera, R.2    Lopez, C.3    Davila, M.4    Domingo, E.5
  • 36
    • 1842536901 scopus 로고    scopus 로고
    • Defective RNA replication and late gene expression in temperature-sensitive influenza viruses expressing deleted forms of the NS1 protein
    • Falcon, A.M. et al. Defective RNA replication and late gene expression in temperature-sensitive influenza viruses expressing deleted forms of the NS1 protein. J. Virol. 78, 3880-3888 (2004).
    • (2004) J. Virol , vol.78 , pp. 3880-3888
    • Falcon, A.M.1
  • 37
    • 13044287344 scopus 로고    scopus 로고
    • Generation of influenza A viruses entirely from cloned cDNAs
    • Neumann, G. et al. Generation of influenza A viruses entirely from cloned cDNAs. Proc. Natl. Acad. Sci. USA 96, 9345-9350 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9345-9350
    • Neumann, G.1
  • 38
    • 0024346154 scopus 로고
    • Molecular cloning and sequencing of influenza virus A/Victoria/3/75 polymerase genes: Sequence evolution and prediction of possible functional domains
    • de la Luna, S., Martinez, C. & Ortin, J. Molecular cloning and sequencing of influenza virus A/Victoria/3/75 polymerase genes: sequence evolution and prediction of possible functional domains. Virus Res. 13, 143-155 (1989).
    • (1989) Virus Res , vol.13 , pp. 143-155
    • de la Luna, S.1    Martinez, C.2    Ortin, J.3
  • 39
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L. & Clardy, J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229, 105-124 (1993).
    • (1993) J. Mol. Biol , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 40
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R. & Lamzin, V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458-463 (1999).
    • (1999) Nat. Struct. Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 41
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D Biol. Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1
  • 42
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Ca geometry: F, c and Cb deviation
    • Lovell, S.C. et al. Structure validation by Ca geometry: f, c and Cb deviation. Proteins 50, 437-450 (2003).
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1
  • 43
    • 0028110061 scopus 로고
    • Monoclonal antibodies against influenza virus PB2 and NP polypeptides interfere with the initiation step of viral mRNA synthesis in vitro
    • Barcena, J. et al. Monoclonal antibodies against influenza virus PB2 and NP polypeptides interfere with the initiation step of viral mRNA synthesis in vitro. J. Virol. 68, 6900-6909 (1994).
    • (1994) J. Virol , vol.68 , pp. 6900-6909
    • Barcena, J.1
  • 44
    • 0030029921 scopus 로고    scopus 로고
    • Mutational analysis identifies functional domains in the influenza A virus PB2 polymerase subunit
    • Perales, B., de la Luna, S., Palacios, I. & Ortin, J. Mutational analysis identifies functional domains in the influenza A virus PB2 polymerase subunit. J. Virol. 70, 1678-1686 (1996).
    • (1996) J. Virol , vol.70 , pp. 1678-1686
    • Perales, B.1    de la Luna, S.2    Palacios, I.3    Ortin, J.4


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