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Volumn 108, Issue 43, 2011, Pages 17667-17671

Cap-snatching mechanism in yeast L-A double-stranded RNA virus

Author keywords

Killer toxin; Saccharomyces cerevisiae; Transcription

Indexed keywords

ARGININE; COAT PROTEIN; DOUBLE STRANDED RNA; GAG PROTEIN; HISTIDINE; MESSENGER RNA;

EID: 80055082823     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1111900108     Document Type: Article
Times cited : (76)

References (34)
  • 1
    • 0016680603 scopus 로고
    • 5′-Terminal 7-methylguanosine in eukaryotic mRNA is required for translation
    • Muthukrishnan S, Both GW, Furuichi Y, Shatkin AJ (1975) 5′-Terminal 7-methylguanosine in eukaryotic mRNA is required for translation. Nature 255:33-37.
    • (1975) Nature , vol.255 , pp. 33-37
    • Muthukrishnan, S.1    Both, G.W.2    Furuichi, Y.3    Shatkin, A.J.4
  • 2
    • 0017351102 scopus 로고
    • 5′-Terminal structure and mRNA stability
    • Furuichi Y, LaFiandra A, Shatkin AJ (1977) 5′-Terminal structure and mRNA stability. Nature 266:235-239.
    • (1977) Nature , vol.266 , pp. 235-239
    • Furuichi, Y.1    LaFiandra, A.2    Shatkin, A.J.3
  • 3
    • 0019320732 scopus 로고
    • Modification of the 5′ end of mRNA Association of RNA triphosphatase with the RNA guanylyltransferase-RNA (guanine-7-) methyltransferase complex from vaccinia virus
    • Venkatesan S, Gershowitz A, Moss B (1980) Modification of the 5′ end of mRNA Association of RNA triphosphatase with the RNA guanylyltransferase- RNA (guanine-7-) methyltransferase complex from vaccinia virus. J Biol Chem 255:903-908.
    • (1980) J Biol Chem , vol.255 , pp. 903-908
    • Venkatesan, S.1    Gershowitz, A.2    Moss, B.3
  • 4
    • 0029107231 scopus 로고
    • Capping enzyme in eukaryotic mRNA synthesis
    • Shuman S (1995) Capping enzyme in eukaryotic mRNA synthesis. Prog Nucleic Acid Res Mol Biol 50:101-129.
    • (1995) Prog Nucleic Acid Res Mol Biol , vol.50 , pp. 101-129
    • Shuman, S.1
  • 5
    • 0019394947 scopus 로고
    • 7 GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription
    • Plotch SJ, Bouloy M, Ulmanen I, Krug RM (1981) A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription. Cell 23:847-858. (Pubitemid 11156997)
    • (1981) Cell , vol.23 , Issue.3 , pp. 847-858
    • Plotch, S.J.1    Bouloy, M.2    Ulmanen, I.3    Krug, R.M.4
  • 7
    • 77956536783 scopus 로고    scopus 로고
    • Influenza A virus polymerase: Structural insights into replication and host adaptation mechanisms
    • Boivin S, Cusack S, Ruigrok RW, Hart DJ (2010) Influenza A virus polymerase: Structural insights into replication and host adaptation mechanisms. J Biol Chem 285:28411-28417.
    • (2010) J Biol Chem , vol.285 , pp. 28411-28417
    • Boivin, S.1    Cusack, S.2    Ruigrok, R.W.3    Hart, D.J.4
  • 8
    • 45249084896 scopus 로고    scopus 로고
    • eds DM Knipe and PM Howley (Lippincott Willians and Wilkins, Philadelphia), 5th Ed
    • Wickner RB (2007) Fields Virology, eds DM Knipe and PM Howley (Lippincott Willians and Wilkins, Philadelphia), 5th Ed, pp 737-768.
    • (2007) Fields Virology , pp. 737-768
    • Wickner, R.B.1
  • 9
    • 0024553006 scopus 로고
    • The double-stranded RNA genome of yeast virus L-A encodes its own putative RNA polymerase by fusing two open reading frames
    • Icho T, Wickner RB (1989) The double-stranded RNA genome of yeast virus L-A encodes its own putative RNA polymerase by fusing two open reading frames. J Biol Chem 264:6716-6723. (Pubitemid 19114778)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.12 , pp. 6716-6723
    • Icho, T.1    Wickner, R.B.2
  • 11
    • 0026795575 scopus 로고
    • Pol of gag-pol fusion protein required for encapsidation of viral RNA of yeast L-A virus
    • Fujimura T, Ribas JC, Makhov AM, Wickner RB (1992) Pol of gag-pol fusion protein required for encapsidation of viral RNA of yeast L-A virus. Nature 359:746-749.
    • (1992) Nature , vol.359 , pp. 746-749
    • Fujimura, T.1    Ribas, J.C.2    Makhov, A.M.3    Wickner, R.B.4
  • 12
    • 0021250375 scopus 로고
    • Sequence of the preprotoxin dsRNA gene of type I killer yeast: Multiple processing events produce a two-component toxin
    • Bostian KA, et al. (1984) Sequence of the preprotoxin dsRNA gene of type I killer yeast: Multiple processing events produce a two-component toxin. Cell 36:741-751. (Pubitemid 14126210)
    • (1984) Cell , vol.36 , Issue.3 , pp. 741-751
    • Bostian, K.A.1    Elliot, Q.2    Bussey, H.3
  • 13
    • 0025956710 scopus 로고
    • Expression of yeast L-A double-stranded RNA virus proteins produces derepressed replication: A ski- Phenocopy
    • Wickner RB, Icho T, Fujimura T, Widner WR (1991) Expression of yeast L-A double-stranded RNA virus proteins produces derepressed replication: A ski- phenocopy. J Virol 65:155-161.
    • (1991) J Virol , vol.65 , pp. 155-161
    • Wickner, R.B.1    Icho, T.2    Fujimura, T.3    Widner, W.R.4
  • 14
    • 0026668288 scopus 로고
    • The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA
    • Blanc A, Goyer C, Sonenberg N (1992) The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA. Mol Cell Biol 12:3390-3398.
    • (1992) Mol Cell Biol , vol.12 , pp. 3390-3398
    • Blanc, A.1    Goyer, C.2    Sonenberg, N.3
  • 15
    • 0028231420 scopus 로고
    • 1 satellite virus expression
    • Blanc A, Ribas JC, Wickner RB, Sonenberg N (1994) His-154 is involved in the linkage of the Saccharomyces cerevisiae L-A double-stranded RNA virus Gag protein to the Cap structure of mRNAs and is essential for M1 satellite virus expression. Mol Cell Biol 14:2664-2674. (Pubitemid 24108248)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.4 , pp. 2664-2674
    • Blanc, A.1    Ribas, J.C.2    Wickner, R.B.3    Sonenberg, N.4
  • 17
    • 77954902027 scopus 로고    scopus 로고
    • Yeast double-stranded RNA virus L-A deliberately synthesizes RNA transcripts with 5′-diphosphate
    • Fujimura T, Esteban R (2010) Yeast double-stranded RNA virus L-A deliberately synthesizes RNA transcripts with 5′-diphosphate. J Biol Chem 285:22911-22918.
    • (2010) J Biol Chem , vol.285 , pp. 22911-22918
    • Fujimura, T.1    Esteban, R.2
  • 18
    • 0024372433 scopus 로고
    • Reconstitution of template-dependent in vitro transcriptase activity of a yeast double-stranded RNA virus
    • Fujimura T, Wickner RB (1989) Reconstitution of template-dependent in vitro transcriptase activity of a yeast double-stranded RNA virus. J Biol Chem 264:10872-10877. (Pubitemid 19161663)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.18 , pp. 10872-10877
    • Fujimura, T.1    Wickner, R.B.2
  • 19
    • 67249100913 scopus 로고    scopus 로고
    • Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site
    • Yuan P, et al. (2009) Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site. Nature 458:909-913.
    • (2009) Nature , vol.458 , pp. 909-913
    • Yuan, P.1
  • 20
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3'→5' exoribonucleases
    • Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D (1997) The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′ → 5′ exoribonucleases. Cell 91:457-466. (Pubitemid 27508235)
    • (1997) Cell , vol.91 , Issue.4 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 22
    • 0036785914 scopus 로고    scopus 로고
    • L-A virus at 3.4 A resolution reveals particle architecture and mRNA decapping mechanism
    • Naitow H, Tang J, Canady M, Wickner RB, Johnson JE (2002) L-A virus at 3.4 A resolution reveals particle architecture and mRNA decapping mechanism. Nat Struct Biol 9:725-728.
    • (2002) Nat Struct Biol , vol.9 , pp. 725-728
    • Naitow, H.1    Tang, J.2    Canady, M.3    Wickner, R.B.4    Johnson, J.E.5
  • 23
    • 14744304265 scopus 로고    scopus 로고
    • The structural basis of recognition and removal of cellular mRNA 7-methyl G 'caps' by a viral capsid protein: A unique viral response to host defense
    • DOI 10.1002/jmr.724
    • Tang J, et al. (2005) The structural basis of recognition and removal of cellular mRNA 7-methyl G 'caps' by a viral cased protein: A unique viral response to host defense. J Mol Recognit 18:158-168. (Pubitemid 40328577)
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.2 , pp. 158-168
    • Tang, J.1    Naitow, H.2    Gardner, N.A.3    Kolesar, A.4    Tang, L.5    Wickner, R.B.6    Johnson, J.E.7
  • 24
    • 0028986119 scopus 로고
    • Decoying the cap-mRNA degradation system by a double-stranded RNA virus and poly(A)- MRNA surveillance by a yeast antiviral system
    • Masison DC, et al. (1995) Decoying the cap-mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system. Mol Cell Biol 15:2763-2771.
    • (1995) Mol Cell Biol , vol.15 , pp. 2763-2771
    • Masison, D.C.1
  • 25
    • 0038228666 scopus 로고    scopus 로고
    • X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes
    • HÅkansson K, Doherty AJ, Shuman S, Wigley DB (1997) X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell 89:545-553.
    • (1997) Cell , vol.89 , pp. 545-553
    • HÅkansson, K.1    Doherty, A.J.2    Shuman, S.3    Wigley, D.B.4
  • 26
    • 79959921492 scopus 로고    scopus 로고
    • Structure of the guanylyltransferase domain of human mRNA capping enzyme
    • Chu C, et al. (2011) Structure of the guanylyltransferase domain of human mRNA capping enzyme. Proc Natl Acad Sci USA 108:10104-10108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 10104-10108
    • Chu, C.1
  • 27
    • 77649260792 scopus 로고    scopus 로고
    • Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase
    • Ogino T, Yadav SP, Banerjee AK (2010) Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase. Proc Natl Acad Sci USA 107:3463-3468.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3463-3468
    • Ogino, T.1    Yadav, S.P.2    Banerjee, A.K.3
  • 28
    • 0031060112 scopus 로고    scopus 로고
    • Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities
    • Ahola T, Laakkonen P, Vihinen H, Kääriäinen L (1997) Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities. J Virol 71:392-397. (Pubitemid 26412304)
    • (1997) Journal of Virology , vol.71 , Issue.1 , pp. 392-397
    • Ahola, T.1    Laakkonen, P.2    Vihinen, H.3    Kaariainen, L.4
  • 29
    • 0032710835 scopus 로고    scopus 로고
    • Putative RNA capping activities encoded by brome mosaic virus: Methylation and covalent binding of guanylate by replicase protein 1a
    • Ahola T, Ahlquist P (1999) Putative RNA capping activities encoded by brome mosaic virus: methylation and covalent binding of guanylate by replicase protein 1a. J Virol 73:10061-10069.
    • (1999) J Virol , vol.73 , pp. 10061-10069
    • Ahola, T.1    Ahlquist, P.2
  • 30
    • 16844378432 scopus 로고    scopus 로고
    • MRNA guanylation catalyzed by the S-adenosylmethionine-dependent guanylyltransferase of bamboo mosaic virus
    • Huang YL, Hsu YH, Han YT, Meng M (2005) mRNA guanylation catalyzed by the S-adenosylmethionine-dependent guanylyltransferase of bamboo mosaic virus. J Biol Chem 280:13153-13162.
    • (2005) J Biol Chem , vol.280 , pp. 13153-13162
    • Huang, Y.L.1    Hsu, Y.H.2    Han, Y.T.3    Meng, M.4
  • 31
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5' cap-binding protein (elF4E) bound to 7-methyl-GDP
    • Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK (1997) Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 89:951-961. (Pubitemid 27513521)
    • (1997) Cell , vol.89 , Issue.6 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.-C.2    Sonenberg, N.3    Burley, S.K.4
  • 32
    • 18144398494 scopus 로고    scopus 로고
    • Recognition of mRNA cap structures by viral and cellular proteins
    • DOI 10.1099/vir.0.80755-0
    • Fechter P, Brownlee GG (2005) Recognition of mRNA cap structures by viral and cellular proteins. J Gen Virol 86:1239-1249. (Pubitemid 40613240)
    • (2005) Journal of General Virology , vol.86 , Issue.5 , pp. 1239-1249
    • Fechter, P.1    Brownlee, G.G.2
  • 33
    • 0034723208 scopus 로고    scopus 로고
    • Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2
    • DOI 10.1074/jbc.275.4.2804
    • Luongo CL, Reinisch KM, Harrison SC, Nibert ML (2000) Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2. J Biol Chem 275:2804-2810. (Pubitemid 30082052)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.4 , pp. 2804-2810
    • Luongo, C.L.1    Reinisch, K.M.2    Harrison, S.C.3    Nibert, M.L.4
  • 34
    • 34547124095 scopus 로고    scopus 로고
    • Interactions of the RNA polymerase with the viral genome at the 5′- and 3′-ends contribute to 20S RNA narnavirus persistence in yeast
    • DOI 10.1074/jbc.M702432200
    • Fujimura T, Esteban R (2007) Interactions of the RNA polymerase with the viral genome at the 5′- and 3′-ends contribute to 20S RNA narnavirus persistence in yeast. J Biol Chem 282:19011-19019. (Pubitemid 47100141)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.26 , pp. 19011-19019
    • Fujimura, T.1    Esteban, R.2


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