This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Deng, T.
Right arrow Articles by Brownlee, G. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Deng, T.
Right arrow Articles by Brownlee, G. G.

 Previous Article

Journal of Virology, July 2005, p. 8669-8674, Vol. 79, No. 13
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.13.8669-8674.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

In Vitro Assembly of PB2 with a PB1-PA Dimer Supports a New Model of Assembly of Influenza A Virus Polymerase Subunits into a Functional Trimeric Complex

Tao Deng, Jane Sharps, Ervin Fodor, and George G. Brownlee*

Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom

Received 17 January 2005/ Accepted 7 March 2005

Influenza virus RNA-dependent RNA polymerase is a heterotrimeric complex of PB1, PB2, and PA. We show that the individually expressed PB2 subunit can be assembled with the coexpressed PB1-PA dimer in vitro into a transcriptionally active complex. Furthermore, we demonstrate that a model viral RNA promoter can bind to the PB1-PA dimer prior to assembly with PB2. Our results are consistent with a recently proposed model for the sequential assembly of viral RNA polymerase complex in which the PB1-PA dimeric complex and the PB2 monomer are transported into the nucleus separately and then assembled in the nucleus.

* Corresponding author. Mailing address: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom. Phone: 44 (01865) 275559. Fax: 44 (01865) 275556. E-mail: george.brownlee{at}path.ox.ac.uk.

Journal of Virology, July 2005, p. 8669-8674, Vol. 79, No. 13
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.13.8669-8674.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • te Velthuis, A. J. W., Arnold, J. J., Cameron, C. E., van den Worm, S. H. E., Snijder, E. J. (2009). The RNA polymerase activity of SARS-coronavirus nsp12 is primer dependent. Nucleic Acids Res 0: gkp904v1-gkp904 [Abstract] [Full Text]  
  • Hemerka, J. N., Wang, D., Weng, Y., Lu, W., Kaushik, R. S., Jin, J., Harmon, A. F., Li, F. (2009). Detection and Characterization of Influenza A Virus PA-PB2 Interaction through a Bimolecular Fluorescence Complementation Assay. J. Virol. 83: 3944-3955 [Abstract] [Full Text]  
  • Bradel-Tretheway, B. G., Kelley, Z., Chakraborty-Sett, S., Takimoto, T., Kim, B., Dewhurst, S. (2008). The human H5N1 influenza A virus polymerase complex is active in vitro over a broad range of temperatures, in contrast to the WSN complex, and this property can be attributed to the PB2 subunit. J. Gen. Virol. 89: 2923-2932 [Abstract] [Full Text]  
  • Vreede, F. T., Brownlee, G. G. (2007). Influenza Virion-Derived Viral Ribonucleoproteins Synthesize both mRNA and cRNA In Vitro. J. Virol. 81: 2196-2204 [Abstract] [Full Text]  
  • Naito, T., Momose, F., Kawaguchi, A., Nagata, K. (2007). Involvement of Hsp90 in Assembly and Nuclear Import of Influenza Virus RNA Polymerase Subunits. J. Virol. 81: 1339-1349 [Abstract] [Full Text]  
  • Deng, T., Engelhardt, O. G., Thomas, B., Akoulitchev, A. V., Brownlee, G. G., Fodor, E. (2006). Role of Ran Binding Protein 5 in Nuclear Import and Assembly of the Influenza Virus RNA Polymerase Complex. J. Virol. 80: 11911-11919 [Abstract] [Full Text]  
  • Deng, T., Sharps, J. L., Brownlee, G. G. (2006). Role of the influenza virus heterotrimeric RNA polymerase complex in the initiation of replication.. J. Gen. Virol. 87: 3373-3377 [Abstract] [Full Text]  
  • Hara, K., Schmidt, F. I., Crow, M., Brownlee, G. G. (2006). 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 [Abstract] [Full Text]  
  • Jung, T. E., Brownlee, G. G. (2006). A new promoter-binding site in the PB1 subunit of the influenza A virus polymerase.. J. Gen. Virol. 87: 679-688 [Abstract] [Full Text]  
  • Deng, T., Vreede, F. T., Brownlee, G. G. (2006). Different De Novo Initiation Strategies Are Used by Influenza Virus RNA Polymerase on Its cRNA and Viral RNA Promoters during Viral RNA Replication. J. Virol. 80: 2337-2348 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»