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 Curran, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Curran, J.

 Previous Article  |  Next Article 

J Virol, May 1998, p. 4274-4280, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

A Role for the Sendai Virus P Protein Trimer in RNA Synthesis

Joseph Curran*

Department of Genetics and Microbiology, University of Geneva Medical School, CH1211 Geneva, Switzerland

Received 16 September 1997/Accepted 10 February 1998

The SeV P protein is found as a homotrimer (P3) when it is expressed in mammalian cells, and trimerization is mediated by a predicted coiled-coil motif which maps within amino acids (aa) 344 to 411 (the BoxA region). The bacterially expressed protein also appears to be trimeric, apparently precluding a role for phosphorylation in the association of the P monomers. I have examined the role of P trimerization both in the protein's interaction with the nucleocapsid (N:RNA) template and in the protein's function on the template during RNA synthesis. As with the results of earlier experiments (32), I found that both the BoxA and BoxC (aa 479 to 568) regions were required for stable binding of P to the N:RNA. Binding was also observed with P proteins containing less than three BoxC regions, suggesting that trimerization may be required to permit contacts between multiple BoxC regions and the N:RNA. However, these heterologous trimers failed to function in viral RNA synthesis, indicating that the third C-terminal leg of the trimer plays an essential role in P function on the template. We speculate that this function may involve the movement of P (and possibly the polymerase complex) on the template and the maintenance of processivity.

* Mailing address: Department of Genetics and Microbiology, University of Geneva Medical School, 9 avenue de Champel, CH1211 Geneva, Switzerland. Phone: (41 22) 702 5727. Fax: (41 22) 702 5702. E-mail: curran{at}cmu.unige.ch.

J Virol, May 1998, p. 4274-4280, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Timani, K. A., Sun, D., Sun, M., Keim, C., Lin, Y., Schmitt, P. T., Schmitt, A. P., He, B. (2008). A Single Amino Acid Residue Change in the P Protein of Parainfluenza Virus 5 Elevates Viral Gene Expression. J. Virol. 82: 9123-9133 [Abstract] [Full Text]  
  • Llorente, M. T., Garcia-Barreno, B., Calero, M., Camafeita, E., Lopez, J. A., Longhi, S., Ferron, F., Varela, P. F., Melero, J. A. (2006). Structural analysis of the human respiratory syncytial virus phosphoprotein: characterization of an {alpha}-helical domain involved in oligomerization. J. Gen. Virol. 87: 159-169 [Abstract] [Full Text]  
  • Moller, P., Pariente, N., Klenk, H.-D., Becker, S. (2005). Homo-Oligomerization of Marburgvirus VP35 Is Essential for Its Function in Replication and Transcription. J. Virol. 79: 14876-14886 [Abstract] [Full Text]  
  • Bernado, P., Blanchard, L., Timmins, P., Marion, D., Ruigrok, R. W. H., Blackledge, M. (2005). A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. Proc. Natl. Acad. Sci. USA 102: 17002-17007 [Abstract] [Full Text]  
  • Schneider, U., Blechschmidt, K., Schwemmle, M., Staeheli, P. (2004). Overlap of Interaction Domains Indicates a Central Role of the P Protein in Assembly and Regulation of the Borna Disease Virus Polymerase Complex. J. Biol. Chem. 279: 55290-55296 [Abstract] [Full Text]  
  • Kingston, R. L., Baase, W. A., Gay, L. S. (2004). Characterization of Nucleocapsid Binding by the Measles Virus and Mumps Virus Phosphoproteins. J. Virol. 78: 8630-8640 [Abstract] [Full Text]  
  • Chan, Y. P., Koh, C. L., Lam, S. K., Wang, L.-F. (2004). Mapping of domains responsible for nucleocapsid protein-phosphoprotein interaction of henipaviruses. J. Gen. Virol. 85: 1675-1684 [Abstract] [Full Text]  
  • Johansson, K., Bourhis, J.-M., Campanacci, V., Cambillau, C., Canard, B., Longhi, S. (2003). Crystal Structure of the Measles Virus Phosphoprotein Domain Responsible for the Induced Folding of the C-terminal Domain of the Nucleoprotein. J. Biol. Chem. 278: 44567-44573 [Abstract] [Full Text]  
  • Longhi, S., Receveur-Brechot, V., Karlin, D., Johansson, K., Darbon, H., Bhella, D., Yeo, R., Finet, S., Canard, B. (2003). The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein. J. Biol. Chem. 278: 18638-18648 [Abstract] [Full Text]  
  • Henrickson, K. J. (2003). Parainfluenza Viruses. Clin. Microbiol. Rev. 16: 242-264 [Abstract] [Full Text]  
  • de Breyne, S., Simonet, V., Pelet, T., Curran, J. (2003). Identification of a cis-acting element required for shunt-mediated translational initiation of the Sendai virus Y proteins. Nucleic Acids Res 31: 608-618 [Abstract] [Full Text]  
  • Tuckis, J., Smallwood, S., Feller, J. A., Moyer, S. A. (2002). The C-Terminal 88 Amino Acids of the Sendai Virus P Protein Have Multiple Functions Separable by Mutation. J. Virol. 76: 68-77 [Abstract] [Full Text]  
  • Gubbay, O., Curran, J., Kolakofsky, D. (2001). Sendai virus genome synthesis and assembly are coupled: a possible mechanism to promote viral RNA polymerase processivity. J. Gen. Virol. 82: 2895-2903 [Abstract] [Full Text]  
  • Huang, C., Kiyotani, K., Fujii, Y., Fukuhara, N., Kato, A., Nagai, Y., Yoshida, T., Sakaguchi, T. (2000). Involvement of the Zinc-Binding Capacity of Sendai Virus V Protein in Viral Pathogenesis. J. Virol. 74: 7834-7841 [Abstract] [Full Text]  
  • De, B. P., Hoffman, M. A., Choudhary, S., Huntley, C. C., Banerjee, A. K. (2000). Role of NH2- and COOH-Terminal Domains of the P Protein of Human Parainfluenza Virus Type 3 in Transcription and Replication. J. Virol. 74: 5886-5895 [Abstract] [Full Text]  
  • Bowman, M. C., Smallwood, S., Moyer, S. A. (1999). Dissection of Individual Functions of the Sendai Virus Phosphoprotein in Transcription. J. Virol. 73: 6474-6483 [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»