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 Key, S. C. S.
Right arrow Articles by Pagano, J. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Key, S. C. S.
Right arrow Articles by Pagano, J. S.

 Previous Article  |  Next Article 

Journal of Virology, November 1998, p. 8485-8492, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Epstein-Barr Virus (EBV) SM Protein Enhances Pre-mRNA Processing of the EBV DNA Polymerase Transcript

S. Catherine Silver Key,1,2 Tomokazu Yoshizaki,2,3 and Joseph S. Pagano1,2,4,*

Department of Microbiology and Immunology,1 Department of Medicine,4 and UNC Lineberger Comprehensive Cancer Center,2 University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, and Department of Otolaryngology, School of Medicine, Kanazawa University, Kanazawa, Ishikawa 920, Japan3

Received 2 March 1998/Accepted 29 July 1998

The Epstein-Barr virus (EBV) DNA polymerase (pol) mRNA, which contains a noncanonical polyadenylation signal, UAUAAA, is cleaved and polyadenylated inefficiently (S. C. S. Key and J. S. Pagano, Virology 234:147-159, 1997). We postulated that the EBV early proteins SM and M, which appear to act posttranscriptionally and are homologs of herpes simplex virus (HSV) ICP27, might compensate for the inefficient processing of pol pre-mRNA. Here we show that the SM and M proteins interact with each other in vitro. In addition, glutathione S-transferase-SM/M fusion proteins precipitate the heterogeneous ribonucleoprotein (hnRNP) C1 splicing protein. Further, the SM protein is coimmunoprecipitated from SM-expressing cell extracts with an antibody to the hnRNP A1/A2 proteins, which are splicing and nuclear shuttling proteins. Finally, the amount of processed EBV DNA polymerase mRNA was increased three- to fourfold in a HeLa cell line expressing SM; this increase was not due to enhanced transcription. Thus, inefficient processing of EBV pol RNA by cellular cleavage and polyadenylation factors appears to be compensated for and may be regulated by the early EBV protein, SM, perhaps via RNA 3'-end formation.

* Corresponding author. Mailing address: Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, UNC Lineberger Comprehensive Cancer Center, Chapel Hill, NC 27599. Phone: (919) 966-3036. Fax: (919) 966-3015. E-mail: mcaldwel{at}med.unc.edu.

Journal of Virology, November 1998, p. 8485-8492, Vol. 72, No. 11
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Calderwood, M. A., Venkatesan, K., Xing, L., Chase, M. R., Vazquez, A., Holthaus, A. M., Ewence, A. E., Li, N., Hirozane-Kishikawa, T., Hill, D. E., Vidal, M., Kieff, E., Johannsen, E. (2007). Epstein-Barr virus and virus human protein interaction maps. Proc. Natl. Acad. Sci. USA 104: 7606-7611 [Abstract] [Full Text]  
  • Hiriart, E., Farjot, G., Gruffat, H., Nguyen, M. V. C., Sergeant, A., Manet, E. (2003). A Novel Nuclear Export Signal and a REF Interaction Domain Both Promote mRNA Export by the Epstein-Barr Virus EB2 Protein. J. Biol. Chem. 278: 335-342 [Abstract] [Full Text]  
  • Poppers, J., Mulvey, M., Perez, C., Khoo, D., Mohr, I. (2002). Identification of a Lytic-Cycle Epstein-Barr Virus Gene Product That Can Regulate PKR Activation. J. Virol. 77: 228-236 [Abstract] [Full Text]  
  • Boyer, J. L., Swaminathan, S., Silverstein, S. J. (2002). The Epstein-Barr Virus SM Protein Is Functionally Similar to ICP27 from Herpes Simplex Virus in Viral Infections. J. Virol. 76: 9420-9433 [Abstract] [Full Text]  
  • Ruvolo, V., Gupta, A. K., Swaminathan, S. (2001). Epstein-Barr Virus SM Protein Interacts with mRNA In Vivo and Mediates a Gene-Specific Increase in Cytoplasmic mRNA. J. Virol. 75: 6033-6041 [Abstract] [Full Text]  
  • Farjot, G., Buisson, M., Duc Dodon, M., Gazzolo, L., Sergeant, A., Mikaelian, I. (2000). Epstein-Barr Virus EB2 Protein Exports Unspliced RNA via a Crm-1-Independent Pathway. J. Virol. 74: 6068-6076 [Abstract] [Full Text]  
  • Soliman, T. M., Silverstein, S. J. (2000). Herpesvirus mRNAs Are Sorted for Export via Crm1-Dependent and -Independent Pathways. J. Virol. 74: 2814-2825 [Abstract] [Full Text]  
  • Gupta, A. K., Ruvolo, V., Patterson, C., Swaminathan, S. (2000). The Human Herpesvirus 8 Homolog of Epstein-Barr Virus SM Protein (KS-SM) Is a Posttranscriptional Activator of Gene Expression. J. Virol. 74: 1038-1044 [Abstract] [Full Text]  
  • Boyle, S. M., Ruvolo, V., Gupta, A. K., Swaminathan, S. (1999). Association with the Cellular Export Receptor CRM 1 Mediates Function and Intracellular Localization of Epstein-Barr Virus SM Protein, a Regulator of Gene Expression. J. Virol. 73: 6872-6881 [Abstract] [Full Text]  
  • Zhao, J., Hyman, L., Moore, C. (1999). Formation of mRNA 3' Ends in Eukaryotes: Mechanism, Regulation, and Interrelationships with Other Steps in mRNA Synthesis. Microbiol. Mol. Biol. Rev. 63: 405-445 [Abstract] [Full Text]  
  • Buisson, M., Hans, F., Kusters, I., Duran, N., Sergeant, A. (1999). The C-Terminal Region but Not the Arg-X-Pro Repeat of Epstein-Barr Virus Protein EB2 Is Required for Its Effect on RNA Splicing and Transport. J. Virol. 73: 4090-4100 [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»