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 Parrish, S.
Right arrow Articles by Moss, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Parrish, S.
Right arrow Articles by Moss, B.

 Previous Article  |  Next Article 

Journal of Virology, December 2007, p. 12973-12978, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01668-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Characterization of a Second Vaccinia Virus mRNA-Decapping Enzyme Conserved in Poxviruses{triangledown}

Susan Parrish{dagger} and Bernard Moss*

Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0320

Received 31 July 2007/ Accepted 8 September 2007

Vaccinia virus (VACV) encodes enzymes that cap the 5' end of viral mRNAs, which enhances their stability and translation. Nevertheless, recent studies demonstrated that the VACV D10 protein (VACV-WR_115) decaps mRNA, an enzymatic activity not previously shown to be encoded by a virus. The decapping activity of D10 is dependent on a Nudix hydrolase motif that is also present in the VACV D9 protein (VACV-WR_114), which shares 25% sequence identity with D10. Here, we showed that a purified recombinant VACV D9 fusion protein also decaps mRNA and that this activity was abolished by point mutations in the Nudix hydrolase motif. Decapping was specific for a methylated cap attached to RNA and resulted in the liberation of m7GDP. D9 differed from D10 in requiring a longer capped RNA substrate for optimal activity, having greater sensitivity to inhibition by uncapped RNA, and having lower sensitivity to inhibition by nucleotide cap analogs unattached to RNA. Since D9 is expressed early in infection and D10 late, we suggest that the two proteins enhance mRNA turnover and manipulate gene expression in a complementary and overlapping manner.

* Corresponding author. Mailing address: Laboratory of Viral Diseases, National Institutes of Health, Building 33, Room 1E13C.1, 33 North Drive, MSC 3210, Bethesda, MD 20892-3210. Phone: (301) 496-9869. Fax: (480) 1535. E-mail: bmoss{at}nih.gov

{triangledown} Published ahead of print on 19 September 2007.

{dagger} Present address: McDaniel College, Westminster, MD 21157.

Journal of Virology, December 2007, p. 12973-12978, Vol. 81, No. 23
0022-538X/07/$08.00+0     doi:10.1128/JVI.01668-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Senkevich, T. G., Koonin, E. V., Moss, B. (2009). Predicted poxvirus FEN1-like nuclease required for homologous recombination, double-strand break repair and full-size genome formation. Proc. Natl. Acad. Sci. USA 106: 17921-17926 [Abstract] [Full Text]  
  • Walsh, D., Arias, C., Perez, C., Halladin, D., Escandon, M., Ueda, T., Watanabe-Fukunaga, R., Fukunaga, R., Mohr, I. (2008). Eukaryotic Translation Initiation Factor 4F Architectural Alterations Accompany Translation Initiation Factor Redistribution in Poxvirus-Infected Cells. Mol. Cell. Biol. 28: 2648-2658 [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»