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 Ogino, T.
Right arrow Articles by Banerjee, A. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ogino, T.
Right arrow Articles by Banerjee, A. K.

 Previous Article  |  Next Article 

Journal of Virology, August 2008, p. 7729-7734, Vol. 82, No. 15
0022-538X/08/$08.00+0     doi:10.1128/JVI.00326-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Formation of Guanosine(5')Tetraphospho(5')Adenosine Cap Structure by an Unconventional mRNA Capping Enzyme of Vesicular Stomatitis Virus{triangledown}

Tomoaki Ogino and Amiya K. Banerjee*

Department of Molecular Genetics, Section of Virology, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195

Received 14 February 2008/ Accepted 12 May 2008

The RNA-dependent RNA polymerase L protein of vesicular stomatitis virus (VSV) elicits GTPase and RNA:GDP polyribonucleotidyltransferase (PRNTase) activities to produce a 5'-cap core structure, guanosine(5')triphospho(5')adenosine (GpppA), on viral mRNAs. Here, we report that the L protein produces an unusual cap structure, guanosine(5')tetraphospho(5')adenosine (GppppA), that is formed by the transfer of the 5'-monophosphorylated viral mRNA start sequence to GTP by the PRNTase activity before the removal of the {gamma}-phosphate from GTP by GTPase. Interestingly, GppppA-capped and polyadenylated full-length mRNAs were also found to be synthesized by an in vitro transcription system with the native VSV RNP.

* Corresponding author. Mailing address: Department of Molecular Genetics, Section of Virology, Lerner Research Institute, Cleveland Clinic, 9500 Euclid Avenue, Cleveland, OH 44195. Phone: (216) 444-0625. Fax: (216) 444-2998. E-mail: banerja{at}ccf.org

{triangledown} Published ahead of print on 21 May 2008.

Journal of Virology, August 2008, p. 7729-7734, Vol. 82, No. 15
0022-538X/08/$08.00+0     doi:10.1128/JVI.00326-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gopinath, M., Shaila, M. S. (2009). RNA triphosphatase and guanylyl transferase activities are associated with the RNA polymerase protein L of rinderpest virus. J. Gen. Virol. 90: 1748-1756 [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»