This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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 Souki, S. K.
Right arrow Articles by Sandri-Goldin, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Souki, S. K.
Right arrow Articles by Sandri-Goldin, R. M.

 Previous Article  |  Next Article 

Journal of Virology, June 2009, p. 5309-5320, Vol. 83, No. 11
0022-538X/09/$08.00+0     doi:10.1128/JVI.00238-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Arginine Methylation of the ICP27 RGG Box Regulates ICP27 Export and Is Required for Efficient Herpes Simplex Virus 1 Replication{triangledown} ,{dagger}

Stuart K. Souki,1 Paul D. Gershon,2 and Rozanne M. Sandri-Goldin1*

Department of Microbiology and Molecular Genetics, School of Medicine,1 Department of Molecular Biology and Biochemistry, University of California, Irvine, California 926972

Received 3 February 2009/ Accepted 19 March 2009

The herpes simplex virus 1 (HSV-1) multifunctional regulatory protein ICP27 shuttles between the nucleus and cytoplasm in its role as a viral mRNA export factor. Arginine methylation on glycine- and arginine-rich motifs has been shown to regulate protein export. ICP27 contains an RGG box and has been shown to be methylated during viral infection. We found by mass spectrometric analysis that three arginine residues within the RGG box were methylated. Viral mutants with substitutions of lysine for arginine residues were created as single, double, and triple mutants. Growth of these mutants was impaired and the viral replication cycle was delayed compared to wild-type HSV-1. Most striking was the finding that under conditions of hypomethylation resulting from infection with arginine substitution mutants or treatment of wild-type HSV-1-infected cells with the methylation inhibitor adenosine dialdehyde, ICP27 export to the cytoplasm occurred earlier and was more rapid than wild-type ICP27 export. We conclude that arginine methylation of the ICP27 RGG box regulates its export activity and that early export of ICP27 interferes with the performance of its nuclear functions.


* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, School of Medicine, Medical Sciences, B240, University of California, Irvine, CA 92697-4025. Phone: (949) 824-7570. Fax: (949) 824-9054. E-mail: rmsandri{at}uci.edu

{triangledown} Published ahead of print on 25 March 2009.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.


Journal of Virology, June 2009, p. 5309-5320, Vol. 83, No. 11
0022-538X/09/$08.00+0     doi:10.1128/JVI.00238-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Souki, S. K., Sandri-Goldin, R. M. (2009). Arginine Methylation of the ICP27 RGG Box Regulates the Functional Interactions of ICP27 with SRPK1 and Aly/REF during Herpes Simplex Virus 1 Infection. J. Virol. 83: 8970-8975 [Abstract] [Full Text]