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Journal of Virology, September 2009, p. 8970-8975, Vol. 83, No. 17
0022-538X/09/$08.00+0 doi:10.1128/JVI.00801-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Department of Microbiology and Molecular Genetics, School of Medicine, University of California, Irvine, California 92697
Received 20 April 2009/ Accepted 16 June 2009
The herpes simplex virus 1 protein ICP27 is methylated on arginine residues within an RGG box, and arginine methylation regulates ICP27 export to the cytoplasm. Arginine methylation can regulate protein-protein interactions; therefore, we examined the effect of hypomethylation on ICP27's interactions with cellular proteins SRPK1 and Aly/REF, which bind to ICP27 through the RGG box region. During infections with viral mutants containing lysine substitutions or the methylation inhibitor adenosine dialdehyde, the interaction of ICP27 with SRPK1 and Aly/REF was decreased, as determined by coimmunoprecipitation and colocalization studies, indicating that ICP27 RGG box methylation regulates interaction with these proteins.
Published ahead of print on 24 June 2009.
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