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Journal of Virology, March 2009, p. 2393-2396, Vol. 83, No. 5
0022-538X/09/$08.00+0     doi:10.1128/JVI.02339-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Interaction of Human Cytomegalovirus pUL84 with Casein Kinase 2 Is Required for oriLyt-Dependent DNA Replication{triangledown}

Yang Gao and Gregory S. Pari*

University of Nevada School of Medicine, Department of Microbiology & Immunology and the Cell and Molecular Biology Graduate Program, Reno, Nevada 89557

Received 10 November 2008/ Accepted 5 December 2008

Human cytomegalovirus pUL84 is a phosphorylated protein that is required for lytic DNA replication and participates in regulation of virus gene expression. We previously used a proteomics assay to show that human cytomegalovirus pUL84 interacts with casein kinase 2 (CK2). We now have demonstrated that pUL84 is a substrate for CK2 in vitro, and we have determined that two putative CK2 phosphorylation sites within pUL84 mediate binding to CK2. Mutation of a threonine residue at amino acid (aa) 148 and a serine residue at aa 157 within the pUL84 protein resulted in the inability of the protein to interact with the CK2{alpha} subunit in transfected cells. Interaction of pUL84 with CK2 was essential for complementation of oriLyt-dependent DNA replication, suggesting that phosphorylation is an essential modification.


* Corresponding author. Mailing address: University of Nevada—Reno, Department of Microbiology, Howard Bldg. 210, Reno, NV 89557. Phone: (775) 784-4824. Fax: (775) 327-2332. E-mail: gpari{at}medicine.nevada.edu

{triangledown} Published ahead of print on 17 December 2008.


Journal of Virology, March 2009, p. 2393-2396, Vol. 83, No. 5
0022-538X/09/$08.00+0     doi:10.1128/JVI.02339-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.




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