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Journal of Virology, June 2004, p. 6067-6072, Vol. 78, No. 11
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.11.6067-6072.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

CKII Site in Epstein-Barr Virus Nuclear Protein 2 Controls Binding to hSNF5/Ini1 and Is Important for Growth Transformation

Bogaslaw Kwiatkowski,1 Szu Yu Jenny Chen, and William H. Schubach1,2*

Division of Oncology, Department of Medicine, VA Puget Sound Health Care System, and Department of Medicine, University of Washington,1 Fred Hutchinson Cancer Research Center, Seattle, Washington2

Received 14 October 2003/ Accepted 27 January 2004

Substitution mutagenesis of EBNA2 shows that its interaction with hSNF5/Ini1 involves two sites (286IPP and DQQ313), and a mutation at a CKII phosphorylation site (SS469) is essential for the interaction. An alanine substitution (SS469AA) prevents binding to EBNA2 and diminishes the growth-promotion potential of EBNA2 in the transcomplementation assay.

* Corresponding author. Mailing address: VA Puget Sound Health Care System, S-111-ONC, 1660 S. Columbian Way, Seattle, WA 98108. Phone: (206) 764-2681. Fax: (206) 764-2851. E-mail: wschu{at}u.washington.edu.

Journal of Virology, June 2004, p. 6067-6072, Vol. 78, No. 11
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.11.6067-6072.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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Copyright © 2004 by the American Society for Microbiology. All rights reserved.