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Journal of Virology, February 2007, p. 1072-1082, Vol. 81, No. 3
0022-538X/07/$08.00+0     doi:10.1128/JVI.01473-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Kaposi's Sarcoma-Associated Herpesvirus-Encoded Protein Kinase and Its Interaction with K-bZIP{triangledown}

Yoshihiro Izumiya,1 Chie Izumiya,1 Albert Van Geelen,2 Don-Hong Wang,1,3 Kit S. Lam,3 Paul A. Luciw,2* and Hsing-Jien Kung1*

Department of Biological Chemistry and Molecular Medicine, University of California-Davis School of Medicine, University of California-Davis Cancer Center, Research Building III, Room 2400, 4645 2nd Avenue, Sacramento, California 95817,1 Center for Comparative Medicine and Department of Pathology, University of California-Davis, 1 Shields Avenue, Davis, California 95616,2 Division of Hematology and Oncology, Department of Internal Medicine, University of California-Davis Cancer Center, 4501 X Street, Sacramento, California 958173

Received 11 July 2006/ Accepted 30 October 2006

The oncogenic herpesvirus, Kaposi's sarcoma-associated herpesvirus, also identified as human herpesvirus 8, contains genes producing proteins that control transcription and influence cell signaling. Open reading frame 36 (ORF36) of this virus encodes a serine/threonine protein kinase, which is designated the viral protein kinase (vPK). Our recent efforts to elucidate the role of vPK in the viral life cycle have focused on identifying viral protein substrates and determining the effects of vPK-mediated phosphorylation on specific steps in viral replication. The vPK gene was transcribed into 4.2-kb and 3.6-kb mRNAs during the early and late phases of viral reactivation. vPK is colocalized with viral DNA replication/transcription compartments as marked by a polymerase processivity factor, and K-bZIP, a protein known to bind the viral DNA replication origin (Ori-Lyt) and to regulate viral transcription. The vPK physically associated with and strongly phosphorylated K-bZIP at threonine 111, a site also recognized by the cyclin-dependent kinase Cdk2. Both K-bZIP and vPK were corecruited to viral promoters targeted by K-bZIP as well as to the Ori-Lyt region. Phosphorylation of K-bZIP by vPK had a negative impact on K-bZIP transcription repression activity. The extent of posttranslational modification of K-bZIP by sumoylation, a process that influences its repression function, was decreased by vPK phosphorylation at threonine 111. Our data thus identify a new role of vPK as a modulator of viral transcription.

* Corresponding author. Mailing address for Hsing-Jien Kung: University of California-Davis, Cancer Center, Research III Room 2400B, 4645 2nd Ave., Sacramento, CA 95817. Phone: (916) 734-1538. Fax: (916) 734-2589. E-mail: hkung{at}ucdavis.edu. Mailing address for Paul A. Luciw: Center for Comparative Medicine, Department of Pathology and Laboratory Medicine, University of California-Davis, 1 Shields Ave., Davis, CA 95616. Phone: (530) 752-3430. Fax: (530) 752-7914. E-mail: paluciw{at}ucdavis.edu.

{triangledown} Published ahead of print on 15 November 2006.

Journal of Virology, February 2007, p. 1072-1082, Vol. 81, No. 3
0022-538X/07/$08.00+0     doi:10.1128/JVI.01473-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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