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Journal of Virology, June 2005, p. 6757-6762, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6757-6762.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Carboxyl-Terminal Domain of RNA Polymerase II Is Phosphorylated by a Complex Containing cdk9 and Infected-Cell Protein 22 of Herpes Simplex Virus 1

Lizette O. Durand, Sunil J. Advani, Alice P. W. Poon, and Bernard Roizman*

The Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago, Chicago, Illinois 60637

Received 17 December 2004/ Accepted 1 February 2005

The infected-cell protein 22 (ICP22), a regulatory protein encoded by the {alpha}22 gene of herpes simplex virus 1, is required for the optimal expression of a set of late viral proteins that includes the products of the US11, UL38, and UL41 genes. ICP22 has two activities. Thus, ICP22 and the UL13 protein kinase mediate the activation of cdc2 and degradation of its partners, cyclins A and B. cdc2 and its new partner, the DNA polymerase accessory factor (UL42), bind topoisomerase II{alpha} in an ICP22-dependent manner. In addition, ICP22 and UL13 mediate an intermediate phosphorylation of the carboxyl terminus of RNA polymerase II (RNA POL II). Here we report another function of ICP22. Thus, ICP22 physically interacts with cdk9, a constitutively active cyclin-dependent kinase involved in transcriptional regulation. A protein complex containing ICP22 and cdk9 phosphorylates in vitro the carboxyl-terminal domain of RNA POL II in a viral US3 protein kinase-dependent fashion. Finally, the carboxyl-terminal domain of RNA POL II fused to glutathione S-transferase is phosphorylated in reaction mixtures containing complexes pulled down with ICP22 or cdk9 immune precipitated from lysates of wild-type parent virus or {Delta}UL13 but not {Delta}US3 mutant-infected cells. The experiments described here place ICP22 and cdk9 in a complex with the carboxyl-terminal domain of RNA POL II. At the same time we confirm the requirement of ICP22 and the UL13 protein kinase in the posttranslational modification of RNA POL II that alters its electrophoretic mobility, although US3 kinase appears to play a role in a cell-type-dependent fashion.

* Corresponding author. Mailing address: The Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago, 910 East 58th Street, Chicago, IL 60637. Phone: (773) 702-1898. Fax: (773) 702-1631. E-mail: Bernard.Roizman{at}bsd.uchicago.edu.

Journal of Virology, June 2005, p. 6757-6762, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6757-6762.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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