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J Biol Chem, Vol. 274, Issue 41, 28991-28998, October 8, 1999
From the Herpes simplex virus type 1 (HSV-1), the
prototype
The Multifunctional Herpes Simplex Virus IE63 Protein Interacts
with Heterogeneous Ribonucleoprotein K and with Casein Kinase 2
,,,
,, and
Institute of Virology, University of
Glasgow, Church St., Glasgow G11 5JR, Scotland, United Kingdom,
¶ Laboratoire de Biochimie des Regulations Cellulaires Endocrines,
INSERM U244, 17 rue des Martyrs, F-38054 Grenoble, France, and the
Department of Molecular Microbiology and Immunology, University
of Southern California School of Medicine,
Los Angeles, California 90033-1054.
-herpesvirus, causes several prominent diseases. The HSV-1
immediate early (IE) protein IE63 (ICP27) is the only regulatory gene
with a homologue in every mammalian and avian herpesvirus sequenced so
far. IE63 is a multifunctional protein affecting transcriptional and
post-transcriptional processes, and it can shuttle from the nucleus to
the cytoplasm. To identify interacting cellular proteins, a HeLa
cDNA library was screened in the yeast two-hybrid system using IE63
as bait. Several interacting proteins were identified including
heterogeneous nuclear ribonucleoprotein K (hnRNP K), a multifunctional
protein like IE63, and the 
subunit of casein kinase 2 (CK2), a
protein kinase, and interacting regions were mapped. Confirmation of
interactions was provided by fusion protein binding assays,
co-immunoprecipitation from infected cells, and CK2 activity assays.
hnRNP K co-immunoprecipitated from infected cells with anti-IE63 serum
was a more rapidly migrating subfraction than hnRNP K
immunoprecipitated by anti-hnRNP K serum. Using anti-IE63 serum, both
IE63 and hnRNP K were phosphorylated in vitro by CK2, while
in immunoprecipitates using anti-hnRNP K serum, IE63 but not hnRNP K
was phosphorylated by CK2. These data provide important new insights
into how this key viral regulatory protein exerts its functions.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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