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J Biol Chem, Vol. 273, Issue 28, 17651-17659, July 10, 1998
From the § Howard Hughes Medical Institute and
Hepatitis C virus (HCV) core protein, a component
of viral nucleocapsid, has been shown to modulate cellular and viral
promoter activities. To identify potential cellular targets for HCV
core protein, a human liver cDNA library was screened for
core-interacting proteins using the yeast two-hybrid system. Among the
proteins identified was heterogeneous nuclear ribonucleoprotein K
(hnRNP K), which has been demonstrated to be a transcriptional
regulator. The interaction of HCV core protein with hnRNP K was
confirmed by glutathione S-transferase fusion protein
binding assay, protein-protein blotting assay, and
coimmunoprecipitation in vitro and in vivo. Additionally, these two proteins were shown to be partially colocalized in the nucleus. The hnRNP K-binding site in HCV core protein was mapped
to the region from amino acid residues 25-91, a hydrophilic area near
the N terminus. The HCV core protein-binding domain was located within
amino acid residues 250 to 392, which contain the three proline-rich
domains, of hnRNP K. Furthermore, HCV core protein relieved the
suppression effect of hnRNP K on the activity of the human thymidine
kinase gene promoter. The specific binding of HCV core protein to hnRNP
K suggests that multiple functions of hnRNP K may be disrupted by the
core protein during HCV infection and thus explains, in part, the
pathogenesis of HCV.
Hepatitis C Virus Core Protein Interacts with Heterogeneous
Nuclear Ribonucleoprotein K
,,
, and§
Department of Molecular Microbiology and Immunology,
Department of Biochemistry and the Norris Cancer Research
Institute, University of Southern California School of Medicine, Los
Angeles, California 90033-1054 and the ¶ Institute of Environment
and Life Science, the Hallym Academy of Science, Hallym
University, Chuncheon 200-702, Korea
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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