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Abstract
The Epstein-Barr virus-encoded nuclear antigens EBNA2 and EBNA3C both interact with the cellular transcription factor RBP-Jkappa and modulate the expression of several shared target genes, suggesting a tight cooperation in latently infected cells. In a survey for additional cellular factors that bind to EBNA2 as well as EBNA3C, we have isolated and characterized DP103, a novel human member of the DEAD box family of putative ATP-dependent RNA helicases. The interaction with DP103 is mediated by amino acids (aa) 121-213 of EBNA2 and aa 534-778 of EBNA3C, regions that are not involved in binding of the viral proteins to RBP-Jkappa. The DP103-cDNA encodes a protein of 824 aa that harbors all of the common DEAD box motifs. Monoclonal antibodies raised against DP103 detect a protein of 103 kDa in mammalian cells that resides in high molecular weight complexes in vivo. We have detected an ATPase activity intrinsic to or closely associated with DP103. By subcellular fractionation, we find DP103 in both a soluble nuclear fraction as well as in the insoluble skeletal fraction. Whereas the protein and its mRNA are uniformly expressed in all tested cell lines, we observed differential expression of the mRNA in normal human tissues.
Highlights
The Epstein-Barr virus (EBV),1 a ubiquitous human ␥-herpesvirus, is the etiological agent of infectious mononucleosis and is associated with a number of tumors, such as the endemic form of Burkitt’s lymphoma (BL), nasopharyngeal carcinoma, and Hodgkin’s disease
Isolation of a cDNA Clone Interacting with EBNA2A and EBNA3C—In a search for proteins that interact with both EBNA2 and EBNA3C, we determined whether candidate clones identified in a previous two-hybrid screen for EBNA2associated proteins could bind to EBNA3C in this assay
The ability to interact with the protein encoded by SE97 is conserved between the EBNA2 and EBNA3C alleles of both types 1 and 2 EBV strains
Summary
Vol 274, No 27, Issue of July 2, pp. 19136 –19144, 1999 Printed in U.S.A. Characterization of DP103, a Novel DEAD Box Protein That Binds to the Epstein-Barr Virus Nuclear Proteins EBNA2 and EBNA3C*. The Epstein-Barr virus-encoded nuclear antigens EBNA2 and EBNA3C both interact with the cellular transcription factor RBP-J and modulate the expression of several shared target genes, suggesting a tight cooperation in latently infected cells. In a survey for additional cellular factors that bind to EBNA2 as well as EBNA3C, we have isolated and characterized DP103, a novel human member of the DEAD box family of putative ATP-dependent RNA helicases. We report the cloning and characterization of DP103, a novel member of the DEAD box family of putative ATP-dependent RNA helicases, which was isolated due to its ability to bind to EBNA2 as well as EBNA3C. DEAD box proteins have been shown to play important roles in cell development, differentiation, and proliferation They are implicated in most processes that are linked to RNA metabolism, such as translation initiation, pre-mRNA splicing, ribosome assembly, mRNA stabilization, and mRNA transport
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