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Open Access Green as soon as Postprint is submitted to ZB.
Asymmetric Arginine dimethylation of Epstein-Barr virus nuclear antigen 2 promotes DNA targeting.
Virology 397, 299-310 (2010)
The Epstein-Barr virus (EBV) growth-transforms B-lymphocytes. The virus-encoded nuclear antigen 2 (EBNA2) is essential for transformation and activates gene expression by association with DNA-bound transcription factors such as RBPJκ (CSL/CBF1). We have previously shown that EBNA2 contains symmetrically dimethylated Arginine (sDMA) residues. Deletion of the RG-repeat results in a reduced ability of the virus to immortalise B-cells. We now show that the RG repeat also contains asymmetrically dimethylated Arginines (aDMA) but neither non-methylated (NMA) Arginines nor citrulline residues. We demonstrate that only aDMA-containing EBNA2 is found in a complex with DNA-bound RBPJκ in vitro and preferentially associates with the EBNA2-responsive EBV C, LMP1 and LMP2A promoters in vivo. Inhibition of methylation in EBV-infected cells results in reduced expression of the EBNA2-regulated viral gene LMP1, providing additional evidence that methylation is a prerequisite for DNA-binding by EBNA2 via association with the transcription factor RBPJκ.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Epstein-Barr virus; EBV; Nuclear antigen 2; EBNA2; Methylation; Arginine; sDMA; aDMA; RBPJκ; DNA-binding
ISSN (print) / ISBN
0042-6822
e-ISSN
0042-6822
Journal
Virology
Quellenangaben
Volume: 397,
Issue: 2,
Pages: 299-310
Publisher
Elsevier
Non-patent literature
Publications
Reviewing status
Peer reviewed