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Gross, H.* ; Barth, S.* ; Palermo, R.D.* ; Mamiani, A.* ; Hennard, C. ; Zimber-Strobl, U. ; West, M.J.* ; Kremmer, E. ; Grässer, F.A.*

Asymmetric Arginine dimethylation of Epstein-Barr virus nuclear antigen 2 promotes DNA targeting.

Virology 397, 299-310 (2010)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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
Corresponding Author
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 Article Number: , Supplement: ,
Publisher Elsevier
Non-patent literature Publications
Reviewing status Peer reviewed