University of Sussex
Browse

File(s) not publicly available

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

journal contribution
posted on 2023-06-08, 07:08 authored by Henrik Gross, Stephanie Barth, Richard D Palermo, Alfredo Mamiani, Christine Hennard, Ursula Zimber-Strobl, Michelle WestMichelle West, Elisabeth Kremmer, Friedrich A Grasser
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 RBPJk (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 RBPJk 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 RBPJk.

History

Publication status

  • Published

Journal

Virology

ISSN

0042-6822

Publisher

Elsevier

Issue

2

Volume

397

Page range

299-310

Pages

12.0

Department affiliated with

  • Biochemistry Publications

Research groups affiliated with

  • Haematology Research Group Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

Usage metrics

    University of Sussex (Publications)

    Categories

    No categories selected

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC