Acetylated histone H3 and H4 mark the upregulated LMP2A promoter of Epstein-Barr virus in lymphoid cells

J Virol. 2007 Dec;81(23):13242-7. doi: 10.1128/JVI.01396-07. Epub 2007 Sep 26.

Abstract

We analyzed the levels of acetylated histones and histone H3 dimethylated on lysine 4 (H3K4me2) at the LMP2A promoter (LMP2Ap) of Epstein-Barr virus in well-characterized type I and type III lymphoid cell line pairs and additionally in the nasopharyngeal carcinoma cell line C666-1 by using chromatin immunoprecipitation. We found that enhanced levels of acetylated histones marked the upregulated LMP2Ap in lymphoid cells. In contrast, in C666-1 cells, the highly DNA-methylated, inactive LMP2Ap was also enriched in acetylated histones and H3K4me2. Our results suggest that the combinatorial effects of DNA methylation, histone acetylation, and H3K4me2 modulate the activity of LMP2Ap.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetylation
  • Cell Line, Tumor
  • Chromatin Immunoprecipitation
  • DNA, Viral / chemistry*
  • Herpesvirus 4, Human / chemistry
  • Herpesvirus 4, Human / physiology*
  • Histones / analysis*
  • Humans
  • Lymphocytes / chemistry
  • Lymphocytes / virology*
  • Methylation
  • Molecular Sequence Data
  • Promoter Regions, Genetic*
  • Protein Binding
  • Viral Matrix Proteins / biosynthesis*
  • Viral Matrix Proteins / genetics

Substances

  • DNA, Viral
  • EBV-associated membrane antigen, Epstein-Barr virus
  • Histones
  • Viral Matrix Proteins

Associated data

  • GENBANK/AM746938
  • GENBANK/AM746939
  • GENBANK/AM746940
  • GENBANK/AM746941
  • GENBANK/AM746942