| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Previous Article | Next Article ![]()
Journal of Virology, December 2007, p. 13242-13247, Vol. 81, No. 23
0022-538X/07/$08.00+0 doi:10.1128/JVI.01396-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Anita Koroknai,1,
György Fejer,2,
Agnes Bakos,1
Ferenc Banati,1
Kalman Szenthe,1
Hans Wolf,3
Hans Helmut Niller,3
Janos Minarovits,1 and
Daniel Salamon1*
Microbiological Research Group, National Center for Epidemiology, Pihenö u. 1, H-1529 Budapest, Hungary,1 Max-Planck Institut für Immunbiologie, Stübeweg 51, D-79108 Freiburg,2 Department of Microbiology and Hygiene, University of Regensburg, Franz-Josef-Strauss Allee 11, D-93053 Regensburg, Germany3
Received 26 June 2007/ Accepted 31 August 2007
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.
Published ahead of print on 26 September 2007.
These authors contributed equally to the work.
This article has been cited by other articles:
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
|---|
| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
|---|