Affiliation:
1. Molecular Biology Institute, University of California Los Angeles, Los Angeles, California, USA
2. Department of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, California, USA
Abstract
Despite a wealth of data associating promoter and enhancer region histone N-terminal tail lysine acetylation with transcriptional activity, there are relatively few examples of studies that establish causation between these histone posttranslational modifications and transcription. While hypoacetylation of histone H3 lysines 18 and 27 is associated with repression, the step(s) in the overall process of transcription that is blocked at a hypoacetylated promoter is not clearly established in most instances. Studies presented here confirm that the adenovirus 2 large E1A protein activation domain interacts with p300, as reported previously (P. Pelka, J. N. G. Ablack, J. Torchia, A. S. Turnell, R. J. A. Grand, J. S. Mymryk, Nucleic Acids Res
37:
1095–1106, 2009,
https://doi.org/10.1093/nar/gkn1057
), and that the resulting acetylation of H3K18/27 affects varied steps in transcription at different viral promoters.
Funder
HHS | National Institutes of Health
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Cited by
15 articles.
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