Lysine acetylation of histones defines the epigenetic status of human embryonic stem cells
and orchestrates DNA replication, chromosome condensation, transcription, telomeric …

Histone lysine acetylation is a major mechanism by which cells regulate the structure and
function of chromatin, and new sites of acetylation continue to be discovered. Here we …

The histone code hypothesis holds that covalent posttranslational modifications of histone
tails are interpreted by the cell to yield a rich combinatorial transcriptional output. This …

The Gcn5p histone acetyltransferase exhibits a limited substrate specificity in vitro. However,
neither the specificity of this enzyme in vivo nor the importance of particular acetylated …

Post-translational modification of histones is a central aspect of gene regulation. Emerging
data indicate that modification at one site can influence modification of a second site. As one …

Transcriptionally active DNA is packaged with histones that are post-translationally
acetylated on multiple lysines within their amino termini. While the majority of this acetylation …

During periods of active DNA replication and chromatin assembly, newly synthesized
histone H4 is deposited in a diacetylated form. In Tetrahymena, a specific pair of residues …

The N‐terminal domains of all four core histones are subject to reversible acetylation at
certain lysine residues. This modification has been functionally linked to transcription …

Post-translational histone modifications abound and regulate multiple nuclear processes.
Most modifications are targeted to the amino-terminal domains of histones. Here we report …

Diverse agents, including growth factors and phorbol esters, induce rapid transcriptional
activation of a subset of immediate-early (IE) genes that include the protooncogenes c-fos …