The association of histones with specific chaperone complexes is important for their folding,
oligomerization, post-translational modification, nuclear import, stability, assembly and …

Histone acetylation marks are written by histone acetyltransferases (HATs) and read by
bromodomains (BrDs), and less commonly by other protein modules. These proteins …

The many factors that control chromatin biology play key roles in essential nuclear functions
like transcription, DNA damage response and repair, recombination, and replication and are …

Methylation of histone H3 lysine 4 (H3K4me) is an evolutionarily conserved modification
whose role in the regulation of gene expression has been extensively studied. In contrast …

In Saccharomyces cerevisiae, histone H3 lysine 56 acetylation (H3K56ac) occurs in newly
synthesized histones that are deposited throughout the genome during DNA replication …

Protein kinases catalyze phosphorylation, a posttranslational modification widely utilized in
cell signaling. Histone acetyltransferases (HATs) catalyze a counterpart posttranslational …

Alteration of the acetylation state of histone proteins contributes to transcriptional regulation
and epigenetic inheritance. Dysregulation of these processes may lead to human diseases …

Rtt109 is a unique histone acetyltransferase acetylating histone H3 lysine 56 (H3K56), a
modification critical for DNA replication-coupled nucleosome assembly and genome …

Histone chaperones can be broadly defined as histone-binding proteins that influence
chromatin dynamics in an ATP-independent manner. Their existence reflects the importance …

Acetylation is a post-translational modification (PTM) that regulates chromatin dynamics and
function. Dysregulation of acetylation or acetyltransferase activity has been correlated with …