Post-translational acetylation of lysine residues has emerged as a key regulatory
mechanism in all eukaryotic organisms. Originally discovered in 1963 as a unique …

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

Acetylation of histones by lysine acetyltransferases (KATs) is essential for chromatin
organization and function. Among the genes coding for the MYST family of KATs (KAT5 …

The histone acetyltransferase (HAT) p300/CBP is a transcriptional coactivator implicated in
many gene regulatory pathways and protein acetylation events. Although p300 inhibitors …

Histone modifying enzymes catalyze the addition or removal of an array of covalent
modifications in histone and non-histone proteins. Within the context of chromatin, these …

Histone modifications and more specifically ε-lysine acylations are key epigenetic regulators
that control chromatin structure and gene transcription, thereby impacting on various …

Reversible protein acetylation is controlled by the opposing actions of protein lysine
acetyltransferases and deacetylations. Recent developments on the structure and …

Human acetyltransferases MOZ and MORF are implicated in chromosomal translocations
associated with aggressive leukemias. Oncogenic translocations involve the far amino …

The monocytic leukemia zinc finger protein MOZ and the related factor MORF form
tetrameric complexes with ING5 (inhibitor of growth 5), EAF6 (Esa1-associated factor 6 …

Lysine lactylation (Kla) links metabolism and gene regulation and plays a key role in
multiple biological processes. However, the regulatory mechanism and functional …