H3K27ac

[1] The regulation of transcription factors, effector proteins, molecular chaperones, and cytoskeletal proteins by acetylation and deacetylation is a significant post-translational regulatory mechanism[2] These regulatory mechanisms are analogous to phosphorylation and dephosphorylation by the action of kinases and phosphatases.

Not only can the acetylation state of a protein modify its activity, but there has been a recent suggestion that this post-translational modification may also crosstalk with phosphorylation, methylation, ubiquitination, sumoylation, and others for dynamic control of cellular signaling.

[3][4][5] In the field of epigenetics, histone acetylation (and deacetylation) have been shown to be important mechanisms in the regulation of gene transcription.

[9] The current understanding and interpretation of histones comes from two large scale projects: ENCODE and the Epigenomic roadmap.

This led to chromatin states which define genomic regions by grouping the interactions of different proteins or histone modifications together.

Chromatin states were investigated in Drosophila cells by looking at the binding location of proteins in the genome.

[12] A look in to the data obtained led to the definition of chromatin states based on histone modifications.

H3K27ac is enriched in the regulatory regions of genes implicated in Alzheimer's disease, including those in tau and amyloid neuropathology.

It results in good optimization and is used in vivo to reveal DNA-protein binding occurring in cells.

Micrococcal Nuclease sequencing (MNase-seq) is used to investigate regions that are bound by well-positioned nucleosomes.

Lysine acetylation