MYST Histone Acetyltransferases (HAT), a diverse family of proteins responsible for a variety of functions in eukaryotes from yeast to humans[1]. These particular histone acetyltransferases are part of the MYST family because of their structure which includes and .
Function
Highly conserved in eukaryotes, their key roles in post-translation modification of histones. Profound effect on chromatin structure in eukaryotes. Composed of an Acetyl-CoA binding motif and a zinc finger. The enzyme looks for lysine residues which are the universal target for acetylation, and by the addition of an acetyl group stablilizes the electrons of a histone making them less positively charged.
Relevance
These enzymes acetylate lysine amino acids of histone by transferring the acetyl group of acetyl CoA to form N-acetyllysine. While the DNA coiled around histones and the activity of histone acetyltransferase is able to turn genes on or off, along with influencing gene expression by acetylating non-histone proteins[2].
Disease
HATs activate the residues of p53 by acetylation which leads to the elevation of p53 DNA binding or loss of its transcriptional activity[3]. If there’s any type of mutation where acetylation occurs of the p53 residues the functionality is hindered leading to the growth of tumors/cancers.
Structural highlights
The binding site for this structure , which is involved in the transfer of an acetyl group from acetyl-CoA to the amine group of a lysine residue. The finger region of this structure is involved in the acetyltransferase activity and chromatin binding of the histone. The residues are needed for catalyzing specific acetylation.
