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 .
Part of the Myst Family, this histone modifier adds and removes a variety of chemical moieties to histone residues. Such modifications on a single or on several neighboring nucleosomes combine to produce a specific effect on the local chromatin structure.
You may include any references to papers as in: the use of JSmol in Proteopedia [2] or to the article describing Jmol [3] to the rescue.[4],[5]
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.
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.
Disease
HATs activate the residues of p53 by acetylation which leads to the elevation of p53 DNA binding or loss of its transcriptional activity. 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.
