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.
Disease
residues of p53 acetylated by HATs may be located in variable sites, which leads to elevation of p53 DNA binding or loss of its transcriptional activity. It has been demonstrated that mutation of the C-terminal site of p53, where acetylation occurs, prompts comprehensively the loss of p53-dependent cyclin-dependent kinase inhibitor p21 transcription [49,50]. Acetylation of signal mediators may be prominent in subsequent stages in cancer progression.
Relevance
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 zinc finger region of this structure is involved in the acetyltransferase activity and chromatin binding of the histone.
