What is Myst family?

Originally named for its four founding members in yeast and mammals, the family currently comprises five human HATs: Tip60, MOZ, MORF, HBO1 and MOF. Their defining feature is the presence of the highly conserved MYST domain composed of an acetyl-CoA binding motif and a zinc finger.

What is Myst domain?

The MYST (Moz, YBF2, Sas2p, Tip) protein family is defined by a highly conserved histone acet- yltransferase domain, the MYST domain, containing an atypical zinc finger. Five MYST proteins have been identified in mammals (Fig.

How many histone Acetyltransferases are there?

3 Histone acetyltransferases (HATs) Histone acetyltransferases (HATs) can be divided into five groups according to the structure and function of their catalytic domains. These are GNAT (GCN5-related N-acetyltransferase), MYST, p300/CBP, the general transcription factor HATs, and the nuclear hormone-related HATs.

Who discovered histone acetylation?

Vincent Allfrey
In pioneering research beginning in the early 1960s, Vincent Allfrey found that histones were modified by post-transla- tional acetylation and methylation, and he correlated these modifications with control of gene expression (Allfrey et al., 1964).

How does histone acetylation affect chromatin structure?

Histone acetylation may affect chromatin structure directly by altering DNA‐histone interactions within and between nucleosomes, thus resulting in a more open higher‐order chromatin structure.

Are histone Acetyltransferases coactivators?

The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell.

What do histone Acetyltransferases do?

Histone acetyltransferases (HATs) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl-CoA to form ε-N-acetyllysine. DNA is wrapped around histones, and, by transferring an acetyl group to the histones, genes can be turned on and off.

How does histone acetylation change chromatin structure?

Histone acetylation alters chromatin structure. Acetylation of histones alters accessibility of chromatin and allows DNA binding proteins to interact with exposed sites to activate gene transcription and downstream cellular functions.

What happens when histones acetylated?

Acetylation removes positive charges thereby reducing the affinity between histones and DNA. Thus, in most cases, histone acetylation enhances transcription while histone deacetylation represses transcription, but the reverse is seen as well (Reamon-Buettner and Borlak, 2007).

What are consequences of histone acetylation in gene expression?

How does histone acetylation affect chromatin?

How does acetylation change the conformation of chromatin?

Acetylation of lysyl residues of—NH2 terminal regions of histones leads to a decrease in their positive charge density. Since the interaction of histones with DNA is largely ionic in nature, this modification may well weaken histone-DNA interaction and alter the conformation of DNA-histone complexes.