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Histone Acetyltransferases (HATs; also known as Lysine Aceyltransferases or KATs) are domains found in a diverse range of enzymes, which catalyze the acetylation of lysine residues. This post-translational modification involves the transfer of an acetyl group from acetyl CoA to form ε-N-acetyl lysine. The reverse reaction is carried out by histone deacetylases (HDACs).
|Cat. No.||Product Name / Activity|
|Potent and selective p300/CBP inhibitor; orally bioavailable|
|Noncompetitive PCAF/p300 inhibitor|
|Selective p300/CBP inhibitor|
|Reversible and non-competitive CBP/p300 inhibitor|
|Potent p300/CBP inhibitor|
|Dual CBP/p300 and BRD4 bromodomain inhibitor|
|Selective p300 inhibitor|
|Inhibitor of KAT5 (Tip60)|
|Steroid receptor coactivator 3 (SRC-3) inhibitor|
|High affinity KAT6A (MOZ) competitive inhibitor|
|Cat. No.||Product Name / Activity|
|Selective CBP/p300 BRD inhibitor|
|Potent CBP/p300 BRD inhibitor|
Histone Acetyltransferases (HATs; also known as Lysine Aceyltransferases or KATs) are catalytic domains found in a diverse range of proteins; there are 37 endogenous mammalian proteins that are thought to have HAT activity. HAT domains can be found in proteins alongside other epigenetic domains, such as bromodomains, which recognize acetylated lysine residues. Proteins with HAT activity are found in multiprotein complexes, the components of which regulate HAT specificity and integration with other proteins, as well as enabling the detection of post-translational modifications.
HATs are grouped into families based on their amino acid sequence homology:
The function of HATs is to catalyze the acetylation of lysine residues in proteins, by the transfer of an acetyl group from acetyl CoA to form ε-N-acetyl lysine. The reverse process, removal of acetylation marks, is catalyzed by histone deacetylases (HDACs; also known as lysine deacetylases or KDACs). Over 2000 actylation targets have been identified including proteins from most subcellular compartments and organelles. Acetylation of lysine residues can affect the cellular localization and catalytic activity of a protein, as well as its ability to interact with other proteins. This post-translation modification governs the ability of proteins to respond to intracellular and extracellular processes.
HATs act on gene regulatory elements of transcriptionally-active genes, such as promoter and enhancer regions, to modulate transcriptional output. For example, MOF and GNC5 localize to promoter regions of their targets, and their identification correlates with increased transcriptional activity. Similarly, p300 and CBP activate transcription via their recruitment by transcription factors, to enhancer and promoter regions. p53 recruits p300 and CBP to its target loci in response to DNA damage, where they mediate the acetylation of histone 3 lysine 18 (H3K18) and H3K27, stimulating RNA polymerase II to leave the promotor and activate transcriptional elongation.
A key function of HATs is the acetylation of lysine residues on histone protein tails, which is an important epigenetic regulator of chromatin architecture and gene transcription. Acetylation of histone lysine residues, such as H4K16ac, can disrupt interactions between neighbouring nucleosomes, and between histones and DNA. These changes create an environment that is more conducive to transcription. Some histone acetylation marks are also associated with increased release of RNA polymerase, while other acetylation marks affect the recruitment of bromodomain containing proteins.
Tocris offers the following scientific literature for Histone Acetyltransferases to showcase our products. We invite you to request* your copy today!
*Please note that Tocris will only send literature to established scientific business / institute addresses.
Written by Susanne Müller-Knapp and Peter J. Brown, this review gives an overview of the development of chemical probes for epigenetic targets, as well as the impact of these tool compounds being made available to the scientific community. In addition, their biological effects are also discussed. Epigenetic compounds available from Tocris are listed.
Produced by Tocris and updated in 2014, the epigenetics research bulletin gives an introduction into mechanisms of epigenetic regulation, and highlights key Tocris products for epigenetics targets including:
|Gene||Species||Gene Symbol||Gene Accession No.||Protein Accession No.|
|Histone acetyltransferase 1||Human||HAT1||NM_003642||O14929|
|K(lysine) acetyltransferase 2A||Human||KAT2A||NM_021078||Q92830|
|K(lysine) acetyltransferase 2B||Human||KAT2B||NM_003884||Q92831|
|K(lysine) acetyltransferase 5||Human||KAT5||NM_006388||Q92993|
|K(lysine) acetyltransferase 6A||Human||KAT6A||NM_006766||Q92794|
|K(lysine) acetyltransferase 6B||Human||KAT6B||NM_012330||Q8WYB5|
|K(lysine) acetyltransferase 7||Human||KAT7||NM_007067||Q95251|
|K(lysine) acetyltransferase 8||Human||KAT8||NM_032188||Q9H7Z6|
|Clock homolog (mouse)||Human||CLOCK||NM_004898||O15516|
|CREB binding protein||Human||CREBBP||NM_004380||Q92793|
|E1A binding protein p300||Human||EP300||NM_001429||Q09472|
|General transcription factor IIIC, polypeptide 4, 90kDa||Human||GTF3C4||NM_012204||Q9UKN8|
|Nuclear receptor coactivator 1||Human||NCOA1||NM_147223||Q15788|
|Nuclear receptor coactivator 2||Human||NCOA2||NM_006540||Q15596|
|Nuclear receptor coactivator 3||Human||NCOA3||NM_006534||Q9Y6Q9|
|Retinoblastoma binding protein 7||Human||RBBP7||NM_002893||Q16576|
|TAF1 RNA polymerase II, TAT box binding protein (TBP)-associated factor, 250kDa||Human||TAF1||NM_004606||P21675|