KAT2A

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KAT2A

A gene on chromosome 17q12-q21 that encodes a ubiquitously expressed histone acetyltransferase, which acts primarily as a transcriptional activator. KAT2A also downregulates NF-kappB by promoting ubiquitination of the NF-kappB subunit RELA in a HAT-independent manner. It is recruited by HIV-1’s viral Tat protein, regulates Tat's transactivating activity, and may help induce chromatin remodelling of proviral genes.
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The N-terminal domain of Myc forms complexes with transcriptional factors including TRRAP, GCN5 and TBP (Liu et al.
Metformin suppresses hepatic gluconeogenesis through induction of SIRT1 and GCN5.
We previously reported that a treatment with TPA activated HAT including p300 and GCN5, which contribute to the TPA-elicited expression of SOD3 in human leukemic THP-1 cells [29], suggesting that TPA-elicited Slug expression might be associated with the activation of HAT.
Ataxin-7 is a subunit of GCN5 histone acetyltransferase
Besides the target of the ELONGATOR complex, SHY2/IAA3 gene is also the target of Arabidopsis GCN5 histone acetyltransferase and since its auxin-induced expression is not affected in elo mutants, it was suggested that there is a complex chromatin-related control and specificity in target gene selection.
One of these ethanol-regulated HATs is called GCN5 (Choudhury et al.
El heterodimero Myc-Max unido al ADN, interacciona a traves de la region N-terminal de Myc con una variedad de proteinas involucradas en la transcripcion de multiples genes; entre estas proteinas se incluyen las TRRAP (por la sigla en ingles de transactivation-transformation domain-associated proteins), que se asocian con la histona acetilasa GCN5 (40).
Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo.
GCN5 was found to be present at each stage of embryo development.
His biology project, "The Expression of Arabidopsis HAT GCN5 in Yeast" attempts to use a chemical from plants that controls what chemicals are made by the plant in yeast.
It has been previously documented that E2F1 is able to recruit other histone acetyltransferases such as GCN5 to acetylate localized H3K9 residues (Guo et al.
The acetyltransferase GCN5 increases the PGC-1[alpha] acetylation, resulting in reduced PGC-1[alpha] activity [64].