In addition to its role as a classical transcription factor, N-myc may recruit histone acetyltransferases (HATs). This allows it to regulate global chromatin structure via histone acetylation.

The transcription factor MYC binds specific DNA sites in cellular chromatin and induces the acetylation of histones H3 and H4. However, the histone acetyltransferases (HATs) that are responsible for these modifications have not yet been identified. MYC associates with TRRAP, a subunit of distinct ma …

两种相互竞争的酶家族， 组蛋白赖氨酸乙酰转移酶 (HATs)和 组蛋白去乙酰化酶 (HDACs)，调节 组蛋白乙酰化。 在人类中有三个主要的HAT家族被充分研究，包括GNAT (HAT1, GCN5, PCAF)， MYST (Tip60, MOF,MOZ, MORF, HBO1)和p300/CBP。

Myc标签蛋白，是一个含11个氨基酸的小标签，标签序列Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu，这11个氨基酸作为抗原表位表达在不同的蛋白质框架中仍可识别其相应抗体。

2020年8月21日 · MYC recruits histone acetyl transferases (HATs) to hyperacetylate chromatin, in turn facilitating the binding of RNApolII. 18 We hypothesized that MYC-bound HDAC2, in addition to being a HAT antagonist, plays a role in maintaining the MYC-dependent transcriptional profile by regulating the expression of MYC/HDAC2 co-bound genes.

2003年7月1日 · Targeting histone deacetylases (HDAC) and histone acetyl transferases (HAT) with small molecular inhibitors such as SAHA, MS-275, EML-425, C646, among others, have proven to be effective in ...

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2005年10月14日 · Myc recruits histone acetyltransferases (HATs) to modify chromatin and is, itself, acetylated in mammalian cells by several of these HATs including p300/CBP, GCN5, and Tip60. The Myc residues that are directly modified by these different HATs remain unknown.

2021年3月5日 · Most notable MYC cofactors are members of nucleosome remodeling complexes that directly modify histone tails to mediate transcriptional activation, including histone acetyl transferases (HATs) and histone deacetylases (HDACs) or demethylases such as …

The recruitment of HATs by MYC/MAX complexes and HDACs by MXD/MAX complexes can be seen as a transcriptional switch that regulates the activity of canonical MYC target genes through histone acetylation, shifting an equilibrium by “opening” or “closing” the local chromatin structure, allowing or preventing RNA Pol II binding, respectively.