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Reading and Function of a Histone Code Involved in Targeting Corepressor Complexes for Repression

机译：涉及针对镇压器的复合物的组蛋白代码的阅读和功能

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A central question in histone code theory is how various codes are recognized and utilized in vivo. Here we show that TBL1 and TBLR1, two WD-40 repeat proteins in the corepressor SMRT/N-CoR complexes, are functionally redundant and essential for transcriptional repression by unliganded thyroid hormone receptors (TR) but not essential for transcriptional activation by liganded TR. TBL1 and TBLR1 bind preferentially to hypoacetylated histones H2B and H4 in vitro and have a critical role in targeting the corepressor complexes to chromatin in vivo. We show that targeting SMRT/N-CoR complexes to the deiodinase 1 gene (D1) requires at least two interactions, one between unliganded TR and SMRT/N-CoR and the other between TBL1/TBLR1 and hypoacetylated histones. Neither interaction alone is sufficient for the stable association of the corepressor complexes with the D1 promoter. Our data support a feed-forward working model in which deacetylation exerted by initial unstable recruitment of SMRT/N-CoR complexes via their interaction with unliganded TR generates a histone code that serves to stabilize their own recruitment. Similarly, we find that targeting of the Sin3 complex to pericentric heterochromatin may also follow this model. Our studies provide an in vivo example that a histone code is not read independently but is recognized in the context of other interactions.
机译：组蛋白密码理论的中心问题是如何在体内识别和利用各种密码。在这里，我们显示TBL1和TBLR1，这两个WD-40重复蛋白是在心脏紧迫剂SMRT / N-CoR复合物中，在功能上是多余的，对于未配体的甲状腺激素受体（TR）的转录抑制是必不可少的，但对于配体TR的转录激活不是必需的。 TBL1和TBLR1在体外优先与低乙酰化的组蛋白H2B和H4结合，并且在体内将共表达复合物靶向染色质中起关键作用。我们显示，靶向SMRT / N-CoR复合物至脱碘酶1基因（D1）需要至少两个相互作用，一个在未配体的TR和SMRT / N-CoR之间，另一个在TBL1 / TBLR1和低乙酰化的组蛋白之间。单独的两种相互作用都不足以使corepressor复合物与D1启动子稳定结合。我们的数据支持前馈工作模型，其中SMRT / N-CoR复合物通过与未配体TR的相互作用最初不稳定募集而产生的脱乙酰基作用产生了组蛋白代码，该组蛋白代码有助于稳定其自身募集。类似地，我们发现将Sin3复合物靶向于外周中心异染色质也可能遵循该模型。我们的研究提供了一个体内的例子，组蛋白密码不是独立阅读的，而是在其他相互作用的背景下被识别的。

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