Structural insights into the interaction between transcription factors and the nucleosome
Structural insights into the interaction between transcription factors and the nucleosome
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转录因子与核小体之间相互作用的结构见解
DOI：
10.1016/j.sbi.2021.06.016
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发表时间：
2021
影响因子：
6.8
通讯作者：
Morgunova E
中科院分区：
文献类型：
--
作者：
Morgunova E
在真核细胞中，DNA与两种主要类型的结合蛋白相互作用：转录因子和组蛋白。组蛋白形成核小体的核心，并且由于不同DNA序列的可弯曲性的差异而显示弱序列偏好性。相比之下，转录因子的亲和力高度依赖于DNA序列-所有序列都以中等亲和力结合，但只有少数特定序列通过DNA碱基的分子识别更紧密地结合。转录因子可以通过识别核小体相关DNA直接与核小体相互作用，也可以通过招募组蛋白修饰酶和核小体重塑剂间接与核小体相互作用。这些相互作用导致开放和闭合染色质模式的序列依赖性形成，其中特定位置被转录因子、组蛋白修饰酶和修饰的组蛋白占据。然后，这些模式被大的DNA相关的大分子复合物识别，如粘附素和RNA聚合酶II，它们分别参与调节高阶染色质结构和转录。在这里，我们回顾了最近的工作，提供了结构和机制的见解，所有这些类的DNA相关蛋白之间的相互作用。
In eukaryotic cells, DNA interacts with two main types of binding proteins: transcription factors and histones. Histones form the core of nucleosomes and display weak sequence preference owing to differences in bendability of different DNA sequences. By contrast, the affinity of transcription factors is highly dependent on DNA sequence — all sequences are bound with moderate affinity, but only few specific sequences are bound more tightly via molecular recognition of the DNA bases. Transcription factors can interact with nucleosomes directly by recognizing nucleosome-associated DNA and also indirectly by recruiting histone-modifying enzymes and nucleosome remodelers. These interactions result in sequence-dependent formation of a pattern of open and closed chromatin, where specific positions are occupied by transcription factors, histone-modifying enzymes, and modified histones. These patterns are then recognized by large DNA-associated macromolecular complexes such as cohesin and RNA polymerase II, which are involved in regulation of higher-order chromatin structure and transcription, respectively. Here, we review recent work that has provided structural and mechanistic insight into the interactions between all these classes of DNA-associated proteins.