The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder.
The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder.
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DOI：
10.1042/bst20220342
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发表时间：
2023-02-27
影响因子：
3.9
通讯作者：
中科院分区：
文献类型：
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作者：
选择性识别无序蛋白质的相互作用支架强烈地塑造了蛋白质相互作用。TFIIS N末端结构域(TND)是这种类型的有助于转录的重要支架。TND是一个五螺旋的束，没有已知的酶活性，而是选择性地阅读其他蛋白质内在无序的序列。在这里，我们综述了TND及其同源无序配体的结构和功能性质，这些配体被称为TND相互作用基序(TIM)。TND或TIMs存在于转录机制的重要成员中，包括TFIIS、超延伸复合体、SWI/SNF、Mediator、IWS1、SPT6、PP1-PNUTS磷酸酶、拉伸蛋白、H3K36me3阅读器、转录因子MYC等。我们还回顾了TND互动组如何对转录调控做出贡献。由于TND是转录延伸调节因子中最显著丰富的折叠，TND和TIM驱动的相互作用在许多转录过程的调控中具有广泛的作用。
Interaction scaffolds that selectively recognize disordered protein strongly shape protein interactomes. An important scaffold of this type that contributes to transcription is the TFIIS N-terminal domain (TND). The TND is a five-helical bundle that has no known enzymatic activity, but instead selectively reads intrinsically disordered sequences of other proteins. Here, we review the structural and functional properties of TNDs and their cognate disordered ligands known as TND-interacting motifs (TIMs). TNDs or TIMs are found in prominent members of the transcription machinery, including TFIIS, super elongation complex, SWI/SNF, Mediator, IWS1, SPT6, PP1-PNUTS phosphatase, elongin, H3K36me3 readers, the transcription factor MYC, and others. We also review how the TND interactome contributes to the regulation of transcription. Because the TND is the most significantly enriched fold among transcription elongation regulators, TND- and TIM-driven interactions have widespread roles in the regulation of many transcriptional processes.
DOI：
10.3390/pathogens11050583
发表时间：
2022-05-15
期刊：
Pathogens (Basel, Switzerland)
影响因子：
--
作者：
通讯作者：
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影响因子：
3.3
作者：
Schrijvers R;Vets S;De Rijck J;Malani N;Bushman FD;Debyser Z;Gijsbers R
通讯作者：
Gijsbers R