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Recent insights into the structure of TFIID, its assembly, and its binding to core promoter.近期对 TFIID 结构、组装及其与核心启动子结合的深入了解。
Curr Opin Struct Biol. 2020 Apr;61:17-24. doi: 10.1016/j.sbi.2019.10.001. Epub 2019 Nov 18.
2
Structure of promoter-bound TFIID and model of human pre-initiation complex assembly.启动子结合型TFIID的结构与人预起始复合物组装模型
Nature. 2016 Mar 31;531(7596):604-9. doi: 10.1038/nature17394. Epub 2016 Mar 23.
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Cryo-EM reveals promoter DNA binding and conformational flexibility of the general transcription factor TFIID.冷冻电镜揭示了通用转录因子 TFIID 的启动子 DNA 结合和构象灵活性。
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Promoter Recognition: Putting TFIID on the Spot.启动子识别:将 TFIID 置于聚光灯下。
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本文引用的文献

1
TFIID Enables RNA Polymerase II Promoter-Proximal Pausing.TFIID 促进 RNA 聚合酶 II 启动子近端暂停。
Mol Cell. 2020 May 21;78(4):785-793.e8. doi: 10.1016/j.molcel.2020.03.008. Epub 2020 Mar 30.
2
Co-translational assembly of mammalian nuclear multisubunit complexes.哺乳动物核多亚基复合物的共翻译组装。
Nat Commun. 2019 Apr 15;10(1):1740. doi: 10.1038/s41467-019-09749-y.
3
Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly.伴侣蛋白 CCT 在基础转录因子 TFIID 组装中的检查点功能。
Nat Struct Mol Biol. 2018 Dec;25(12):1119-1127. doi: 10.1038/s41594-018-0156-z. Epub 2018 Dec 3.
4
Structure of human TFIID and mechanism of TBP loading onto promoter DNA.人源 TFIID 结构与 TBP 加载到启动子 DNA 的机制。
Science. 2018 Dec 21;362(6421). doi: 10.1126/science.aau8872. Epub 2018 Nov 15.
5
Molecular structure of promoter-bound yeast TFIID.启动子结合的酵母 TFIID 的分子结构。
Nat Commun. 2018 Nov 7;9(1):4666. doi: 10.1038/s41467-018-07096-y.
6
Zinc knuckle of TAF1 is a DNA binding module critical for TFIID promoter occupancy.TAF1 的锌指结构是一个 DNA 结合模块,对于 TFIID 启动子占据至关重要。
Sci Rep. 2018 Mar 15;8(1):4630. doi: 10.1038/s41598-018-22879-5.
7
Cryo-EM in the study of challenging systems: the human transcription pre-initiation complex.冷冻电镜在具有挑战性的系统研究中的应用:人类转录起始前复合物
Curr Opin Struct Biol. 2016 Oct;40:120-127. doi: 10.1016/j.sbi.2016.09.009. Epub 2016 Sep 30.
8
Structure of promoter-bound TFIID and model of human pre-initiation complex assembly.启动子结合型TFIID的结构与人预起始复合物组装模型
Nature. 2016 Mar 31;531(7596):604-9. doi: 10.1038/nature17394. Epub 2016 Mar 23.
9
Cryo-EM: A Unique Tool for the Visualization of Macromolecular Complexity.冷冻电镜:一种用于可视化大分子复杂性的独特工具。
Mol Cell. 2015 May 21;58(4):677-89. doi: 10.1016/j.molcel.2015.02.019.
10
Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules.细胞质TAF2-TAF8-TAF10复合物为从预先形成的子模块组装核全酶TFIID提供了证据。
Nat Commun. 2015 Jan 14;6:6011. doi: 10.1038/ncomms7011.

近期对 TFIID 结构、组装及其与核心启动子结合的深入了解。

Recent insights into the structure of TFIID, its assembly, and its binding to core promoter.

机构信息

Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA.

Molecular Biophysics and Integrative Bio-Imaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, CA 94720, USA.

出版信息

Curr Opin Struct Biol. 2020 Apr;61:17-24. doi: 10.1016/j.sbi.2019.10.001. Epub 2019 Nov 18.

DOI:10.1016/j.sbi.2019.10.001
PMID:31751889
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7156316/
Abstract

TFIID is a large multiprotein assembly that serves as a general transcription factor for transcription initiation by eukaryotic RNA polymerase II (Pol II). TFIID is involved in the recognition of the core promoter sequences and neighboring chromatin marks, and can interact with gene-specific activators and repressors. In order to obtain a better molecular and mechanistic understanding of the function of TFIID, its structure has been pursued for many years. However, the scarcity of TFIID and its highly flexible nature have made this pursuit very challenging. Recent breakthroughs, largely due to methodological advances in cryo-electron microscopy, have finally described the structure of this complex, both alone and engaged with core promoter DNA, revealing the functional significance of its conformational complexity in the process of core promoter recognition and initiation of Pol II transcription. Here, we review these recent structural insights and discuss their implications for our understanding of eukaryotic transcription initiation.

摘要

TFIID 是一个大型的多蛋白复合物,作为真核 RNA 聚合酶 II (Pol II) 转录起始的通用转录因子。TFIID 参与识别核心启动子序列和相邻的染色质标记,并可以与基因特异性激活剂和抑制剂相互作用。为了更好地了解 TFIID 的分子和机制功能,多年来一直致力于研究其结构。然而,TFIID 的稀缺性及其高度灵活的性质使得这一研究极具挑战性。最近的突破,主要得益于低温电子显微镜方法学的进步,终于描述了该复合物的结构,包括单独的和与核心启动子 DNA 结合的结构,揭示了其构象复杂性在核心启动子识别和 Pol II 转录起始过程中的功能意义。在这里,我们回顾这些最近的结构见解,并讨论它们对我们理解真核转录起始的意义。