Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation.

Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation.
复制标题

DOI:
10.1038/s41467-017-00126-1
复制
发表时间:
2017-07-25
影响因子:
16.6
通讯作者:
Vannini A
Vannini A
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Gouge J;Guthertz N;Kramm K;Dergai O;Abascal-Palacios G;Satia K;Cousin P;Hernandez N;Grohmann D;Vannini A

文献摘要

参考文献

被引文献

相似文献

通过RNA聚合酶(Pol)III启动基因转录需要TFIIIB的活性,TFIIIB是由Brf 1(或Brf 2)、TBP(TATA结合蛋白)和Bdp 1形成的复合物。TFIIIB是募集Pol III所必需的,并促进从封闭的Pol III前起始复合物过渡到开放的Pol III前起始复合物,这是一个依赖于Bdp 1亚基活性的过程。在这里,我们提出了一个晶体结构的Brf 2-TBP-Bdp 1复合物结合到DNA在2.7 μ m的分辨率,集成了单分子FRET分析和体外生化测定。我们的研究提供了Bdp 1如何组装成TFIIIB复合物的结构见解,揭示了Bdp 1和Pol II因子TFIIA和TFIIF之间的结构和功能相似性,并揭示了与DNA和上游因子SNAPc的重要相互作用。此外,我们的数据支持的想法,一个协调的机制,涉及TFIIIB和RNA聚合酶III亚基的封闭到开放的起始前复杂的过渡。RNA聚合酶III的转录起始需要TFIIIB,这是一种由Brf 1/Brf 2、TBP和Bdp 1形成的复合物。在这里,作者描述了与DNA启动子结合的Brf 2-TBP-Bdp 1复合物的晶体结构,并表征了Bdp 1在TFIIIB组装和预起始复合物形成中的作用。
Initiation of gene transcription by RNA polymerase (Pol) III requires the activity of TFIIIB, a complex formed by Brf1 (or Brf2), TBP (TATA-binding protein), and Bdp1. TFIIIB is required for recruitment of Pol III and to promote the transition from a closed to an open Pol III pre-initiation complex, a process dependent on the activity of the Bdp1 subunit. Here, we present a crystal structure of a Brf2–TBP–Bdp1 complex bound to DNA at 2.7 Å resolution, integrated with single-molecule FRET analysis and in vitro biochemical assays. Our study provides a structural insight on how Bdp1 is assembled into TFIIIB complexes, reveals structural and functional similarities between Bdp1 and Pol II factors TFIIA and TFIIF, and unravels essential interactions with DNA and with the upstream factor SNAPc. Furthermore, our data support the idea of a concerted mechanism involving TFIIIB and RNA polymerase III subunits for the closed to open pre-initiation complex transition. Transcription initiation by RNA polymerase III requires TFIIIB, a complex formed by Brf1/Brf2, TBP and Bdp1. Here, the authors describe the crystal structure of a Brf2-TBP-Bdp1 complex bound to a DNA promoter and characterize the role of Bdp1 in TFIIIB assembly and pre-initiation complex formation.
DOI: 10.1016/j.cell.2011.10.041
发表时间: 2011-12-09
期刊: Cell
影响因子: 64.5
作者:
Feklistov A;Darst SA
通讯作者: Darst SA
DOI: 10.1261/rna.055426.115
发表时间: 2016-03
期刊: RNA (New York, N.Y.)
影响因子: --
作者:
Jakob L;Treiber T;Treiber N;Gust A;Kramm K;Hansen K;Stotz M;Wankerl L;Herzog F;Hannus S;Grohmann D;Meister G
通讯作者: Meister G
DOI: 10.1093/nar/gku273
发表时间: 2014-06
影响因子: 14.9
作者:
Gietl A;Holzmeister P;Blombach F;Schulz S;von Voithenberg LV;Lamb DC;Werner F;Tinnefeld P;Grohmann D
通讯作者: Grohmann D
DOI: 10.1107/s0907444904016427
发表时间: 2004-12-01
影响因子: 2.2
作者:
Blanc, E;Roversi, P;Bricogne, G
通讯作者: Bricogne, G
DOI: 10.1073/pnas.0507653102
发表时间: 2005-10-25
影响因子: 11.1
作者:
Kassavetis, GA;Soragni, E;Geiduschek, EP
通讯作者: Geiduschek, EP