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

被引：44

作者：

Gouge, Jerome ^{[1
]}

Guthertz, Nicolas ^{[1
]}

Kramm, Kevin ^{[2
]}

Dergai, Oleksandr ^{[3
]}

Abascal-Palacios, Guillermo ^{[1
]}

Satia, Karishma ^{[1
]}

Cousin, Pascal ^{[3
]}

Hernandez, Nouria ^{[3
]}

Grohmann, Dina ^{[2
]}

Vannini, Alessandro ^{[1
]}

机构：

[1] Inst Canc Res, London SW7 3RP, England

[2] Univ Regensburg, Dept Biochem Genet & Microbiol, Inst Microbiol, D-93053 Regensburg, Germany

[3] Univ Lausanne, Ctr Integrat Genom, Fac Biol & Med, CH-1015 Lausanne, Switzerland

来源：

NATURE COMMUNICATIONS | 2017年 / 8卷

基金：

英国惠康基金; 英国生物技术与生命科学研究理事会; 瑞士国家科学基金会;

关键词：

STRUCTURAL BASIS; CROSS-LINKING; SUBUNIT; COMPLEX; PROTEIN; ROLES; SITE; RECRUITMENT; RESOLUTION; PROMOTERS;

D O I：

10.1038/s41467-017-00126-1

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 angstrom 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.

引用

页数：11

共 46 条

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