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

Jerome Gouge, Nicolas Guthertz, Kevin Kramm, Oleksandr Dergai, Guillermo Abascal-Palacios, Karishma Satia, Pascal Cousin, Nouria Hernandez, Dina Grohmann and Alessandro Vannini ()
Additional contact information
Jerome Gouge: The Institute of Cancer Research
Nicolas Guthertz: The Institute of Cancer Research
Kevin Kramm: University of Regensburg
Oleksandr Dergai: University of Lausanne
Guillermo Abascal-Palacios: The Institute of Cancer Research
Karishma Satia: The Institute of Cancer Research
Pascal Cousin: University of Lausanne
Nouria Hernandez: University of Lausanne
Dina Grohmann: University of Regensburg
Alessandro Vannini: The Institute of Cancer Research

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract 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.

Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-017-00126-1 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00126-1

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-00126-1

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().