Gouge, Jerome and Guthertz, Nicolas and Kramm, Kevin and Dergai, Oleksandr and Abascal-Palacios, Guillermo and Satia, Karishma and Cousin, Pascal and Hernandez, Nouria and Grohmann, Dina and Vannini, Alessandro (2017) Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation. NATURE COMMUNICATIONS, 8: 130. ISSN 2041-1723,
Full text not available from this repository. (Request a copy)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 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | STRUCTURAL BASIS; CROSS-LINKING; SUBUNIT; COMPLEX; PROTEIN; ROLES; SITE; RECRUITMENT; RESOLUTION; PROMOTERS; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie > Prof. Dr. Dina Grohmann |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Dec 2018 13:16 |
| Last Modified: | 25 Feb 2019 13:23 |
| URI: | https://pred.uni-regensburg.de/id/eprint/1525 |
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