Asset Details
Do you wish to reserve the book?
Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation
Do you wish to request the book?
Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation
2017
Overview
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/45
/ 631/535
/ Assembly
/ DNA
/ Humanities and Social Sciences
/ Humans
/ Promoter Regions, Genetic - genetics
/ RNA
/ RNA Polymerase III - metabolism
/ Science
/ Sequence Homology, Amino Acid
/ TATA-Box Binding Protein - chemistry
/ TATA-Box Binding Protein - genetics
/ TATA-Box Binding Protein - metabolism
/ Transcription Factor TFIIIB - chemistry
/ Transcription Factor TFIIIB - genetics
