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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Jerome Gouge & Nicolas Guthertz & Kevin Kramm & Oleksandr Dergai & Guillermo Abascal-Palacios & Karishma Satia & Pascal Cousin & Nouria Hernandez & Dina Grohmann & Alessandro Vannini, 2017. "Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation," Nature Communications, Nature, vol. 8(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00126-1
    DOI: 10.1038/s41467-017-00126-1
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    Cited by:

    1. Jianfeng Sun & Xue Li & Xuben Hou & Sujian Cao & Wenjin Cao & Ye Zhang & Jinyang Song & Manfu Wang & Hao Wang & Xiaodong Yan & Zengpeng Li & Robert G. Roeder & Wei Wang, 2022. "Structural basis of human SNAPc recognizing proximal sequence element of snRNA promoter," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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