Author
Listed:
- Yashar Sadian
(Structural and Computational Biology Unit
University of Geneva)
- Florence Baudin
(Structural and Computational Biology Unit)
- Lucas Tafur
(Structural and Computational Biology Unit
Faculty of Biosciences
University of Geneva Sciences III)
- Brice Murciano
(Structural and Computational Biology Unit)
- Rene Wetzel
(Structural and Computational Biology Unit)
- Felix Weis
(Structural and Computational Biology Unit)
- Christoph W. Müller
(Structural and Computational Biology Unit)
Abstract
RNA polymerase I (Pol I) assembles with core factor (CF) and Rrn3 on the rDNA core promoter for transcription initiation. Here, we report cryo-EM structures of closed, intermediate and open Pol I initiation complexes from 2.7 to 3.7 Å resolution to visualize Pol I promoter melting and to structurally and biochemically characterize the recognition mechanism of Pol I promoter DNA. In the closed complex, double-stranded DNA runs outside the DNA-binding cleft. Rotation of CF and upstream DNA with respect to Pol I and Rrn3 results in the spontaneous loading and opening of the promoter followed by cleft closure and positioning of the Pol I A49 tandem winged helix domain (tWH) onto DNA. Conformational rearrangement of A49 tWH leads to a clash with Rrn3 to initiate complex disassembly and promoter escape. Comprehensive insight into the Pol I transcription initiation cycle allows comparisons with promoter opening by Pol II and Pol III.
Suggested Citation
Yashar Sadian & Florence Baudin & Lucas Tafur & Brice Murciano & Rene Wetzel & Felix Weis & Christoph W. Müller, 2019.
"Molecular insight into RNA polymerase I promoter recognition and promoter melting,"
Nature Communications, Nature, vol. 10(1), pages 1-13, December.
Handle:
RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13510-w
DOI: 10.1038/s41467-019-13510-w
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