DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability

Kevin Kramm, Tim Schröder, Jerome Gouge, Andrés Manuel Vera, Kapil Gupta, Florian B. Heiss, Tim Liedl, Christoph Engel, Imre Berger, Alessandro Vannini, Philip Tinnefeld and Dina Grohmann ()
Additional contact information
Kevin Kramm: University of Regensburg
Tim Schröder: Ludwig-Maximilians-Universität München
Jerome Gouge: The Institute of Cancer Research
Andrés Manuel Vera: Ludwig-Maximilians-Universität München
Kapil Gupta: University of Bristol
Florian B. Heiss: University of Regensburg
Tim Liedl: Ludwig-Maximilians-Universität München
Christoph Engel: University of Regensburg
Imre Berger: University of Bristol
Alessandro Vannini: The Institute of Cancer Research
Philip Tinnefeld: Ludwig-Maximilians-Universität München
Dina Grohmann: University of Regensburg

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: Abstract The TATA-binding protein (TBP) and a transcription factor (TF) IIB-like factor are important constituents of all eukaryotic initiation complexes. The reason for the emergence and strict requirement of the additional initiation factor Bdp1 in the RNA polymerase (RNAP) III system, however, remained elusive. A poorly studied aspect in this context is the effect of DNA strain arising from DNA compaction and transcriptional activity on initiation complex formation. We made use of a DNA origami-based force clamp to follow the assembly of human initiation complexes in the RNAP II and RNAP III systems at the single-molecule level under piconewton forces. We demonstrate that TBP-DNA complexes are force-sensitive and TFIIB is sufficient to stabilise TBP on a strained promoter. In contrast, Bdp1 is the pivotal component that ensures stable anchoring of initiation factors, and thus the polymerase itself, in the RNAP III system. Thereby, we offer an explanation for the crucial role of Bdp1 for the high transcriptional output of RNAP III.

Date: 2020
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-020-16702-x 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:11:y:2020:i:1:d:10.1038_s41467-020-16702-x

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

DOI: 10.1038/s41467-020-16702-x

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 ().