DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability
TATA-binding protein (TBP) and a transcription factor (TF) IIB-like factor are important constituents of all eukaryotic initiation complexes. Here, the authors use a DNA origami-based force clamp to investigate the assembly dynamics of human initiation complexes in the RNAP II and RNAP III systems a...
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Nature Portfolio
2020
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oai:doaj.org-article:6c52a4bb73744eafa2b7a2b2daca73212021-12-02T15:02:55ZDNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability10.1038/s41467-020-16702-x2041-1723https://doaj.org/article/6c52a4bb73744eafa2b7a2b2daca73212020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16702-xhttps://doaj.org/toc/2041-1723TATA-binding protein (TBP) and a transcription factor (TF) IIB-like factor are important constituents of all eukaryotic initiation complexes. Here, the authors use a DNA origami-based force clamp to investigate the assembly dynamics of human initiation complexes in the RNAP II and RNAP III systems at the single-molecule level under pico newton forces.Kevin KrammTim SchröderJerome GougeAndrés Manuel VeraKapil GuptaFlorian B. HeissTim LiedlChristoph EngelImre BergerAlessandro VanniniPhilip TinnefeldDina GrohmannNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020) |
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Science Q Kevin Kramm Tim Schröder Jerome Gouge Andrés Manuel Vera Kapil Gupta Florian B. Heiss Tim Liedl Christoph Engel Imre Berger Alessandro Vannini Philip Tinnefeld Dina Grohmann DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability |
description |
TATA-binding protein (TBP) and a transcription factor (TF) IIB-like factor are important constituents of all eukaryotic initiation complexes. Here, the authors use a DNA origami-based force clamp to investigate the assembly dynamics of human initiation complexes in the RNAP II and RNAP III systems at the single-molecule level under pico newton forces. |
format |
article |
author |
Kevin Kramm Tim Schröder Jerome Gouge Andrés Manuel Vera Kapil Gupta Florian B. Heiss Tim Liedl Christoph Engel Imre Berger Alessandro Vannini Philip Tinnefeld Dina Grohmann |
author_facet |
Kevin Kramm Tim Schröder Jerome Gouge Andrés Manuel Vera Kapil Gupta Florian B. Heiss Tim Liedl Christoph Engel Imre Berger Alessandro Vannini Philip Tinnefeld Dina Grohmann |
author_sort |
Kevin Kramm |
title |
DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability |
title_short |
DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability |
title_full |
DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability |
title_fullStr |
DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability |
title_full_unstemmed |
DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability |
title_sort |
dna origami-based single-molecule force spectroscopy elucidates rna polymerase iii pre-initiation complex stability |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/6c52a4bb73744eafa2b7a2b2daca7321 |
work_keys_str_mv |
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