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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Auteurs principaux:	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
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2020
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/6c52a4bb73744eafa2b7a2b2daca7321
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spelling	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)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	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
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DNA origami-based single-molecule force spectroscopy elucidates RNA Polymerase III pre-initiation complex stability

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