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Your search keyword '"Dina, Grohmann"' showing total 5 results
Start Over Author "Dina, Grohmann" Journal nature communications
5 results on '"Dina, Grohmann"'

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

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, and Dina Grohmann

Subjects
Science
Abstract

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.

Published
2020
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3. Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase III transcription initiation

Author

Jerome Gouge, Nicolas Guthertz, Kevin Kramm, Oleksandr Dergai, Guillermo Abascal-Palacios, Karishma Satia, Pascal Cousin, Nouria Hernandez, Dina Grohmann, and Alessandro Vannini

Subjects
Science
Abstract

Transcription initiation by RNA polymerase III requires TFIIIB, a complex formed by Brf1/Brf2, TBP and Bdp1. Here, the authors describe the crystal structure of a Brf2-TBP-Bdp1 complex bound to a DNA promoter and characterize the role of Bdp1 in TFIIIB assembly and pre-initiation complex formation.

Published
2017
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4. Repression of RNA polymerase by the archaeo-viral regulator ORF145/RIP

Author

Carol Sheppard, Fabian Blombach, Adam Belsom, Sarah Schulz, Tina Daviter, Katherine Smollett, Emilie Mahieu, Susanne Erdmann, Philip Tinnefeld, Roger Garrett, Dina Grohmann, Juri Rappsilber, and Finn Werner

Subjects
Science
Abstract

How archaeal viruses perturb host transcription machinery is poorly understood. Here, the authors provide evidence that the archaeo-viral transcription factor ORF145/RIP targets host RNA polymerase, repressing its activity.

Published
2016
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5. Complete architecture of the archaeal RNA polymerase open complex from single-molecule FRET and NPS

Author

Dina Grohmann, Julia Nagy, Sarah Schulz, Alan C. M. Cheung, Katherine Smollett, Jens Michaelis, and Finn Werner

Subjects
Archaeal Proteins, General Physics and Astronomy, RNA polymerase II, RNA, Archaeal, Article, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, RNA polymerase, RNA polymerase II holoenzyme, 030304 developmental biology, 0303 health sciences, Multidisciplinary, biology, General transcription factor, DNA-Directed RNA Polymerases, General Chemistry, Molecular biology, enzymes and coenzymes (carbohydrates), DNA, Archaeal, chemistry, Biophysics, biology.protein, Transcription factor II E, Transcription factor II D, Transcription factor II B, 030217 neurology & neurosurgery, Transcription factor II A
Abstract

The molecular architecture of RNAPII-like transcription initiation complexes has been studied for years but its structure has remained opaque due to its conformational flexibility and size. We determined the three-dimensional architecture of the complete open complex (OC) composed of the promoter DNA, TATA box-binding protein (TBP), transcription factors TFB and TFE, and the 12-subunit RNA polymerase (RNAP) from M. jannaschii. By combining single-molecule Förster resonance energy transfer (smFRET) and the Bayesian parameter estimation based Nano-Positioning System (NPS) analysis, we modelled the entire archaeal OC, which elucidates the path of the ntDNA strand and interaction sites of the transcription factors with the RNAP. Compared to models of the eukaryotic OC, the position of the TATA DNA region with TBP and TFB is positioned closer to the surface of the RNAP, likely providing the mechanism by which DNA melting can occur in a minimal factor configuration, without the dedicated translocase/helicase encoding factor TFIIH.

Published
2015
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