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Showing 1–13 of 13 results
Advanced filters: Author: Lucas Farnung Clear advanced filters

  • In this study, the authors present the cryogenic electron microscopy reconstruction of the Rpd3S complex engaged with a nucleosome. The corresponding model describes the interactions that facilitate histone deacetylation within gene bodies by the Rpd3S complex.

    • Jonathan W. Markert
    • Seychelle M. Vos
    • Lucas Farnung
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-11

  • Eukaryotic transcription requires passage of RNA polymerase II (Pol II) through chromatin, which is impaired by nucleosomes. Here the authors report the cryo-EM structure of transcribing Pol II engaged with a downstream nucleosome core particle at an overall resolution of 4.4 Å, providing insights into the mechanism of chromatin transcription.

    • Lucas Farnung
    • Seychelle M. Vos
    • Patrick Cramer
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-6

  • The cryo-electron microscopy structure of a paused transcription elongation complex of RNA polymerase II bound to DRB sensitivity-inducing factor and negative elongation factor is reported at 3.2 Å resolution.

    • Seychelle M. Vos
    • Lucas Farnung
    • Patrick Cramer
    Research
    Nature
    Volume: 560, P: 601-606

  • A cryo-electron microscopy structure of the RNA-dependent RNA polymerase of SARS-CoV-2 sheds light on coronavirus replication and enables the analysis of the inhibitory mechanisms of candidate antiviral drugs.

    • Hauke S. Hillen
    • Goran Kokic
    • Patrick Cramer
    Research
    Nature
    Volume: 584, P: 154-156

  • Remdesivir is a nucleoside analog that inhibits the SARS-CoV-2 RNA dependent RNA polymerase (RdRp) and is used as a drug to treat COVID19 patients. Here, the authors provide insights into the mechanism of remdesivir-induced RdRp stalling by determining the cryo-EM structures of SARS-CoV-2 RdRp with bound RNA molecules that contain remdesivir at defined positions and observe that addition of the fourth nucleotide following remdesivir incorporation into the RNA product is impaired by a barrier to further RNA translocation.

    • Goran Kokic
    • Hauke S. Hillen
    • Patrick Cramer
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-7

  • Structural and functional analyses of RNA polymerase II−nucleosome complexes reveal how the chromatin remodeler Chd1 and the histone chaperone FACT mediate Pol II transcription through a nucleosome.

    • Lucas Farnung
    • Moritz Ochmann
    • Patrick Cramer
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 28, P: 382-387

  • Although chromatin remodelers have been shown to align nucleosome arrays to barriers and to generate spacing regularity among nucleosomes within arrays, it has remained unclear how the distance to barrier and the spacing length are determined in absolute terms. Here, the authors reveal that remodelers contain a ‘ruler’ element that sets remodeler-specific alignment and spacing distances when generating nucleosome arrays.

    • Elisa Oberbeckmann
    • Vanessa Niebauer
    • Philipp Korber
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-17

  • The cryo-electron microscopy structure of an activated transcription elongation complex of RNA polymerase II bound to DRB sensitivity-inducing factor and the elongation factors PAF1 complex and SPT6 is reported at 3.1 Å resolution.

    • Seychelle M. Vos
    • Lucas Farnung
    • Patrick Cramer
    Research
    Nature
    Volume: 560, P: 607-612

  • Cyclin-dependent kinase 12 (Cdk12) phosphorylates the C-terminal domain (CTD) of RNA polymerase II to regulate transcription. Here, the authors solve the crystal structure of the Cdk12 kinase domain and show that Cdk12 has its highest activity on a CTD substrate that carries a serine 7 phosphorylation.

    • Christian A. Bösken
    • Lucas Farnung
    • Matthias Geyer
    ResearchOpen Access
    Nature Communications
    Volume: 5, P: 1-14