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Showing 1–5 of 5 results
Advanced filters: Author: Alexandra Stützer Clear advanced filters

  • Phosphorylation of residues in the N-terminal tail of histone H3 signals different biological outcomes. High-resolution NMR analyses now reveal a mechanistic hierarchy of H3 phosphorylation events, whereby phosphorylation of Ser10 impedes the phosphorylation of Thr6 and Thr11 by PKC and Chk1, respectively. Because both enzymes also target Ser10, this establishes an autoinhibitory feedback loop on H3 tails.

    • Stamatios Liokatis
    • Alexandra Stützer
    • Philipp Selenko
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 819-823

  • Cross-linking mass spectrometry (XLMS) allows mapping of protein-protein and protein-RNA interactions, but the analysis of protein-DNA complexes remains challenging. Here, the authors develop a UV light-based XLMS workflow to determine protein-DNA interfaces in reconstituted chromatin and isolated nuclei.

    • Alexandra Stützer
    • Luisa M. Welp
    • Henning Urlaub
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12

  • Harasimov, Gorry, Welp, Penir, Horokhovskyi et al. analyse proteostasis in mammalian oocytes and ovaries: the maintenance of oocytes involves exceptional protein longevity, and many of the extremely long-lived proteins decline as the ovary ages.

    • Katarina Harasimov
    • Rebecca L. Gorry
    • Melina Schuh
    ResearchOpen Access
    Nature Cell Biology
    Volume: 26, P: 1124-1138

  • The cryo-electron microscopy structure of the 16-subunit yeast SWI/SNF complex RSC in complex with a nucleosome substrate provides insights into the chromatin-remodelling function of this family of protein complexes.

    • Felix R. Wagner
    • Christian Dienemann
    • Patrick Cramer
    Research
    Nature
    Volume: 579, P: 448-451

  • Structural studies on the yeast transcription coactivator complex SAGA (Spt–Ada–Gcn5–acetyltransferase) provide insights into the mechanism of initiation of regulated transcription by this multiprotein complex, which is conserved among eukaryotes.

    • Haibo Wang
    • Christian Dienemann
    • Patrick Cramer
    Research
    Nature
    Volume: 577, P: 717-720