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Showing 1–10 of 10 results
Advanced filters: Author: Michael Uckelmann Clear advanced filters

  • A protein complex called the rixosome helps to degrade RNA transcripts that linger after gene expression ceases. This discovery points to distinct roles for the rixosome in regulating chromatin in different species.

    • Michael Uckelmann
    • Chen Davidovich
    News & Views
    Nature
    Volume: 604, P: 41-42

  • Ubiquitination of histone H2A can occur on distinct lysine residues, but how each site is recognised by the specific E3 ligase remains poorly understood. Here the authors demonstrate that the E3 ligase RNF168 binds the acidic patch on the nucleosome surface, directing the E2 to the target lysine K13/K15.

    • Velten Horn
    • Michael Uckelmann
    • Hugo van Ingen
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12

  • The E3 ubiquitin ligase RNF168 ubiquitinates specific lysines on histone H2A as part of the DNA damage response. Here, the authors show that the acidic patch on the histone H2A/H2B dimer catalyses RNF168-dependent ubiquitination of histone 2A by redirecting ubiquitination activity towards the relevant target lysines.

    • Francesca Mattiroli
    • Michael Uckelmann
    • Titia K. Sixma
    ResearchOpen Access
    Nature Communications
    Volume: 5, P: 1-11

  • Here the authors show that a gene-inactivating protein complex packs inactive genes into a dynamic and accessible structure. The study challenges the traditional views that restricted accessibility and low dynamics cause gene repression.

    • Michael Uckelmann
    • Vita Levina
    • Chen Davidovich
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 520-530

  • BRCA1 ligase activity is tightly regulated to maintain genome stability and confer DNA double strand repair. Here the authors identify USP48 as a H2A deubiquitinating enzyme that acts as a BRCA1 E3 ligase antagonist and characterize its role during DNA repair.

    • Michael Uckelmann
    • Ruth M. Densham
    • Joanna R. Morris
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-16

  • The polycomb repressive complex 2 (PRC2) is a histone methyltransferase regulating cell differentiation and identity. Here, the authors show that the vertebrate-specific PRC2 accessory subunit PALI1 facilitates substrate binding by the complex and elucidate the allosteric mechanism of PALI1- mediated PRC2 activation.

    • Qi Zhang
    • Samuel C. Agius
    • Chen Davidovich
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-18