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Showing 1–4 of 4 results
Advanced filters: Author: Felix Mueller-Planitz Clear advanced filters

  • Chromatin condensation does not impede nucleosome sliding by ISWI remodelers. Notably, ATP energy is used not only for remodeling but also for enzyme mobility and to prevent solidification of chromatin. A ‘monkey-bar’ model rationalizes the findings.

    • Petra Vizjak
    • Dieter Kamp
    • Felix Mueller-Planitz
    Research
    Nature Structural & Molecular Biology
    Volume: 31, P: 1331-1340

  • Nucleosomes form arrays with even spacing between them in virtually all eukaryotes; however, their biogenesis is incompletely understood. Here the authors show that nucleosome density and DNA sequence along with the Ino80 chromatin remodeling complex play a role in nucleosome array formation in yeast and that the transcriptional machinery disrupts evenly-spaced nucleosomes.

    • Ashish Kumar Singh
    • Tamás Schauer
    • Felix Mueller-Planitz
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-15

  • Previous work has implied that the ATPase domain of ISWI chromatin remodelers cooperates with a DNA-binding accessory domain to achieve remodeling. Quantitative biochemical analyses now reveal that the ATPase domain exists in two conformations and that DNA binding induces the catalytically active conformation. The ATPase domain has an intrinsic ability to bind and remodel nucleosomes, which suggests that it acts autonomously.

    • Felix Mueller-Planitz
    • Henrike Klinker
    • Peter B Becker
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 82-89

  • Nucleosome-remodeling factors are instrumental in assembling and disassembling nucleosomes and moving nucleosomes along DNA in a process called nucleosome sliding. This Review summarizes recent progress in understanding of the basic nucleosome sliding mechanism and the interplay of the ATPase and accessory domains in optimizing and regulating nucleosome sliding.

    • Felix Mueller-Planitz
    • Henrike Klinker
    • Peter B Becker
    Reviews
    Nature Structural & Molecular Biology
    Volume: 20, P: 1026-1032