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Showing 1–6 of 6 results
Advanced filters: Author: Markus Hassler Clear advanced filters

  • Despite a ban on ozone depleting substances, ozone depletion during cold winters in the Arctic stratosphere has been increasing in recent decades. Here, the authors show conditions favourable for Arctic ozone depletion could worsen as a response of stratospheric temperature and water to continued release of greenhouse gases.

    • Peter von der Gathen
    • Rigel Kivi
    • Markus Rex
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-17

  • ADP-ribosylation catalyzed by PARPs and sirtuins is an important post-translation modification. Macrodomain proteins MacroD1 and D2 are now shown to preferentially bind mono-ADP-ribosylated proteins and to act as proximal ADP-ribosylhydrolases. The crystal structure of the MacroD2–ADPr complex suggests a catalytic mechanism for the reaction.

    • Gytis Jankevicius
    • Markus Hassler
    • Andreas G Ladurner
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 508-514

  • Cryo-EM structures of the S. cerevisiae condensin holo complex reveal that ATP binding triggers exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains, potentially leading to an interconversion of DNA-binding sites in the catalytic core of condensin that might form the basis of its DNA translocation and loop-extrusion activities.

    • Byung-Gil Lee
    • Fabian Merkel
    • Christian H. Haering
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 743-751

  • PARP1 is activated by sensing DNA damage, forming ADP-ribose chains that recruit DNA repair and chromatin remodeling factors. PARP1 recognizes DNA damage through its DNA-binding domain, which contains two zinc-finger regions (ZnF1 and ZnF2). The crystal structure of human PARP1-DBD bound to a DNA break reveals a dimeric arrangement, in which ZnF1 from one monomer interacts with ZnF2 from the other monomer, to recognize the DNA strand break.

    • Ammar A E Ali
    • Gyula Timinszky
    • Antony W Oliver
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 685-692

  • The crystal structure of the FACT histone chaperone domain Spt16M in complex with the H2A–H2B heterodimer is solved; Spt16M makes several interactions with histones and seems to block the interaction of H2B with DNA, which could explain how FACT destabilizes nucleosomes to promote transcription.

    • Maria Hondele
    • Tobias Stuwe
    • Andreas G. Ladurner
    Research
    Nature
    Volume: 499, P: 111-114