DNA repair factor APLF is a histone chaperone

Pawan Vinod Mehrotra, Dragana Ahel, Daniel P. Ryan, Ria Weston, Nicola Wiechens, Rolf Kraehenbuehl, Tom Owen-Hughes, Ivan Ahel

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    Poly(ADP-ribosyl)ation plays a major role in DNA repair, where it regulates chromatin relaxation as one of the critical events in the repair process. However, the molecular mechanism by which poly (ADP-ribose) modulates chromatin remains poorly understood. Here we identify the poly(ADP-ribose)regulated protein APLF as a DNA-damage-specific histone chaperone. APLF preferentially binds to the histone H3/H4 tetramer via its C-terminal acidic motif, which is homologous to the motif conserved in the histone chaperones of the NAP1L family (NAP1L motif). We further demonstrate that APLF exhibits histone chaperone activities in a manner that is dependent on its acidic domain and that the NAP1L motif is critical for the repair capacity of APLF in vivo. Finally, we identify structural analogs of APLF in lower eukaryotes with the ability to bind histones and localize to the sites of DNA-damage-induced poly(ADP-ribosyl)ation. Collectively, these findings define the involvement of histone chaperones in poly(ADP-ribose)-regulated DNA repair reactions.

    Original languageEnglish
    Pages (from-to)46-55
    Number of pages10
    JournalMolecular Cell
    Issue number1
    Publication statusPublished - 7 Jan 2011


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    Mehrotra, P. V., Ahel, D., Ryan, D. P., Weston, R., Wiechens, N., Kraehenbuehl, R., Owen-Hughes, T., & Ahel, I. (2011). DNA repair factor APLF is a histone chaperone. Molecular Cell, 41(1), 46-55. https://doi.org/10.1016/j.molcel.2010.12.008