DNA repair factor APLF is a histone chaperone.

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  • Additional Information
    • Source:
      Publisher: Cell Press Country of Publication: United States NLM ID: 9802571 Publication Model: Print Cited Medium: Internet ISSN: 1097-4164 (Electronic) Linking ISSN: 10972765 NLM ISO Abbreviation: Mol Cell Subsets: MEDLINE
    • Publication Information:
      Publication: Cambridge Ma : Cell Press
      Original Publication: Cambridge, Mass. : Cell Press, c1997-
    • Subject Terms:
      DNA Repair*; Histone Chaperones/*physiology ; Phosphoproteins/*physiology; Amino Acid Motifs ; Animals ; Caenorhabditis elegans/genetics ; Cell Line ; DNA Damage ; DNA-(Apurinic or Apyrimidinic Site) Lyase ; Eukaryota/genetics ; HeLa Cells ; Histone Chaperones/chemistry ; Histone Chaperones/genetics ; Histones/metabolism ; Humans ; Molecular Sequence Data ; Phosphoproteins/chemistry ; Phosphoproteins/genetics ; Poly-ADP-Ribose Binding Proteins ; Protein Interaction Mapping ; Proteins/chemistry ; Proteins/genetics ; Proteins/physiology ; Sequence Homology ; tRNA Methyltransferases
    • Abstract:
      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.
      (Copyright © 2011 Elsevier Inc. All rights reserved.)
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    • Grant Information:
      095062 United Kingdom WT_ Wellcome Trust; 064414 United Kingdom WT_ Wellcome Trust; BB/E022286/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; United Kingdom WT_ Wellcome Trust; United Kingdom CRUK_ Cancer Research UK
    • Contributed Indexing:
      Indexing Agency: NLM Local ID #: UKMS49749.
    • Accession Number:
      0 (Histone Chaperones)
      0 (Histones)
      0 (Phosphoproteins)
      0 (Poly-ADP-Ribose Binding Proteins)
      0 (Proteins)
      EC 2.1.1.- (TRMO protein, human)
      EC 2.1.1.- (tRNA Methyltransferases)
      EC 4.2.99.18 (APLF protein, human)
      EC 4.2.99.18 (DNA-(Apurinic or Apyrimidinic Site) Lyase)
    • Publication Date:
      Date Created: 20110108 Date Completed: 20110217 Latest Revision: 20230610
    • Publication Date:
      20240829
    • Accession Number:
      PMC3443741
    • Accession Number:
      10.1016/j.molcel.2010.12.008
    • Accession Number:
      21211722