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Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1.

Posttranslational modifications play key roles in regulating chromatin plasticity. Although various chromatin-remodeling enzymes have been described that respond to specific histone modifications, little is known about the role of poly[adenosine 5'-diphosphate (ADP)-ribose] in chromatin remodeling. Here, we identify a chromatin-remodeling enzyme, ALC1 (Amplified in Liver Cancer 1, also known as CHD1L), that interacts with poly(ADP-ribose) and catalyzes PARP1-stimulated nucleosome sliding. Our results define ALC1 as a DNA damage-response protein whose role in this process is sustained by its association with known DNA repair factors and its rapid poly(ADP-ribose)-dependent recruitment to DNA damage sites. Furthermore, we show that depletion or overexpression of ALC1 results in sensitivity to DNA-damaging agents. Collectively, these results provide new insights into the mechanisms by which poly(ADP-ribose) regulates DNA repair.

Pubmed ID: 19661379


  • Ahel D
  • Horejs√≠ Z
  • Wiechens N
  • Polo SE
  • Garcia-Wilson E
  • Ahel I
  • Flynn H
  • Skehel M
  • West SC
  • Jackson SP
  • Owen-Hughes T
  • Boulton SJ


Science (New York, N.Y.)

Publication Data

September 4, 2009

Associated Grants

  • Agency: Wellcome Trust, Id: 064414
  • Agency: Wellcome Trust, Id: 064414
  • Agency: Cancer Research UK, Id: 11224
  • Agency: Cancer Research UK, Id: A3549
  • Agency: Cancer Research UK, Id: A5290
  • Agency: Biotechnology and Biological Sciences Research Council, Id:
  • Agency: Cancer Research UK, Id:
  • Agency: Department of Health, Id:

Mesh Terms

  • Adenosine Triphosphatases
  • Adenosine Triphosphate
  • Cell Line
  • Chromatin
  • Chromatin Assembly and Disassembly
  • DNA Damage
  • DNA Helicases
  • DNA Repair
  • DNA-Binding Proteins
  • Humans
  • Hydrogen Peroxide
  • Immunoprecipitation
  • Kinetics
  • Mutant Proteins
  • Nucleosomes
  • Phleomycins
  • Poly Adenosine Diphosphate Ribose
  • Poly(ADP-ribose) Polymerases
  • Protein Structure, Tertiary
  • Radiation, Ionizing
  • Recombinant Proteins