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TitleAsymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 1000, Year 2024
Publish dateFeb 2, 2024
AuthorsLuka Bacic / Guillaume Gaullier / Jugal Mohapatra / Guanzhong Mao / Klaus Brackmann / Mikhail Panfilov / Glen Liszczak / Anton Sabantsev / Sebastian Deindl /
PubMed AbstractThe chromatin remodeler ALC1 is activated by DNA damage-induced poly(ADP-ribose) deposited by PARP1/PARP2 and their co-factor HPF1. ALC1 has emerged as a cancer drug target, but how it is recruited ...The chromatin remodeler ALC1 is activated by DNA damage-induced poly(ADP-ribose) deposited by PARP1/PARP2 and their co-factor HPF1. ALC1 has emerged as a cancer drug target, but how it is recruited to ADP-ribosylated nucleosomes to affect their positioning near DNA breaks is unknown. Here we find that PARP1/HPF1 preferentially initiates ADP-ribosylation on the histone H2B tail closest to the DNA break. To dissect the consequences of such asymmetry, we generate nucleosomes with a defined ADP-ribosylated H2B tail on one side only. The cryo-electron microscopy structure of ALC1 bound to such an asymmetric nucleosome indicates preferential engagement on one side. Using single-molecule FRET, we demonstrate that this asymmetric recruitment gives rise to directed sliding away from the DNA linker closest to the ADP-ribosylation site. Our data suggest a mechanism by which ALC1 slides nucleosomes away from a DNA break to render it more accessible to repair factors.
External linksNat Commun / PubMed:38307862 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

15777

8b0a

EMDB-15777, PDB-8b0a:
Cryo-EM structure of ALC1 bound to an asymmetric, site-specifically PARylated nucleosome
Method: EM (single particle) / Resolution: 3.0 Å

Source
  • homo sapiens (human)
  • xenopus laevis (African clawed frog)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN / ALC1 / CHD1L / nucleosome / PARylation / ADP-ribosylation / post-translational modification / chromatin

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