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Single-particle cryo-EM dataset of ALC1 bound to an asymmetric, site-specifically PARylated nucleosome


ABSTRACT:

SUBMITTER: Guillaume Gaullier 

PROVIDER: EMPIAR-11211 | biostudies-other |

REPOSITORIES: biostudies-other

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Publications

Asymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1.

Bacic Luka L   Gaullier Guillaume G   Mohapatra Jugal J   Mao Guanzhong G   Brackmann Klaus K   Panfilov Mikhail M   Liszczak Glen G   Sabantsev Anton A   Deindl Sebastian S  

Nature communications 20240202 1


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-ribo  ...[more]

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