{"entity": "publication", "iuid": "974cca67083146548a6809ca2511681e", "timestamp": "2026-09-25T15:29:24.279Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/974cca67083146548a6809ca2511681e.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/974cca67083146548a6809ca2511681e"}}, "title": "Asymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1.", "authors": [{"family": "Bacic", "given": "Luka", "initials": "L"}, {"family": "Gaullier", "given": "Guillaume", "initials": "G", "orcid": "0000-0003-3405-6021", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e5b881e6afc64eaa95c82097346e33f6.json"}}, {"family": "Mohapatra", "given": "Jugal", "initials": "J"}, {"family": "Mao", "given": "Guanzhong", "initials": "G"}, {"family": "Brackmann", "given": "Klaus", "initials": "K"}, {"family": "Panfilov", "given": "Mikhail", "initials": "M", "orcid": "0000-0003-2875-7315", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/757c08197cec42ccb3995c0af1bb79ca.json"}}, {"family": "Liszczak", "given": "Glen", "initials": "G"}, {"family": "Sabantsev", "given": "Anton", "initials": "A", "orcid": "0000-0002-8559-8894", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1a997c393bf2489699c700ddceecb885.json"}}, {"family": "Deindl", "given": "Sebastian", "initials": "S", "orcid": "0000-0001-6807-8654", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d409ebe1ddd945279b82704b1942fa93.json"}}], "type": "journal article", "published": "2024-02-02", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "15", "issue": "1", "pages": "1000", "issn-l": "2041-1723"}, "abstract": "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.", "doi": "10.1038/s41467-024-45237-8", "pmid": "38307862", "labels": {"SciLifeLab Fellow": "", "Sebastian Deindl": ""}, "xrefs": [{"db": "pmc", "key": "PMC10837151"}, {"db": "pii", "key": "10.1038/s41467-024-45237-8"}, {"db": "PDB", "key": "8B0A"}, {"db": "Dataset DOI", "key": "https://doi.org/10.17044/scilifelab.24764697"}], "notes": [], "created": "2026-09-23T09:05:50.190Z", "modified": "2026-09-23T09:05:50.314Z"}