{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Koshkina D"],"funding":["Scientific project of Lomonosov Moscow State University research and education schools","National Institute of Health","NCI NIH HHS","Russian Science Foundation"],"pagination":["1309"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12427767"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(17)"],"pubmed_abstract":["Poly(ADP-ribose)polymerase 1 (PARP1) is an enzyme that interacts with chromatin during DNA repair and transcription processes; the molecular mechanisms of these processes remain to be determined. Previously, we have shown that PARP1 can bind to and reorganize nucleosomes using two modes of interaction with a mono-nucleosome, which are realized through PARP1 binding to the ends of linker DNA and to the nucleosome core. Here, it is shown that the latter mode of binding induces the reorganization of nucleosome structure and is more stable under the conditions of poly(ADP-ribosyl)ation (PARylation). The initial nucleosome structure is fully recovered after the dissociation of autoPARylated PARP1. The competition between PARP1 and linker histone H1.0 for binding to a nucleosome is mediated by t"],"journal":["Cells"],"pubmed_title":["Non-Classical H1-like PARP1 Binding to Chromatosome."],"pmcid":["PMC12427767"],"funding_grant_id":["#23-Sh04-57","R01 CA269975","R01CA269975","grant No. 19-74-30003"],"pubmed_authors":["Armeev G","Feofanov A","Pushkarev S","Maluchenko N","Nilov D","Kirpichnikov M","Korovina A","Lyubitelev A","Studitsky V","Koshkina D"],"additional_accession":[]},"is_claimable":false,"name":"Non-Classical H1-like PARP1 Binding to Chromatosome.","description":"Poly(ADP-ribose)polymerase 1 (PARP1) is an enzyme that interacts with chromatin during DNA repair and transcription processes; the molecular mechanisms of these processes remain to be determined. Previously, we have shown that PARP1 can bind to and reorganize nucleosomes using two modes of interaction with a mono-nucleosome, which are realized through PARP1 binding to the ends of linker DNA and to the nucleosome core. Here, it is shown that the latter mode of binding induces the reorganization of nucleosome structure and is more stable under the conditions of poly(ADP-ribosyl)ation (PARylation). The initial nucleosome structure is fully recovered after the dissociation of autoPARylated PARP1. The competition between PARP1 and linker histone H1.0 for binding to a nucleosome is mediated by t","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-04-08T19:53:22.408Z","creation":"2026-04-08T14:35:14.518Z"},"accession":"S-EPMC12427767","cross_references":{"pubmed":["40940725"],"doi":["10.3390/cells14171309"]}}