{"doi":"10.64898/2026.05.14.724656","title":"Epigenetic maintenance of PRC2-repressed chromatin requires RTT109 but not H3K56 acetylation","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>\n                  In animals, plants, and some fungi, Polycomb Repressive Complex 2 (PRC2) catalyzes trimethylation of histone H3 lysine 27 (H3K27me3) to establish transcriptionally repressed chromatin. Here, we identify the histone acetyltransferase RTT109 as a key regulator of PRC2-repressed domains in the model fungus\n                  <jats:italic>Neurospora crassa</jats:italic>\n                  . Although RTT109 interacts with the VPS75 homolog Nucleosome Assembly Factor 2 (NAF-2), we show that proper structure and function of PRC2-methylated chromatin require RTT109 catalytic activity but are independent of NAF-2 and H3K56 acetylation. We further demonstrate that H3K27me3 can be stably propagated over multiple rounds of mitosis in the absence of sequence-specific PRC2 targeting, and that RTT109 is essential for maintenance of the repressed state. These findings uncover a replication-linked mechanism for epigenetic memory and establish RTT109 as a key regulator of Polycomb-mediated chromatin inheritance.\n                </jats:p>","journal":null,"year":null,"id":659487,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1398051,"name":"Felicia Ebot-Ojong","orcid":"0000-0002-3408-3487","position":1,"is_corresponding":false},{"id":476490,"name":"Abigail J. Courtney","orcid":"0000-0001-5319-2630","position":2,"is_corresponding":false},{"id":326609,"name":"Zachary Lewis","orcid":"0000-0002-1735-8266","position":3,"is_corresponding":false},{"id":890104,"name":"Rochelle E. Yap","orcid":"0000-0002-9181-280X","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Epigenetic maintenance of PRC2-repressed chromatin requires RTT109 but not H3K56 acetylation","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>\n                  In animals, plants, and some fungi, Polycomb Repressive Complex 2 (PRC2) catalyzes trimethylation of histone H3 lysine 27 (H3K27me3) to establish transcriptionally repressed chromatin. Here, we identify the histone acetyltransferase RTT109 as a key regulator of PRC2-repressed domains in the model fungus\n                  <jats:italic>Neurospora crassa</jats:italic>\n                  . Although RTT109 interacts with the VPS75 homolog Nucleosome Assembly Factor 2 (NAF-2), we show that proper structure and function of PRC2-methylated chromatin require RTT109 catalytic activity but are independent of NAF-2 and H3K56 acetylation. We further demonstrate that H3K27me3 can be stably propagated over multiple rounds of mitosis in the absence of sequence-specific PRC2 targeting, and that RTT109 is essential for maintenance of the repressed state. These findings uncover a replication-linked mechanism for epigenetic memory and establish RTT109 as a key regulator of Polycomb-mediated chromatin inheritance.\n                </jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"42182108","pmcid":null,"openalex_id":"https://openalex.org/W7161580602","authors":[],"funders":[{"funder_name":"","grant_id":"R35GM15213401","title":null}],"total_grants":1,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"green","license":"cc-by-nc-nd","oa_locations":[{"url":"https://doi.org/10.64898/2026.05.14.724656","host_type":"repository"},{"url":"https://doi.org/10.64898/2026.05.14.724656","host_type":"repository"},{"url":"https://syndication.highwire.org/content/doi/10.64898/2026.05.14.724656","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/42182108","host_type":"repository"},{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC13192808/","host_type":"repository"}],"fields_of_study":["Genomics and Chromatin Dynamics","Epigenetics and DNA Methylation","Plant Molecular Biology Research"],"mesh_terms":[],"keywords":["Chromatin","Histone H3","Neurospora crassa","Nucleosome","PRC2","Histone","Histone code","Acetylation","Histone octamer"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T07:01:01.043111Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}