{"title":"凝析油中PRC1压实染色质的染色质网格模型","authors":"Nicole J. Francis","doi":"10.1038/s41594-025-01504-w","DOIUrl":null,"url":null,"abstract":"The structure of chromatin bound by Polycomb repressive complex 1 (PRC1) and how it contributes to transcription repression are unknown. Here, cryo-electron tomography (cryo-ET) of PRC1–chromatin condensates reveal randomly oriented neighboring nucleosomes in a stable, open chromatin mesh that might exclude large protein complexes to repress transcription.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 3","pages":"411-413"},"PeriodicalIF":10.1000,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A chromatin mesh model for compaction of chromatin by PRC1 in condensates\",\"authors\":\"Nicole J. Francis\",\"doi\":\"10.1038/s41594-025-01504-w\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The structure of chromatin bound by Polycomb repressive complex 1 (PRC1) and how it contributes to transcription repression are unknown. Here, cryo-electron tomography (cryo-ET) of PRC1–chromatin condensates reveal randomly oriented neighboring nucleosomes in a stable, open chromatin mesh that might exclude large protein complexes to repress transcription.\",\"PeriodicalId\":49141,\"journal\":{\"name\":\"Nature Structural & Molecular Biology\",\"volume\":\"32 3\",\"pages\":\"411-413\"},\"PeriodicalIF\":10.1000,\"publicationDate\":\"2025-03-03\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature Structural & Molecular Biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.nature.com/articles/s41594-025-01504-w\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature Structural & Molecular Biology","FirstCategoryId":"99","ListUrlMain":"https://www.nature.com/articles/s41594-025-01504-w","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
A chromatin mesh model for compaction of chromatin by PRC1 in condensates
The structure of chromatin bound by Polycomb repressive complex 1 (PRC1) and how it contributes to transcription repression are unknown. Here, cryo-electron tomography (cryo-ET) of PRC1–chromatin condensates reveal randomly oriented neighboring nucleosomes in a stable, open chromatin mesh that might exclude large protein complexes to repress transcription.
期刊介绍：
Nature Structural & Molecular Biology is a comprehensive platform that combines structural and molecular research. Our journal focuses on exploring the functional and mechanistic aspects of biological processes, emphasizing how molecular components collaborate to achieve a particular function. While structural data can shed light on these insights, our publication does not require them as a prerequisite.
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