{"title":"多种变构机制抑制PRC2活性基因的活性","authors":"Evan J. Worden","doi":"10.1038/s41594-025-01487-8","DOIUrl":null,"url":null,"abstract":"PRC2-dependent H3K27 methylation must be excluded from active genes to support appropriate transcriptional programs. Structures of PRC2 bound to nucleosome substrates containing histone modifications associated with active transcription explain how PRC2 is inhibited at active genes.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"32 2","pages":"215-216"},"PeriodicalIF":10.1000,"publicationDate":"2025-02-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Multiple allosteric mechanisms suppress PRC2 activity at active genes\",\"authors\":\"Evan J. Worden\",\"doi\":\"10.1038/s41594-025-01487-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"PRC2-dependent H3K27 methylation must be excluded from active genes to support appropriate transcriptional programs. Structures of PRC2 bound to nucleosome substrates containing histone modifications associated with active transcription explain how PRC2 is inhibited at active genes.\",\"PeriodicalId\":49141,\"journal\":{\"name\":\"Nature Structural & Molecular Biology\",\"volume\":\"32 2\",\"pages\":\"215-216\"},\"PeriodicalIF\":10.1000,\"publicationDate\":\"2025-02-06\",\"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/s41594-025-01487-8\",\"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/s41594-025-01487-8","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}
Multiple allosteric mechanisms suppress PRC2 activity at active genes
PRC2-dependent H3K27 methylation must be excluded from active genes to support appropriate transcriptional programs. Structures of PRC2 bound to nucleosome substrates containing histone modifications associated with active transcription explain how PRC2 is inhibited at active genes.
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.