{"title":"组蛋白H4苏氨酸71的o - glcn酰化是异染色质的一个组成部分。","authors":"Koji Hayakawa, Mitsuko Hirosawa, Daisuke Nara, Nobuyuki Fujiwara, Kunio Shiota, Satoshi Tanaka","doi":"10.1093/jb/mvaf044","DOIUrl":null,"url":null,"abstract":"<p><p>Previous studies have reported several O-linked N-acetylglucosamine (O-GlcNAc) modifications of core histones H2A, H2B, H3 and H4. In parallel, the characteristics and functions of O-GlcNAcylated histones are also shown, and they are involved in various cellular processes, such as development and tumorigenesis, indicating that the exploration of new histone O-GlcNAcylation contributes significantly to the elucidation of molecular mechanisms occurring in cells. Here, we report that O-GlcNAcylation occurs at threonine 71 of histone H4 (H4T71Gc) by developing a monoclonal antibody that recognizes the O-GlcNAcylated H4T71 peptide. Threonine 71 of histone H4 is highly conserved from metazoans to mammals, and H4T71Gc can be detected. Chromatin immunoprecipitation-seq and biochemical analysis revealed that H4T71Gc was localized to the region where histone H3 modified by trimethylation of lysine 9 (H3K9me3) was enriched in a genome-wide manner. H3K9me3 is known to function in chromatin condensation, suggesting that H4T71Gc plays a role in both the progression and maintenance of condensed chromatin in several species.</p>","PeriodicalId":15234,"journal":{"name":"Journal of biochemistry","volume":" ","pages":"277-285"},"PeriodicalIF":1.7000,"publicationDate":"2025-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A novel O-GlcNAcylation at threonine 71 of histone H4 is a component of heterochromatin.\",\"authors\":\"Koji Hayakawa, Mitsuko Hirosawa, Daisuke Nara, Nobuyuki Fujiwara, Kunio Shiota, Satoshi Tanaka\",\"doi\":\"10.1093/jb/mvaf044\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Previous studies have reported several O-linked N-acetylglucosamine (O-GlcNAc) modifications of core histones H2A, H2B, H3 and H4. In parallel, the characteristics and functions of O-GlcNAcylated histones are also shown, and they are involved in various cellular processes, such as development and tumorigenesis, indicating that the exploration of new histone O-GlcNAcylation contributes significantly to the elucidation of molecular mechanisms occurring in cells. Here, we report that O-GlcNAcylation occurs at threonine 71 of histone H4 (H4T71Gc) by developing a monoclonal antibody that recognizes the O-GlcNAcylated H4T71 peptide. Threonine 71 of histone H4 is highly conserved from metazoans to mammals, and H4T71Gc can be detected. Chromatin immunoprecipitation-seq and biochemical analysis revealed that H4T71Gc was localized to the region where histone H3 modified by trimethylation of lysine 9 (H3K9me3) was enriched in a genome-wide manner. H3K9me3 is known to function in chromatin condensation, suggesting that H4T71Gc plays a role in both the progression and maintenance of condensed chromatin in several species.</p>\",\"PeriodicalId\":15234,\"journal\":{\"name\":\"Journal of biochemistry\",\"volume\":\" \",\"pages\":\"277-285\"},\"PeriodicalIF\":1.7000,\"publicationDate\":\"2025-09-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of biochemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1093/jb/mvaf044\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of biochemistry","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1093/jb/mvaf044","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
A novel O-GlcNAcylation at threonine 71 of histone H4 is a component of heterochromatin.
Previous studies have reported several O-linked N-acetylglucosamine (O-GlcNAc) modifications of core histones H2A, H2B, H3 and H4. In parallel, the characteristics and functions of O-GlcNAcylated histones are also shown, and they are involved in various cellular processes, such as development and tumorigenesis, indicating that the exploration of new histone O-GlcNAcylation contributes significantly to the elucidation of molecular mechanisms occurring in cells. Here, we report that O-GlcNAcylation occurs at threonine 71 of histone H4 (H4T71Gc) by developing a monoclonal antibody that recognizes the O-GlcNAcylated H4T71 peptide. Threonine 71 of histone H4 is highly conserved from metazoans to mammals, and H4T71Gc can be detected. Chromatin immunoprecipitation-seq and biochemical analysis revealed that H4T71Gc was localized to the region where histone H3 modified by trimethylation of lysine 9 (H3K9me3) was enriched in a genome-wide manner. H3K9me3 is known to function in chromatin condensation, suggesting that H4T71Gc plays a role in both the progression and maintenance of condensed chromatin in several species.
期刊介绍：
The Journal of Biochemistry founded in 1922 publishes the results of original research in the fields of Biochemistry, Molecular Biology, Cell, and Biotechnology written in English in the form of Regular Papers or Rapid Communications. A Rapid Communication is not a preliminary note, but it is, though brief, a complete and final publication. The materials described in Rapid Communications should not be included in a later paper. The Journal also publishes short reviews (JB Review) and papers solicited by the Editorial Board.
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