HISTONE ARGININE METHYLATION IN ES CELLS

ES 细胞中的组蛋白精氨酸甲基化

• 批准号: 8363846
• 负责人: Joanna Wysocka
• 金额: $ 0.8万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-06-01 至 2012-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8363846
• 关键词: Arginine; Biological; Chemicals; DNA; Development; Epigenetic Process; Funding; Gene Expression; Genetic Enhancer Element; Grant; Histone H3; Histones; Lysine; Mass Spectrum Analysis; Mediating; Methylation; Modification; National Center for Research Resources; Outcome; Pattern; Polycomb; Principal Investigator; Proteins; Reader; Research; Research Infrastructure; Resources; Source; Specific qualifier value; Translating; United States National Institutes of Health; base; cost; embryonic stem cell; histone modification

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. In the last decade evidence emerged that a substantial portion of epigenetic information is transmitted in a form of chemical modifications of histones and associated DNA. Our research focuses on understanding the mechanistic basis by which covalent histone modifications regulate gene expression patterns during vertebrate development and differentiation. We are characterizing downstream effectors of histone methylation, or "readers", which recognize the methyl marks and translate them into specific biological outcomes. The proposed project focuses on identifying reader proteins that recognize Arginine 26 on Histone H3 (H3R26me). This modification occurs right next to the lysine 27 (H3K27), which is a critical residue for Polycomb mediated histone methylation. Moreover, we had recently shown that mutually exclusive H3K27ac versus H3K27me3 modification at enhancer elements in embryonic stem cells specifies their active versus poised state. Here we hypothesize that H3R26me may cross talk with modifications at H3K27 and to investigate H3R26me function we propose to identify and characterize H3R26me readers.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 在过去的十年中，有证据表明，很大一部分表观遗传信息以组蛋白和相关DNA的化学修饰形式传播。我们的研究重点是理解共价组蛋白修饰调节脊椎动物发育和分化过程中基因表达模式的机理基础。我们正在表征组蛋白甲基化的下游效应因子或“读取器”，这些甲基化识别甲基标记并将其转化为特定的生物学结果。拟议的项目着重于识别识别组蛋白H3（H3R26ME）上精氨酸26的读取器蛋白。 这种修饰发生在赖氨酸27（H3K27）旁边，这是Polycomb介导的组蛋白甲基化的关键残基。此外，我们最近表明，在胚胎干细胞中增强子元件上的相互排斥的H3K27AC与H3K27me3修改指定其活性与固定状态。在这里，我们假设H3R26ME可能会与H3K27的修改进行交流，并研究H3R26ME功能，我们建议识别和表征H3R26ME读者。