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.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 子项目的主要研究者可能是由其他来源提供的， 包括其他NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 在过去的十年中，有证据表明，相当一部分表观遗传信息是以组蛋白和相关DNA的化学修饰的形式传递的。我们的研究重点是了解共价组蛋白修饰在脊椎动物发育和分化过程中调节基因表达模式的机制基础。我们正在表征组蛋白甲基化的下游效应子，或“读者”，它们识别甲基标记并将其转化为特定的生物学结果。该项目的重点是识别识别组蛋白H3上精氨酸26（H3 R26 me）的阅读器蛋白。 这种修饰发生在赖氨酸27（H3 K27）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处的互斥H3 K27 ac与H3 K27 me 3修饰指定了它们的活性与平衡状态。在这里，我们假设H3 R26 me可能与H3 K27处的修饰发生串扰，并且为了研究H3 R26 me功能，我们提出鉴定和表征H3 R26 me阅读器。