Acidic domains differentially read histone H3 lysine 4 methylation status and are widely present in

• 作 者: Meng Wu Wei Wei Jiwei Chen Ron
• 机 构: ShanghaiKeyLaboratoryofRegulatoryBiology,CollaborativeInnovationCenterforCancerMedicine,Universityde
• 出 处: 中国科学：生命科学英文版
• 发表日期: 2017年2期
• 关键词: 组蛋白H3 相关蛋白 甲基化 染色质 酸性 赖氨酸 状态 阅读 histone methylation H3K4mel H3K4me2 H3K4me3
• 基金项目: supported by the Ministry of Science and Technology of China (2015CB910402) to Jiemin Wong,,the National Natural Science Foundation of China (91419303),,The Science and Technology Commission of Shangh

Histone methylation is believed to provide binding sites for specific reader proteins, which translate histone code into biological function. Here we show that a family of acidic domain-containing proteins including nucleophosmin (NPM1), pp32, SET/TAF1β,