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由CK2对基因素H2A的氨酸酸化调节了转录延长的过程

Harihar Basnet¹, Xue B Su², Yuliang Tan³

¹1] Howard Hughes Medical Institute, Department of Medicine, University of California San Diego, La Jolla, California 92093, USA [2] Biomedical Sciences Graduate Program, School of Medicine, University of California San Diego, La Jolla, California 92093, USA.

|September 26, 2014

概括

科学家们发现了一种新的基因转录延长调节机制,涉及素激酶2 (CK2) 和基因素H2A酸化. 这一发现在所有物种中都存在,并影响了关键的细胞过程.

科学领域:

分子生物学分子生物学
表观遗传学在表观遗传学中,表观遗传学是指表观遗传学.
基因规则基因规则

背景情况:

翻译后的组织蛋白修饰对于调节包括转录在内的基本细胞过程至关重要.
识别不同阶段 (启动,延伸,终止) 控制转录调节的新型组织蛋白修饰具有重大科学意义.

研究的目的:

确定和描述转录延长的新监管机制.
调查氨酸酸化在转录调节中的histon H2A氨酸酸化作用.
为了阐明素激酶2 (CK2) 在这个新发现的调节途径中的参与.

主要方法:

利用酵母和哺乳动物细胞模型来研究转录延长.
采用位点定向的突变发生法来改变氨酸57 (Tyr57) 在素H2A中.
进行全基因组结合分析,绘制CK2α.的局部位置.
评估了基因组修饰 (H2B单基化,H3K4me3,H3K79me3) 和Spt-Ada-Gcn5乙转移酶 (SAGA) 复合物的活性.

主要成果:

发现Tyr57在基因组H2A中的酸化,由CK2氨酸激酶活性介导,调节了转录延长.
证明抑制CK2或突变H2ATyr57会损害酵母和哺乳动物细胞中的转录延长.
表明CK2α与编码基因和活性增强剂结合.
观察到H2A Tyr57突变导致H2B单基化和H3K4me3/H3K79me3标记的丧失.
发现CK2抑制或H2A Tyr57突变增强了SAGA复合体的H2B二维基化活性.

结论:

确定了一种新型的转录延长调节层,这种调节层从酵母保存到哺乳动物.
已确定 H2A Tyr57 的 CK2-依赖型氨酸酸化是转录延长的关键调节者.
突出了这种酸化在转录期间协调SAGA复合体活动中的作用.

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