通过与ATM相关的Tra1子单元的直接激活器相互作用来招募HAT复合体
1Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, Department of Chemistry, The Pennsylvania State University, 306 Althouse Laboratory, University Park, PA 16802, USA.
Science (New York, N.Y.)
|June 26, 2001
概括
酸性转录激活剂直接与Trap1p结合,Trap1p是希斯乙转移酶复合体SAGA和NuA4.4中常见的子单元. 破坏这种相互作用会损害基因特异性转录和基因素乙化.
科学领域:
- 分子生物学分子生物学
- 基因规则 基因规则
- 表观遗传学 在表观遗传学中,表观遗传学是指表观遗传学.
背景情况:
- 像SAGA和NuA4这样的基因乙转移酶 (HAT) 复合体对于基因转录至关重要.
- 招募HAT活动到特定的基因促进体是关键的监管步骤.
- 转录激活剂和HAT之间的相互作用对于这种招募至关重要.
研究的目的:
- 研究转录激活剂与SAGA和NuA4 HAT复合体之间的直接相互作用.
- 为了确定SAGA和NuA4参与激活剂结合的特定亚单元.
- 阐明破坏激活器-HAT相互作用的功能后果.
主要方法:
- 亲和色谱被用来识别相互作用的蛋白质.
- 进行了照片交叉链接标签转移实验以确认直接相互作用.
- 用于研究特定蛋白质域的作用,采用了位点定向突变发生.
主要成果:
- 酸性转录激活剂直接与Trap1p相互作用,Trap1p是SAGA和NuA4.4的共享子单元.
- 在Tra1p的COOH末端的突变取消了激活剂结合.
- 这些突变导致了基因特异性转录缺陷,并减少了促销者特异性组织蛋白乙化.
结论:
- Tra1蛋白是与SAGA和NuA4 HAT复合体相互作用的转录激活剂的常见和必不可少的目标.
- 与Tra1p的直接相互作用对于招募HAT活性和随后的基因激活至关重要.
- 这项研究提供了对HAT复合体对转录的调节的机制性见解.
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