期刊
NUCLEIC ACIDS RESEARCH
卷 28, 期 21, 页码 4189-4196出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/28.21.4189
关键词
-
资金
- NIGMS NIH HHS [R01 GM044522, GM44522] Funding Source: Medline
The Drosophila Groucho (Gro) protein is the defining member of a family of metazoan corepressors that have roles in many aspects of development, including segmentation, dorsal/ventral pattern formation, Notch signaling, and Wnt/Wg signaling. Previous speculation has suggested that Gro may be orthologous to the yeast corepressor Tup1. In support of this idea, a detailed alignment between the C-terminal WD-repeat domains of these two proteins shows that each Gro WD repeat is most similar to the Tup1 WD repeat occupying the corresponding position in that protein. Our analysis of Gro-histone interactions provides further support for a close evolutionary relationship between Gro and Tup1. In particular, we show that, as with the N-terminal region of Tup1, the N-terminal region of Gro is necessary and sufficient for direct binding to histones. The highest affinity interaction is with histone H3 and binding is primarily observed with hypoacetylated histones. Using transient transfection assays, we show that a Gal4-Gro fusion protein containing the histone-binding domain is able to repress transcription. Deletions that weaken histone binding also weaken repression. These findings, along with our recent report that Gro interacts with the histone deacetylase Rpd3, suggest a mechanism for Gro-mediated repression.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据