期刊
MOLECULAR CELL
卷 7, 期 1, 页码 117-126出版社
CELL PRESS
DOI: 10.1016/S1097-2765(01)00160-5
关键词
-
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM023674, R37GM023674] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM23674] Funding Source: Medline
TUP1 is recruited to and represses genes that regulate mating, glucose and oxygen use, stress response, and DNA damage. It is shown here that disruption of either TUP1 or histone deacetylase HDA1 causes histone H3/H2B-specific hyperacetylation next to the TUP1 binding site at the stress-responsive ENA1 promoter. It is also shown that TUP1 interacts with HDA1 in vitro. These data indicate that TUP1 mediates localized histone deacetylation through HDA1. Interestingly, RPD3 deacetylates the ENA1 coding region, and both deacetylases contribute to ENA1 repression. However, epistasis analysis argues that only HDA1 and TUP1 are likely to function in the same pathway. These data define gene and histone targets of HDA1 and illustrate the role of histone deacetylation in TUP1 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