Srb7p是Tup1p的一个物理和生理靶点。
Srb7p is a physical and physiological target of Tup1p.
作者信息
Gromöller A, Lehming N
机构信息
Max-Delbrück-Laboratorium in der Max-Planck-Gesellschaft, Carl-von-Linné-Weg 10, 50829 Köln, Germany.
出版信息
EMBO J. 2000 Dec 15;19(24):6845-52. doi: 10.1093/emboj/19.24.6845.
Abstract
The holoenzyme of transcription integrates the positive and negative signals from the promoters of eukaryotic genes. We demonstrate that the essential holoenzyme component Srb7p is a physiologically relevant target of the global repressor Tup1p in Saccharomyces cerevisiae. Tup1p binds Srb7p in vivo and in vitro, and all genes tested that are repressed by Tup1p are derepressed when wild-type Srb7p is replaced by a mutant derivative of Srb7p that is no longer capable of interacting with Tup1p. Therefore, Srb7p is the first holoenzyme component essential for repression by Tup1p for which a physical interaction with Tup1p has been demonstrated. Furthermore, we find that Srb7p also binds Med6p and that this interaction is necessary for full transcriptional activation by different activators. Our finding that Med6p and Tup1p compete for the interaction with Srb7p suggests a model for Tup1p-mediated repression.
摘要
转录全酶整合了来自真核基因启动子的正性和负性信号。我们证明，必需的全酶组分Srb7p是酿酒酵母中全局阻遏物Tup1p在生理上相关的作用靶点。Tup1p在体内和体外均能与Srb7p结合，并且当野生型Srb7p被不再能够与Tup1p相互作用的Srb7p突变衍生物取代时，所有受Tup1p抑制的测试基因均会去抑制。因此，Srb7p是首个被证明与Tup1p存在物理相互作用且对Tup1p介导的抑制作用必不可少的全酶组分。此外，我们发现Srb7p还能与Med6p结合，并且这种相互作用对于不同激活剂的完全转录激活是必需的。我们发现Med6p和Tup1p竞争与Srb7p的相互作用，这提示了一种Tup1p介导的抑制模型。
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