Evidence that Ga111 protein is a target of the Ga14 activation domain in the mediator

被引:58
作者
Jeong, CJ
Yang, SH
Xie, YQ
Zhang, L
Johnston, SA
Kodadek, T
机构
[1] Univ Texas, SW Med Ctr, Ryburn Ctr Mol Cardiol, Dept Internal Med, Dallas, TX 75390 USA
[2] Univ Texas, SW Med Ctr, Ryburn Ctr Mol Cardiol, Dept Biochem, Dallas, TX 75390 USA
关键词
D O I
10.1021/bi010011k
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The mediator is an approximately 20 protein complex that is essential for the transcription of most genes in yeast. It is contacted by a number of gene-specific activators, but the details of these interactions are not well understood in most cases. Here, evidence is presented that the mediator component Gal11 represents at least one target of the Gal4 activation domain (AD). Deletion of Gall l is shown to decrease the affinity of the Gal4 AD for the mediator, and direct binding of an N-terminal domain of Gall l with the Gal4 AD is demonstrated. Quantitative studies, however, indicate that the K-D of the 1:1 Gal4 AD-Gal11 complex is modest. Combined with in vivo data showing that Delta gal11 cells exhibit reduced, but still significant, Gal4-mediated gene expression, these results suggest that the dimeric activator might also contact another protein in the mediator in addition to Gal11.
引用
收藏
页码:9421 / 9427
页数:7
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