Jeong C J, Yang S H, Xie Y, Zhang L, Johnston S A, Kodadek T
Department of Internal Medicine, Ryburn Center for Molecular Cardiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-8573, USA.
Biochemistry. 2001 Aug 7;40(31):9421-7. doi: 10.1021/bi010011k.
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 Gal11 is shown to decrease the affinity of the Gal4 AD for the mediator, and direct binding of an N-terminal domain of Gal11 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.
中介体是一种约由20种蛋白质组成的复合体,对酵母中大多数基因的转录至关重要。它与许多基因特异性激活因子相互作用,但在大多数情况下,这些相互作用的细节尚不清楚。本文提供的证据表明,中介体组分Gal11至少是Gal4激活域(AD)的一个靶点。研究表明,删除Gal11会降低Gal4 AD与中介体的亲和力,并且证实了Gal11的N端结构域与Gal4 AD直接结合。然而,定量研究表明,1:1 Gal4 AD - Gal11复合体的解离常数适中。结合体内数据显示,缺失Gal11的细胞中Gal4介导的基因表达降低,但仍很显著,这些结果表明,二聚体激活因子除了与Gal11相互作用外,可能还与中介体中的另一种蛋白质相互作用。