EVIDENCE FOR PHYSICAL INTERACTION BETWEEN THE ZINC-FINGER TRANSCRIPTION FACTORS YY1 AND SP1
EVIDENCE FOR PHYSICAL INTERACTION BETWEEN THE ZINC-FINGER TRANSCRIPTION FACTORS YY1 AND SP1
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DOI：
10.1073/pnas.90.13.6145
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发表时间：
1993-07-01
影响因子：
11.1
通讯作者：
SHI, Y
中科院分区：
文献类型：
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作者：
LEE, JS;GALVIN, KM;SHI, Y
两个启动子元件对于碱基水平的转录非常重要，TATA基序通常位于转录起始位点上游30个核苷酸的位置，而启动子元件（Inr）则包含起始位点。人们对Inr元件的工作机制知之甚少，部分原因是很少有与Inr元件结合的蛋白质被识别和分离出来。最近克隆的YY1就是这样一种结合inr的蛋白。YY1在体外结合其识别序列后能够指导转录。由于TATA基序或转录因子Sp1结合位点的存在，YY1启动转录的能力得到增强。为了研究YY1和Sp1之间明显功能合作的机制，我们探索了这两个转录因子之间蛋白-蛋白相互作用的可能性。我们发现YY1和Sp1可以形成物理络合物。此外，我们在YY1和Sp1中确定了它们之间相互作用的域。因此，YY1和Sp1之间的物理相互作用可能构成先前观察到的功能相互作用的基础。
Two promoter elements are important for basal-level transcription, the TATA motif typically located 30 nucleotides upstream of the transcription initiation site and the initiator (Inr) element encompassing the start site. The mechanism of how Inr elements work is poorly understood, partly because very few proteins that bind to Inr elements have been identified and isolated. The recently cloned YY1 is such an Inr-binding protein. YY1 is able to direct transcription upon binding to its recognition sequence in vitro. The ability of YY1 to initiate transcription is augmented by the presence of a TATA motif or binding sites for transcription factor Sp1. To study the mechanism underlying the apparent functional cooperation between YY1 and Sp1, we explored the possibility of protein-protein interactions between these two transcription factors. We found that YY1 and Sp1 can form a physical complex. In addition, we identified domains within YY1 and Sp1 that mediate their interactions with each other. The physical interaction between YY1 and Sp1 may thus form the basis for the functional interplay observed previously.