How transcriptional activators bind target proteins
How transcriptional activators bind target proteins
复制标题
DOI：
10.1074/jbc.m103793200
复制
发表时间：
2001-10-26
影响因子：
4.8
通讯作者：
Wright, AP
中科院分区：
文献类型：
--
作者：
Hermann, S;Berndt, KD;Wright, AP
原癌基因c-myc的产物通过调节特定的靶基因影响许多细胞过程。C-Myc蛋白通过其反式激活结构域(TAD)与多种转录因子相互作用，包括TATA结合蛋白(TBP)。我们提供的数据表明，与其他一些转录激活剂相反，c-Myc TAD的延长长度是其与TBP结合所必需的。我们的数据还表明，这种相互作用是一个多步骤的过程，在这个过程中，快速形成的低亲和力络合物慢慢转化为更稳定的形式。最初的络合物形成是离子或极性相互作用的结果，而缓慢转变为更稳定的形式本质上是疏水的。基于我们的结果，我们提出了两个可供选择的激活结构域/靶蛋白相互作用模型，这两个模型共同为理解激活剂-靶因子相互作用提供了一个单一的通用范式。
The product of the proto-oncogene c-myc influences many cellular processes through the regulation of specific target genes. Through its transactivation domain (TAD), c-Myc protein interacts with several transcription factors, including TATA-binding protein (TBP). We present data that suggest that in contrast to some other transcriptional activators, an extended length of the c-Myc TAD is required for its binding to TBP. Our data also show that this interaction is a multistep process, in which a rapidly forming low affinity complex slowly converts to a more stable form. The initial complex formation results from ionic or polar interactions, whereas the slow conversion to a more stable form is hydrophobic in nature. Based on our results, we suggest two alternative models for activation domain/target protein interactions, which together provide a single universal paradigm for understanding activator-target factor interactions.