Starr D B, Hawley D K
Department of Chemistry, University of Oregon, Eugene 97403.
Cell. 1991 Dec 20;67(6):1231-40. doi: 10.1016/0092-8674(91)90299-e.
We have analyzed the interaction of the general RNA polymerase II transcription factor TFIID with its DNA-binding site, the TATA box (consensus sequence TATAAAA). We have demonstrated that TFIID, unlike most sequence-specific DNA-binding proteins, interacts primarily within the minor groove of the DNA helix. This was established by a novel approach involving complete replacement of the thymines and adenines in the TATA box with cytosines and inosines, respectively. This substitution exchanged the major groove of TATAAAA for that of the sequence CGCGGGG, without altering the surface of the minor groove. The unusual DNA-binding properties of TFIID revealed by this study have important implications for TFIID specificity and function and, more generally, for sequence-specific recognition by DNA-binding proteins.
我们分析了通用RNA聚合酶II转录因子TFIID与其DNA结合位点TATA框（共有序列TATAAAA）之间的相互作用。我们已经证明，与大多数序列特异性DNA结合蛋白不同，TFIID主要在DNA螺旋的小沟内相互作用。这是通过一种新颖的方法确定的，该方法包括分别用胞嘧啶和次黄嘌呤完全取代TATA框中的胸腺嘧啶和腺嘌呤。这种取代将TATAAAA的大沟换成了序列CGCGGGG的大沟，而没有改变小沟的表面。这项研究揭示的TFIID不同寻常的DNA结合特性对TFIID的特异性和功能具有重要意义，更普遍地说，对DNA结合蛋白的序列特异性识别也具有重要意义。
