How proteins recognize the TATA box
How proteins recognize the TATA box
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DOI：
10.1006/jmbi.1996.0456
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发表时间：
1996-08-16
影响因子：
5.6
通讯作者：
Dickerson, RE
中科院分区：
文献类型：
--
作者：
Juo, ZS;Chiu, TK;Dickerson, RE
已经解决了人TATA结合蛋白与TATA序列DNA的复合体的晶体结构，补充了早期来自酿酒酵母和拟南芥的TBP/DNA分析。通过考虑TBP/DNA复合体，而不是作为一个与DNA结合的蛋白质分子，而是作为一个具有特别大的小凹槽配体的DNA双链，提供了对TATA盒特异性的特殊见解。这一观点解释了：(1)为什么需要T-A碱基对，而不是C-G；(2)为什么需要T和A碱基的交替；(3)TBP如何识别TATA盒的上游和下游末端，以便正确结合；以及(4)为什么TATA盒的后半部分可能比前半部分更可变。(C)1996年学术出版社有限公司
The crystal structure of a complex of human TATA-binding protein with TATA-sequence DNA has been solved, complementing earlier TBP/DNA analyses from Saccharomyces cerevisiae and Arabidopsis thaliana. Special insight into TATA box specificity is provided by considering the TBP/DNA complex, not as a protein molecule with bound DNA, but as a DNA duplex with a particularly large minor groove ligand. This point of view provides explanations for: (1) why T-A base-pairs are required rather than C-G; (2) why an alternation of T and A bases is needed; (3) how TBP recognizes the upstream and downstream ends of the TATA box in order to bind properly; and (4) why the second half of the TATA box can be more variable than the first. (C) 1996 Academic Press Limited