蛋白质如何识别TATA框。

How proteins recognize the TATA box.

作者信息

Juo Z S, Chiu T K, Leiberman P M, Baikalov I, Berk A J, Dickerson R E

机构信息

Molecular Biology Institute, University of California at Los Angeles 90095, USA.

出版信息

J Mol Biol. 1996 Aug 16;261(2):239-54. doi: 10.1006/jmbi.1996.0456.

DOI:10.1006/jmbi.1996.0456

PMID:8757291

Abstract

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.

摘要

人类TATA结合蛋白与TATA序列DNA复合物的晶体结构已得到解析，这对早期来自酿酒酵母和拟南芥的TBP/DNA分析起到了补充作用。通过将TBP/DNA复合物，不是看作一个结合了DNA的蛋白质分子，而是看作一个带有特别大的小沟配体的DNA双链体，能对TATA框特异性有特别深入的了解。这种观点为以下几点提供了解释：（1）为什么需要T.A碱基对而非C.G；（2）为什么需要T和A碱基交替；（3）TBP如何识别TATA框的上游和下游末端以便正确结合；以及（4）为什么TATA框的后半部分比前半部分更具变异性。