How Proteins Recognize the TATA Box

Z. Sean Juo(University of California, Los Angeles), Thang Kien Chiu(University of California, Los Angeles), Paul M. Leiberman(University of California, Los Angeles), Igor Baikalov(University of California, Los Angeles), Arnold Berk(University of California, Los Angeles), Richard E. Dickerson(University of California, Los Angeles)
Journal of Molecular Biology
August 1, 1996
10.1006/jmbi.1996.0456
Cited by 305Open Access
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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.

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