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How proteins recognize the TATA box.

Juo ZS, Chiu TK, Leiberman PM, Baikalov I, Berk AJ, Dickerson RE
J Mol Biol 261 239-54 (1996)
Cited: 191 times
EuropePMC logo 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.

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Related citations provided by authors (2)

  1. 1.9 A Resolution Refined Structure of TBP Recognizing the Minor Groove of TATAAAAG. Kim JL, Burley SK Nat. Struct. Biol. 1 638- (1994)
  2. Co-Crystal Structure of TBP Recognizing the Minor Groove of a TATA Element. Kim JL, Nikolov DB, Burley SK Nature 365 520- (1993)

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