How proteins recognize the TATA box.

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

doi:10.1006/jmbi.1996.0456

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How proteins recognize the TATA box.

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

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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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Amino Acid Sequence Base Sequence Crystallography, X-Ray DNA DNA-Binding Proteins Humans Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Binding Protein Conformation TATA Box TATA-Box Binding Protein Transcription Factors Journal Article Research Support, U.S. Gov't, P.H.S.

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Z S Juo, T K Chiu, P M Leiberman, I Baikalov, A J Berk, R E Dickerson. 1996-08-16. How proteins recognize the TATA box.. https://doi.org/10.1006/jmbi.1996.0456

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