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Vol. 13, No. 24, pp. 3217-3230, December 15, 1999
1 Laboratories of Molecular Biophysics, Howard Hughes
Medical Institute, The Rockefeller University, New York, New York 10021 USA; 2 Departments of Internal Medicine and Biochemistry,
Ryburn Cardiology Center, University of Texas Southwestern Medical
Center, Dallas, Texas 75235-8573 USA
Cocrystal structures of wild-type TATA box-binding protein (TBP)
recognizing 10 naturally occurring TATA elements have been determined
at 2.3-1.8 Å resolution, and compared with our 1.9 Å resolution
structure of TBP bound to the Adenovirus major late promoter (AdMLP)
TATA box (5'-TATAAAAG-3'). Minor-groove recognition by the
saddle-shaped protein induces the same conformational change in each of
these oligonucleotides, despite variations in promoter sequence that
reduce the efficiency of transcription initiation. Three molecular
mechanisms explain assembly of diverse TBP-TATA element complexes. (1)
T 
A and A T transversions leave the minor-groove face
unchanged, permitting formation of TBP-DNA complexes on many
A/T-rich core promoter sequences. (2) Cavities in the interface between TBP and the minor-groove face of the AdMLP TATA box
accommodate the exocyclic NH2 groups of G in a
TACA box and in a TATAAG box. (3) Formation of
a C:G Hoogsteen basepair in a TATAAAC box eliminates steric
clashes that would be produced by the Watson-Crick base pair. We
conclude that the structure of the TBP-TATA box complex found at the
heart of the polymerase II (pol II) transcription machinery has
remained constant over the course of evolution, despite variations in
TBP and its DNA targets.
[Key Words: TATA box; transcription; TBP-TATA complex; Pol II]
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