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J Biol Chem, Vol. 273, Issue 8, 4563-4568, February 20, 1998
From the Department of Biochemistry, Albert Einstein College of
Medicine, Bronx, New York 10461
We have conducted a quantitative thermodynamic
study of the effects of the TATA element and TATA-flanking sequences on
the assembly of complexes containing TATA-binding protein (TBP) and the
TFIIB-related factor, TFIIIB70. TBP binds to the
sequence TATAAAAG in the context of the yeast U6 gene (yU6 hybrid TATA) or the adenovirus major late promoter (AdMLP) with different affinities demonstrating that the sequence context of a TATA element contributes to TBP binding. We also determined the cooperative free energies of
formation of TBP·TFIIIB70·DNA complexes on the yU6 TATA
element, the yU6 hybrid TATA element and a nonconsensus TATA element.
The yU6 hybrid TATA displayed a moderate, less than 5-fold, increase in
TBP affinity similar to the 3-fold increase observed for the AdMLP. In
contrast, the nonconsensus and yU6 TATAs increased the affinity of TBP
for DNA 12- and 17-fold, respectively. Since the TBP-TFIIIB70 cooperativity is greater on lower affinity
TATA boxes and most polymerase III genes contain low affinity "TATA
boxes," we conclude that the cooperative binding of
TFIIIB70 and TBP to DNA represents an important driving
force in the assembly of polymerase III-specific transcription
complexes. An effect of the sequences surrounding the TATA box was also
observed on TBP-TFIIIB70 cooperativity. The mechanistic
implications of the thermodynamic linkage between DNA sequence and
binding cooperativity are discussed.
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