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Nucleic Acids Research, Vol 24, Issue 17 3283-3288, Copyright © 1996 by Oxford University Press

ARTICLES

In the TTF-1 homeodomain the contribution of several amino acids to DNA recognition depends on the bound sequence

D Fabbro, G Tell, A Leonardi, L Pellizzari, C Pucillo, R Lonigro, S Formisano and G Damante

The thyroid transcription factor-1 homeodomain (TTF-1HD) shows a peculiar DNA binding specificity, preferentially recognizing sequences containing the 5'-CAAG-3' core motif. Most other homeodomains instead recognize sites containing the 5'-TAAT-3' core motif. Here, we show that TTF-1HD efficiently recognizes another sequence, called D1, devoid of the 5'-CAAG-3' core motif. Different experimental approaches indicate that TTF-1HD contacts the D1 sequence in a manner which is different to that used to interact with sequences containing the 5'- CAAG-3' core motif. The binding activities that mutants of TTF-1HD display with the D1 sequence or with the sequence containing the 5'- CAAG-3' core motif indicate that the role of several DNA-contacting amino acids is different. In particular, during recognition of the D1 sequence, backbone-interacting amino acids not relevant in binding to sequences containing the 5'-CAAG-3' core motif play an important role. In the TTF-1HD, therefore, the contribution of several amino acids to DNA recognition depends on the bound sequence. These data indicate that although a common bonding network exists in all of the HD/DNA complexes, peculiarities important for DNA recognition may occur in single cases.
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M. I. Ramirez, A. K. Rishi, Y. X. Cao, and M. C. Williams
TGT3, Thyroid Transcription Factor I, and Sp1 Elements Regulate Transcriptional Activity of the 1.3-Kilobase Pair Promoter of T1alpha , a Lung Alveolar Type I Cell Gene
J. Biol. Chem., October 17, 1997; 272(42): 26285 - 26294.
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