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Science 29 September 1995: Vol. 269. no. 5232, pp. 1866 - 1869 DOI: 10.1126/science.7569926
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Articles
Science, Vol 269, Issue 5232, 1866-1869
Copyright © 1995 by American Association for the Advancement of Science
Modulation of transcription factor Ets-1 DNA binding: DNA-induced unfolding of an alpha helix
JM Petersen,
JJ Skalicky,
LW Donaldson,
LP McIntosh,
T Alber,
and
BJ Graves
Department of Oncological Sciences, University of Utah School of Medicine, Salt Lake City 84132, USA.
Conformational changes, including local protein folding, play important roles in protein-DNA interactions. Here, studies of the transcription factor Ets-1 provided evidence that local protein unfolding also can accompany DNA binding. Circular dichroism and partial proteolysis showed that the secondary structure of the Ets-1 DNA-binding domain is unchanged in the presence of DNA. In contrast, DNA allosterically induced the unfolding of an alpha helix that lies within a flanking region involved in the negative regulation of DNA binding. These findings suggest a structural basis for the intramolecular inhibition of DNA binding and a mechanism for the cooperative partnerships that are common features of many eukaryotic transcription factors.
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