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Ets-1 binds cooperatively to the palindromic Ets-binding sites in the p53 promoter

Due to its autoinhibition for DNA binding, the Ets-1 transcription factor must interact with partners to enhance its affinity for DNA. In a study on the stromelysin-1 promoter, we showed that Ets-1 binds cooperatively to two Ets-binding sites (EBS) organized in palindrome, thereby circumventing the...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2009-01, Vol.378 (2), p.213-217
Main Authors: Baillat, David, Laitem, Clélia, Leprivier, Gabriel, Margerin, Charline, Aumercier, Marc
Format: Article
Language:English
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Summary:Due to its autoinhibition for DNA binding, the Ets-1 transcription factor must interact with partners to enhance its affinity for DNA. In a study on the stromelysin-1 promoter, we showed that Ets-1 binds cooperatively to two Ets-binding sites (EBS) organized in palindrome, thereby circumventing the need for a binding partner to counteract autoinhibition. This leads to the formation of an Ets-1–DNA–Ets-1 ternary complex necessary for promoter activation. Here we show that Ets-1 also binds cooperatively to the EBS palindrome of the human p53 promoter, despite the presence of a degenerate EBS to which Ets-1 cannot otherwise bind. Transcriptional transactivation through this palindrome fully correlates to Ets-1 binding. Thus, the cooperative binding model that we initially proposed for the stromelysin-1 promoter may be a general mechanism of Ets-1 binding to palindromic EBS separated by 4 bp and a way to counteract binding site degeneracy.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2008.11.035