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

David Baillat, Clélia Laitem, Gabriel Leprivier, Charline Margerin, Marc Aumercier

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)213-217
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Jan 9 2009
Externally publishedYes


  • Cooperative binding
  • Ets-1
  • Oncogene
  • Surface plasmon resonance
  • Transcriptional regulation
  • p53 promoter

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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