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Chapter category: Gene Expression

The ETS DNA-Binding Domain, Signature of the Family, Has Multiple Functions

Chapter authors:
Alexis Verger* and Martine Duterque-Coquillaud

The Ets family of transcription factors is characterized by an evolutionarily-conserved DNA-binding domain that recognizes a purine-rich GGAA/T sequence. Ets proteins perform a remarkable variety of roles in vertebrate development, either activating or repressing specific target genes through interaction with different partner proteins. Interestingly, these interactions are often mediated by the conserved ETS DNA-binding domain, raising questions as to how each factor’s specificity is achieved. In most cases, such as the ternary DNA complexes GABPa/b, Ets-1/AML-1 and Erg/Fos-Jun, protein-protein interactions facilitate cooperative DNA binding by both proteins but do not alter the DNA-binding specificity of the partner. In some cases, however, protein-protein contacts on DNA serve to modify the way in which one or both DNA-binding domains select suboptimal binding sequences. Examples of this type of cooperativity are seen in the Ets-1/Pax-5, Pu-1/IRF-4 and SAP-1/SRF or Elk-1/SRF complexes. Together, the examples described in this chapter reveal how the ETS domain, and particularly specific residues of the DNA recognition helix, are critical discriminators of the selection of both Ets interacting partners and suboptimal DNA binding motifs, allowing fine-tuning of transcriptional activity.

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