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J. Biol. Chem., Vol. 276, Issue 20, 17181-17189, May 18, 2001

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Identification of Amino Acid Residues in the ETS Transcription Factor Erg That Mediate Erg-Jun/Fos-DNA Ternary Complex Formation^*

Alexis Verger, Eric Buisine^§¶, Séverine Carrère, René Wintjens^§, Anne Flourens, Jean Coll, Dominique Stéhelin, and Martine Duterque-Coquillaud^**

From the  CNRS Unité Mixte de Recherche 8526, Institut de Biologie de Lille, B.P. 447, 1 rue Calmette, 59021 Lille Cedex, ^§ CNRS UMR 8525, Institut Pasteur de Lille, Institut de Biologie de Lille, B.P. 447, 1 rue Calmette, 59021 Lille Cedex, ^¶ Faculté de Pharmacie, Université de Lille II, 3 rue du Professeur Laguesse, 59006 Lille, and  CNRS UMR 8527, Institut de Biologie de Lille, B.P. 447, 1 rue du professeur Calmette, 59021 Lille Cedex, France

Jun, Fos, and Ets proteins belong to distinct families of transcription factors that target specific DNA elements often found jointly in gene promoters. Physical and functional interactions between these families play important roles in modulating gene expression. Previous studies have demonstrated a direct interaction between the DNA-binding domains of the two partners. However, the molecular details of the interactions have not been investigated so far. Here we used the known three-dimensional structures of the ETS DNA-binding domain and Jun/Fos heterodimer to model an ETS-Jun/Fos-DNA ternary complex. Docking procedures suggested that certain ETS domain residues in the DNA recognition helix ₃ interact with the N-terminal basic domain of Jun. To support the model, different Erg ETS domain mutants were obtained by deletion or by single amino acid substitutions and were tested for their ability to mediate DNA binding, Erg-Jun/Fos complex formation, and transcriptional activation. We identified point mutations that affect both the DNA binding properties of Erg and its physical interaction with Jun (R367K), as well as mutations that essentially prevent transcriptional synergy with the Jun/Fos heterodimer (Y371V). These results provide a framework of the ETS/bZIP interaction linked to the manifestation of functional activity in gene regulation.

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