Transcription factors are protein molecules that bind to specific DNA sequences in the genome, resulting in the induction or inhibition of gene transcription [ PUBMED:2163347 ]. The ets oncogene is such a factor, possessing a region of 85-90 amino acids known as the ETS (erythroblast transformation specific) domain [ … expand

Transcription factors are protein molecules that bind to specific DNA sequences in the genome, resulting in the induction or inhibition of gene transcription [ PUBMED:2163347 ]. The ets oncogene is such a factor, possessing a region of 85-90 amino acids known as the ETS (erythroblast transformation specific) domain [ PUBMED:2163347 PUBMED:2253872 PUBMED:14693367 ]. This domain is rich in positively-charged and aromatic residues, and binds to purine-rich segments of DNA. The ETS domain has been identified in other transcription factors such as PU.1, human erg, human elf-1, human elk-1, GA binding protein, and a number of others [ PUBMED:2163347 PUBMED:2253872 PUBMED:8425553 ]. It is generally localized at the C terminus of the protein, with the exception of ELF-1, ELK-1, ELK-3, ELK-4 and ERF where it is found at the N terminus.

NMR-analysis of the structure of the Ets domains revealed that it contains three α-helices (1-3) and four-stranded β-sheets (1-4) arranged in the order α1-β1-β2-α2-α3-β3-β4 forming a winged helix-turn-helix (wHTH) topology [ PUBMED:12559563 ]. The third α-helix is responsive to contact to the major groove of the DNA. Different members of the Ets family proteins display distinct DNA binding specificities. The Ets domains and the flanking amino acid sequences of the proteins influence the binding affinity, and the alteration of a single amino acid in the Ets domain can change its DNA binding specificities.