We compared the sequence-specific DNA binding properties of the proteins encoded by the murine homolog of the ets-1 proto-oncogene and two ets-related genes, murine PU. 1 and Drosophila E74. The protein products of these genes share sequence similarity within a region of-85 amino acids that we propose to call the ETS-domain. This amino acid sequence similarity, combined with the observation that these proteins bind similar DNA sequences, provides the basis for our proposal that the ETS-domain defines a new family of eukaryotic DNA-binding proteins.

The proto-oncogene ets-1 was discovered first as one of two cellular sequences transduced by the avian retrovirus E26. Chicken ets-1 and myb gene sequences are fused to gag sequences to form the tripartite E26 oncogene (Leprinee et al. 1983; Nunn et al. 1983). The ets portion of this oncogene is required for the induction of erythroblastosis in infected chickens (Nunn and Hunter 1989) and also appears to affect the myeloid transformation process (Golay et al. 1988). Over the last five years, a variety of genes have been described whose protein products have predicted amino acid sequences that show strong similarity with that of the avian ets-1 proto-oncogene. These include human ets-1 (Watson et al. 1988}, murine ets-1 {Gunther et al. 1990}, ets-2 (murine, human: Watson et al. 1988; avian: Boulukos et al. 1988), human erg (Reddy et al. 1987),