The DP proteins are components of the E2F transcription factor. They form heterodimers with the E2F proteins and these complexes bind efficiently to E2F response elements in promoters of genes that are involved in cell cycle regulation. The properties of the DP proteins are less documented than those of their E2F counterpart and the present work was aimed at characterizing avian DP genes (named chDP) and their products. Here we describe the cloning of the chicken homologues of the mammalian DP-1 and DP-2 proteins. This work also suggests that DP-2 isoforms have an additional 60 amino acid extension at the N-terminus compared to its human counterpart. Gel-shift assays and coimmunoprecipitation show that both DP-1 and DP-2 dimerize to chE2F-1 and activate transcription efficiently, as demonstrated by transient expression assays. However, contrary to the expression patterns exhibited by E2F-1 during the cell cycle or during neuroretina development, DP member's expression appears more invariant, suggesting that E2F activity is limited by the availability of the E2F proteins.