Delta-crystallin enhancer binding protein delta EF1 is a zinc finger-homeodomain protein implicated in postgastrulation embryogenesis.

We investigated nuclear factors that bind to delta 1-crystallin enhancer core and regulate lens-specific transcription. A nuclear factor delta EF1, which binds to the essential element of the delta 1-crystallin enhancer core, was molecularly cloned from the chicken by a southwestern method. The protein organization of delta EF1 deduced from the cDNA sequence indicated that it has heterogeneous domains for DNA-binding, two widely separated zinc fingers and a homeodomain, analogous to Drosophila ZFH-1 protein. The C-terminal zinc fingers were found to be responsible for binding to the delta 1-crystallin enhancer core sequence. delta EF1 had proline-rich and acidic domains common to various transcriptional activators. During embryogenesis, delta EF1 expression was observed in the postgastrulation period in mesodermal tissues; initially, in the notochord, followed by somites, nephrotomes and other components. The expression level changed dynamically in a tissue, possibly reflecting the differentiation states of the constituent cells. Besides mesoderm, delta EF1 was expressed in the nervous system and the lens, but other ectodermal tissues and endoderm remained very low in delta EF1 expression. Cotransfection experiments indicated that this factor acts as a repressor of delta 1-crystallin enhancer. Possession of heterogeneous DNA-binding domains and its dynamic change of expression in embryogenesis strongly suggest that delta EF1 acts in multiple ways depending on the cell type and the gene under its regulation.