Interacting domains of E2F1, DP1, and the adenovirus E4 protein.

摘要: Recent experiments demonstrate that a family of related proteins constitute the E2F transcription factor activity and interaction two these gene products, E2F1 DP1, generates heterodimer with DNA binding transcriptional activating capacity. Previous have shown adenovirus E4 19-kDa protein facilitates formation stable dimer on E2 promoter. We now show coexpression DP1 products in transfected SAOS-2 cells, together product, multicomponent complex specificity to Using yeast two-hybrid assay system, we find hydrophobic heptad repeat (E2F1 amino acid residues 206 283) allows corresponding domain (amino acids 196 245). also interacts domain, but could not detect direct between E4. Additional assays can dimerize. Since our previous mutations within element abolish E4-mediated enhancement transfection assays, conclude likely E2F1-DP1 by directly product. As consequence ability dimerize, propose formed sites promoter is composed heterodimers held an dimer.