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The E2F family of transcription factors play an important role in regulating cell cycle progression. We report here the characterization and functional properties of a new member of the human E2F family, referred to as E2F-7. E2F-7 has two separate DNA-binding domains, a feature that distinguishes E2F-7 from other mammalian E2F proteins, but resembling the organization of recently isolated E2F-like proteins from Arabidopsis. E2F-7 binds to DNA independently of a DP partner and delays cell cycle progression. Interestingly, E2F-7 modulates the transcription properties of other E2F proteins. A mutational analysis indicates that the integrity of both DNA-binding domains is required for cell cycle delay and transcriptional modulation. Biochemical results and protein modelling studies suggest that in binding to DNA interactions occur between the two DNA-binding domains, most probably as a homodimer, thereby mimicking the organization of an E2F/DP heterodimer. These structural and functional properties of E2F-7 imply a unique role in regulating cellular proliferation.

Original publication




Journal article



Publication Date





5138 - 5150


Amino Acid Motifs, Amino Acid Sequence, Binding Sites, Cell Cycle, Cell Line, Tumor, Cell Nucleus, Conserved Sequence, DNA-Binding Proteins, E2F7 Transcription Factor, Genes, Reporter, HeLa Cells, Humans, Luciferases, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Repressor Proteins, Sequence Homology, Amino Acid, Transcription Factors