The adenovirus E4-6/7 protein transactivates the E2 promoter by inducing dimerization of a heteromeric E2F complex.
作者： S Obert , R J O'Connor , S Schmid , P Hearing
关键词: E2F 、 Biology 、 Mutant 、 Transcription factor 、 Transactivation 、 Mutant protein 、 Binding protein 、 Molecular biology 、 Binding site 、 Immunoprecipitation
摘要: Abstract Binding of the mammalian transcription factor E2F to adenovirus E2a early promoter is modulated through interaction with viral E4-6/7 protein. induces cooperative and stable binding in vitro two correctly spaced inverted sites (E2F induction) by physical protein-DNA complex. The transactivated vivo product. C-terminal 70 amino acids are necessary sufficient for induction transactivation. To assess mechanism(s) transactivation protein, we have analyzed a series point mutants functional domain E4-6/7. Two distinct segments required E2F. Additionally, mutant phenylalanine-to-proline substitution at acid 125 (F-125-P) efficiently interacts but does not induce defective Induction complex formation F-125-P protein restored divalent E4-6/7-specific monoclonal antibodies, monovalent Fab fragment, or appending heterologous dimerization N terminus These other data support involvement promoter. We present evidence that least cellular components involved DNA activity both recently cloned E2F-related activities E2F-1 DP-1 individually bind an site weakly, when combined generate indistinguishable from endogenous Recombinant E2F-1, DP-1, form induced
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