The interaction of the hnRNP family member E1B-AP5 with p53

Paola Barral, A Rusch, Andrew Turnell, Phillip Gallimore, Philip Byrd, T Dobner, Roger Grand

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17 Citations (Scopus)


Adenovirus early region 1B-associated protein 5, E1B-AP5, a member of the heterogeneous nuclear ribonucleoprotein (hnRNP) family, was originally isolated on the basis of its ability to bind to the adenovirus 5 early region1B55K protein. Here, it has been demonstrated that E1B-AP5 interacts with mutant and wild-type p53 from human cells in pull-down assays using GST-E1B-AP5. This interaction has been confirmed by co-immunoprecipitation studies and pull-down experiments with in vitro translated E1B-AP5 and GST-p53. The binding site for E1B-AP5 has been mapped to the C-terminal region of p53. In reciprocal experiments, it has been shown that several regions of E1B-AP5 bound to p53 although it is probable that a major site of interaction is located between amino acids 395 and 732 of E1B-AP5. In reporter assays, E1B-AP5 inhibited p53 transcriptional activity although not as efficiently as the Ad5E1B55K protein. Transfection of E1B-AP5 into human tumour cells affected the cellular response to UV radiation, such that, although p53 expression was induced, little change in the level of p53-inducible genes could be observed.
Original languageEnglish
Pages (from-to)2752-2758
Number of pages7
JournalFEBS Letters
Publication statusPublished - 23 May 2005


  • hnRNP
  • p53
  • adenovirus E1B 55K protein
  • E1B-AP5


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