The interaction of the hnRNP family member E1B-AP5 with p53.
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.
Barral
Paola M
PM
Cancer Research UK Institute for Cancer Studies, University of Birmingham.
Rusch
André
A
Turnell
Andrew S
AS
Gallimore
Phillip H
PH
Byrd
Philip J
PJ
Dobner
Thomas
T
Grand
Roger J A
RJ
D001665:Binding Sites; D045744:Cell Line, Tumor; D034441:Heterogeneous-Nuclear Ribonucleoproteins / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*; D014466:Ultraviolet Rays
D034441:Heterogeneous-Nuclear Ribonucleoproteins; D016159:Tumor Suppressor Protein p53