Barral, P. M. and Rusch, Andre and Turnell, A. S. and Gallimore, P. H. and Byrd, P. J. and Dobner, Thomas and Grand, R. J. A. (2005) The interaction of the hnRNP family member E1B-AP5 with p53. FEBS LETTERS, 579 (13). pp. 2752-2758. ISSN 0014-5793,
Full text not available from this repository. (Request a copy)Abstract
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 tomour 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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NUCLEAR RIBONUCLEOPROTEIN E1B-AP5; TERMINAL DOMAIN; TRANSCRIPTIONAL ACTIVATION; CELLULAR-PROTEIN; ADENOVIRUS; BINDING; COMPLEX; TFIIH; TRANSACTIVATION; MODULATION; E1B-AP5; p53; hnRNP; adenovirus E1B 55K protein |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 11 May 2021 12:53 |
| Last Modified: | 11 May 2021 12:53 |
| URI: | https://pred.uni-regensburg.de/id/eprint/36124 |
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