Interactions between adenovirus E1A and members of the AP-1 family of cellular transcription factors

K. Maguire, X. P. Shi, N. Horikoshi, M. Rosenberg, R. Weinmann, J. Rappaport

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


We have studied interactions between bacterially produced E1A linked to Sepharose and the various DNA-binding proteins present in HeLa cell nuclear extracts (NE). DNA-binding activities and cross-reactive polypeptides recognizing the cAMP-responsive element (CRE) and the activator protein 1 (AP1) sites were bound to the E1A column, whereas nuclear factor 1 (NF1) and the activator protein 2 (AP2) DNA-binding activities were not retained by E1A. The binding activities that were retained belonged to the CRE and JUN protein family, as judged by Western blot analysis. Authentic CRE-BP1, c-Jun and c-Fos proteins produced by in-vitro translation also bound to the E1A column. However, efficient binding of in-vitro-translated CRE-BP1 and c-Fos proteins to E1A required preincubation with NE. We show here that immobilized E1A sequesters several cellular upstream transcription activators, and suggest a role for members of the AP1 family of transcription factors in E1A-mediated gene regulation.

Original languageEnglish (US)
Pages (from-to)1417-1422
Number of pages6
Issue number8
StatePublished - 1991

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research


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