Complete putative metal finger and leucine zipper structures of CRE-BP1 are required for the E1A-induced trans-activation.
The adenovirus E1A protein stimulates transcription of various genes. Recent experiments using a fusion protein have shown that E1A can function through a specific CRE (cyclic AMP response element)-binding protein, CRE-BP1 (also designated ATF-2), which stimulates the transcription from a CRE-containing promoter by homodimer formation or heterodimer formation with c-Jun. In this paper, the functional domains required for mediation of the E1A-induced trans-activation were analyzed using deletion and point mutants of CRE-BP1. The mutation in the putative metal finger structure or leucine zipper structure completely abolished the ability of CRE-BP1 to mediate the E1A-induced trans-activation. Furthermore, overexpression of CRE-BP1 or c-Jun interfered with the E1A-induced trans-activation. These results suggest that the complete putative metal finger structure in the N-terminal region of CRE-BP1 plays an important role for the E1A-induced trans-activation, and the heterodimer of CRE-BP1 with the unidentified protein participates in the interaction with E1A.[1]References
- Complete putative metal finger and leucine zipper structures of CRE-BP1 are required for the E1A-induced trans-activation. Zu, Y.L., Maekawa, T., Matsuda, S., Ishii, S. J. Biol. Chem. (1991) [Pubmed]
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