Abstract
The Epstein-Barr virus nuclear antigen 2 (EBNA2) protein activates the expression of viral and cellular genes. A set of seven yeast GAL4-EBNA2 fusion proteins were constructed in order to identify the transactivation domain of EBNA2. These fusion proteins were tested for their ability to transactivate a target gene in Hela and BJAB cells. This analysis has demonstrated that the EBNA2 polyproline domain is dispensable for transactivation while the acidic carboxy terminus defined by amino acids 337-467 is essential. This result is consistent with the analysis of a variety of viral and cellular eucaryotic transactivators in which an acidic domain of the protein has been shown to be indispensible for function.
Published Version
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