Functional analysis of hepatitis B virus transactivator X: implication of the leucine zipper-like region and C-terminal seven conserved amino acids in functional regions.

X protein of hepatitis B virus (HBV-X) is a transactivator to a wide variety of viral and cellular transcriptional regulatory elements. Since HBV-X does not act on a common cis-regulatory element of a wide variety of regulatory elements nor does it bind to DNA directly, it has been proposed that HBV-X acts indirectly through protein-protein interactions with other transcription factors or signal transducing pathway. In order to determine the functional domain of HBV-X, we have constructed and analyzed a number of deletion and site specific mutants. Our results showed that leucine zipper-like sequences were found in the C-terminal region of HBV-X and were very important for its transactivating activity. In the analysis of deletion mutants, seven conserved and strong basic amino acids (amino acids 135-141) were essential for the transactivating activity of HBV-X.