Functional domains of template-activating factor-I as a protein phosphatase 2A inhibitor

Template-Activating Factor-I (TAF-I) alpha and beta, chromatin remodeling factors, were identified as the stimulatory factor for replication of the adenovirus DNA complexed with viral basic core proteins. Recently, two cellular inhibitors for protein phosphatase 2A (PP2A) have been isolated. One of these inhibitors, designated IPP2A2, is a truncated version of TAF-Ibeta. Here, it is shown using recombinant TAF-I proteins that both TAF-Ialpha and beta have the PP2A inhibitor activity. The N-terminal region but not the C-terminal acidic region, the latter of which is essential for the chromatin remodeling activity, is shown to be required for the PP2A inhibitor activity. Roles of TAF-Ialpha- and beta-specific regions, the C-terminal acidic region, and other regions of TAF-I for the PP2A inhibitor activity are also discussed.