Identification of a novel SNF2/SWI2 protein family member, SRCAP, which interacts with CREB-binding protein

The ability of cAMP response-element binding protein (CREB)-binding protein (CBP) to function as a co-activator for a number of transcription factors appears to be mediated by its ability to act as a histone acetyltransferase and through its interaction with a number of other proteins (general trans cription factors, histone acetyltransferases, and other co-activators). Her e we report that CBP also interacts with a novelATPase termed Snf2-Related CBP Activator Protein (SRCAP). Consistent with this activity, SRCAP contain s the conserved ATPase domain found within members of the Snf2 family. Tran sfection experiments demonstrate that SRCAP is able to activate transcripti on when expressed as a Gal-SRCAP chimera and that SRCAP also enhances the a bility of CBP to activate transcription. The adenoviral protein E1A was fou nd to disrupt interaction between SRCAP and CBP possibly representing a mec hanism for E1A-mediated transcriptional repression.