C-terminal domain (CTD) of RNA-polymerase II and N-terminal segment of the human TATA binding protein (TBP) can mediate remote and proximal transcriptional activation, respectively.

Activation domains of mammalian transcription factors can be subdivided into at least two functional classes. One, exemplified by the glutamine-rich activation domains of Oct and Sp1 factors, mediates transcriptional activation only from a proximal promoter position, and in response to an enhancer. The other, exemplified by the 'acidic' domain of the viral activator VP16, has the ability to activate from remote enhancer as well as from proximal promoter positions. Here we report that two proteins of the basal transcription apparatus also contain activation domains whose stimulatory effect can be detected in fusion proteins containing the GAL4 DNA binding domain. The human TATA-binding protein (TBP) contains at its N-terminus a domain with typical 'promoter' activity. We propose that the TBP N-terminal region acts as an auxiliary activation domain which reinforces the activity of other promoter-bound factors. The largest subunit of RNA polymerase II contains at its C-terminus a conserved heptad repeat structure (CTD). Both natural and synthetic CTD consensus repeats fused to GAL4 can activate transcription from remote positions like a typical enhancer-active domain. Accordingly we propose that the RNA polymerase II large subunit contains a 'portable' domain for transcriptional activation which may synergize with the activation domains of enhancer-bound transcription factors.