Species-specific interaction of the glutamine-rich activation domains of Sp1 with the TATA box-binding protein.

AUTOR(ES)

Emili, A

RESUMO

We have used protein-blotting and protein affinity chromatography to demonstrate that each of the two glutamine-rich activation domains of the human transcription factor Sp1 can bind specifically and directly to the C-terminal evolutionarily conserved domain of the human TATA box-binding protein (TBP). These activation domains of Sp1 also bind directly to Drosophila TBP but bind much less strongly to TBP from the yeast Saccharomyces cerevisiae. The abilities of the Sp1 activation domains to interact directly with the TBPs of various species correlate well with their abilities to activate transcription in extracts derived from the same species. We also show that a glutamine-rich transcriptional activating region of the Drosophila protein Antennapedia binds directly to TBP in a species-specific manner that reflects its ability to activate transcription in vivo. These results support the notion that TBP is a direct and important target of glutamine-rich transcriptional activators.

Documentos Relacionados

• The glutamine-rich activation domains of human Sp1 do not stimulate transcription in Saccharomyces cerevisiae.
• Sp1 activation of a TATA-less promoter requires a species-specific interaction involving transcription factor IID.
• An inhibitor domain in Sp3 regulates its glutamine-rich activation domains.
• Does TATA matter? A structural exploration of the selectivity determinants in its complexes with TATA box-binding protein.
• Properties of a CCAAT box-binding protein.