Open AccessSpecies-specific interaction of the glutamine-rich activation domains of Sp1 with the TATA box-binding protein.
Author(s) -
Andrew Emili,
Jack Greenblatt,
C J Ingles
Publication year - 1994
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.14.3.1582
Subject(s) - biology , tata binding protein , saccharomyces cerevisiae , transcription factor , glutamine , tata box binding protein , tata box , biochemistry , microbiology and biotechnology , protein–protein interaction , transcription (linguistics) , conserved sequence , dna binding protein , antennapedia , plasma protein binding , yeast , peptide sequence , amino acid , promoter , gene , gene expression , linguistics , philosophy , homeobox
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.