dTAFII40, e(y)1, dTAFII42, TAFII40, TFIID
Gene model reviewed during 5.51
There is only one protein coding transcript and one polypeptide associated with this gene
Belongs to the TFIID complex which is composed of TATA binding protein (Tbp) and a number of TBP-associated factors (TAFs). E(y)1 and Taf6 exist as a heterotetramer. Interacts with e(y)2.
The C-terminus is important for mediating interaction with e(y)2.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Taf9 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Taf9 in GBrowse 2
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
dsRNA has been made from templates generated with primers directed against this gene.
Does not interact, in vitro, with human thryroid-hormone receptor-β.
The amino terminal portions of e(y)1 and Taf6 adopt the canonical histone fold, consisting of two short α-helices flanking a long central α helix. e(y)1 and Taf6 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state the e(y)1/Taf6 complex exists as a heterotetramer, resembling the (His3/His4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.
TFIID subunit proteins and the Tbp protein can interact in pairwise combinations with several subunits in a network of interactions within TFIID.
A number of polypeptides (encoded by Taf1, Taf4, Taf5, Taf6, e(y)1 and Taf12) that are tightly associated with Tbp and are native TFIID components have been purified. Protein blotting experiments suggest that one of these proteins, Taf1, interacts directly with Tbp, while the association between Tbp and the other proteins is either weak or is an indirect association via Taf1.
The e(y)1 protein interacts directly with the Taf6 protein. Tbp, Taf1, Taf4 and Taf6 products can assemble into a mini-complex in vitro, showing that Taf6 and Taf4 occupy distinct binding sites on the C terminal part of Taf1.