dTAFII60, TAFII60, Taf60, dTAFII62, TFIID
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.46
None of the polypeptides share 100% sequence identity.
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 Taf1.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Taf6 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Taf6 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.
The N-terminal domain of the Taf6 protein is necessary and sufficient to stabilize TFIID.
Interacts, 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.
The products of the Taf4 and Taf6 loci serve as coactivators to mediate transcriptional activation by the bcd and hb enhancer binding proteins. A quadruple complex containing Tbp, Taf1, Taf4 and Taf6 mediates transcriptional synergism by bcd and hb, whereas triple Tbp-Taf complexes lacking one or other coactivator failed to support synergistic activation. The concerted action of multiple regulators with different coactivators helps to establish the pattern and level of segmentation gene transcription during development.
Both of the Taf4 and Taf6 coactivators are required for bcd to recruit the Tbp-Taf complex to the promoter and direct synergistic activation of transcription. Contact between multiple activation domains for bcd and different targets within the TfIID complex can mediate transcriptional synergism.
Mutagenesis studies in combination with protein binding experiments and reconstituted transcription reactions identified two independent activation domains of bcd that target different coactivator subunits (Taf4 and Taf6).
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.