FB2020_06, released Dec 22, 2020
Gene: Dmel\Taf6
FB2020_06, released Dec 22, 2020
Gene: Dmel\Taf6
Gene: Dmel\Taf6
Gene: Dmel\Taf6
dTAFII60, TAFII60, Taf60, dTAFII62, TFIID
Please see the JBrowse view of Dmel\Taf6 for information on other features
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Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.46
2.0 (longest cDNA)
2.1 (unknown)
None of the polypeptides share 100% sequence identity.
592 (aa); 64 (kD predicted)
60 (kD)
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.
Comment: maternally deposited
GBrowse - Visual display of RNA-Seq signals
View Dmel\Taf6 in GBrowse 2
3-45
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
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.
Identified on the basis of genetic interaction with Ras85DV12.sev.
Taf6 does not exhibit histone acetyltransferase (HAT) activity in vitro.
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.
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.
