dTAFII250, dTAFII230, TAFII250, Taf250, TAFII230
component of the conserved general transcription factor TFIID - kinase and histone transacetylase activities - regulates transcription by binding the initiator element at transcription start sites and binding acetylated histones via its bromodomains
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 5.50
Annotated transcripts do not represent all possible combinations of alternative exons and/or alternative promoters.
Gene model reviewed during 5.55
Low-frequency RNA-Seq exon junction(s) not annotated.
6.552 (compiled cDNA)
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). Taf1 is the largest component of the TFIID complex. Interacts with Tbp, Taf2, Taf4 and Taf6.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Taf1 using the Feature Mapper tool.
Taf1 protein is first detected in mitotically profliferating spermatogonia at the apical tip of the testis. Taf1 levels increases in spermatocytes and reaches the highest levels in nuclei of spermatocytes undergoing growth in an extended pre-meiotic G2 phase. Upon entry into meiosis, expression is reduced and the Taf1 protein is dispersed throughout the cell. @Taf1 is dynamically localized within the nucleus during spermatogenesis and predominantly localizes to spermatocyte nucleoli.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Taf1 in GBrowse 2
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.
When dsRNA constructs are made and transiently transfected into S2 cells in RNAi experiments, an increase in the proportion of S phase cells, an increase in the proportion of G2/M phase cells, a decrease in mitotic index and a whole range of mitotic abnormalities are seen.
Taf1 is required in ovary, eye, ocelli, wing bristle and terminalia development and has a suggested role in regulating the cell cycle, cell differentiation, cell proliferation and cell survival.
Transcriptional regulation may involve, in part, competitive interactions between transcriptional activators and TAFs on the Tbp surface.
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.
In vitro expressed 'TAF110' interacts directly with the 'TAF250' which itself interacts with Tbp, a complex of all three is suggested. Binding study with various mutants of Taf1 suggests that both 'TAF110' and Tbp interact with the N-terminal 352-amino acid portion of 'TAF250'.