Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P20226 (TATA-binding protein)
 1,297 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have cloned cDNAs encoding three novel TAFIIs [TATA-binding protein (TBP)-associated factors] from the human (h) HeLa cell TFIID complexes hTAFII28, hTAFII20 and hTAFII18. hTAFII28 is a core hTAFII present in both of the previously described hTFIID species which either lack or contain hTAFII30 (hTFIID alpha and hTFIID beta respectively), and is the homologue of Drosophila (d)TAFII30 beta. hTAFII18 is a novel hTAFII which shows homology to the N-terminal region of the yeast TAFIISPT3, but has no known Drosophila counterpart. In contrast to hTAFII28, hTAFII18 is a TFIID beta-specific hTAFII. hTAFII20 is the homologue of p22, an alternatively spliced form of dTAFII30 alpha (p32). Using a combination of protein affinity chromatography and cotransfection and immunoprecipitation assays, we have identified a series of in vitro and intracellular interactions among the novel hTAFIIs and between the novel hTAFIIs and hTAFII30 or TBP. We show that hTAFII28 interacts with hTAFII18 both in vitro and intracellularly; in contrast to its Drosophila homologue, hTAFII28 also interacts directly with TBP. Deletion analysis indicates that TBP and hTAFII18 bind to distinct domains of hTAFII28. hTAFII18 also interacts with TBP, but it interacts more strongly with hTAFII28 and hTAFII30. The binding of hTAFII28 and hTAFII30 requires distinct domains of hTAFII18. As observed with the homologous Drosophila proteins, hTAFII20 interacts directly with TBP; however, additional interactions between hTAFII20 and hTAFII28 or hTAFII30 were detected. These results reveal differences not only in subunit composition, but also in the organization of dTFIID and hTFIID complexes.
 ...
PMID:Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID. 772 27

Initiation of transcription of most human genes transcribed by RNA polymerase II (RNAP II) requires the formation of a preinitiation complex comprising TFIIA, B, D, E, F, H and RNAP II. The general transcription factor TFIID is composed of the TATA-binding protein and up to 13 TBP-associated factors. During transcription of snRNA genes, RNAP II does not appear to make the transition to long-range productive elongation, as happens during transcription of protein-coding genes. In addition, recognition of the snRNA gene-type specific 3' box RNA processing element requires initiation from an snRNA gene promoter. These characteristics may, at least in part, be driven by factors recruited to the promoter. For example, differences in the complement of TAFs might result in differential recruitment of elongation and RNA processing factors. As precedent, it already has been shown that the promoters of some protein-coding genes do not recruit all the TAFs found in TFIID. Although TAF5 has been shown to be associated with RNAP II-transcribed snRNA genes, the full complement of TAFs associated with these genes has remained unclear. Here we show, using a ChIP and siRNA-mediated approach, that the TBP/TAF complex on snRNA genes differs from that found on protein-coding genes. Interestingly, the largest TAF, TAF1, and the core TAFs, TAF10 and TAF4, are not detected on snRNA genes. We propose that this snRNA gene-specific TAF subset plays a key role in gene type-specific control of expression.
 ...
PMID:A novel TBP-TAF complex on RNA polymerase II-transcribed snRNA genes. 2244 27

We isolated two TATA-binding protein-associated factor (TAF) genes, TAF10 and TAF13, from pepper (Capsicum annuum). The complete coding sequences were amplified using reverse transcriptase-PCR on the basis of conserved sequence information of eggplant and several other plant species. Nucleotide sequence analysis of these two genes revealed that the pepper TAF10 gene encodes a protein of 103 amino acids that belongs to the TAF10 superfamily. The pepper TAF10 gene was highly expressed in the pericarp and placenta, moderately expressed in the stems, flowers, seeds and leaves, and weakly expressed in roots. The TAF13 gene was found to encode a protein of 130 amino acids that belongs to the TAF13 superfamily. The TAF13 gene was highly expressed in the stems, flowers and pericarp, moderately expressed in the leaves, placenta and seeds, and weakly expressed in roots.
...
PMID:Cloning and bioinformatic analysis of full-length novel pepper (Capsicum annuum) genes TAF10 and TAF13. 2439 Oct 43

General transcription factor TFIID is a cornerstone of RNA polymerase II transcription initiation in eukaryotic cells. How human TFIID-a megadalton-sized multiprotein complex composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs)-assembles into a functional transcription factor is poorly understood. Here we describe a heterotrimeric TFIID subcomplex consisting of the TAF2, TAF8 and TAF10 proteins, which assembles in the cytoplasm. Using native mass spectrometry, we define the interactions between the TAFs and uncover a central role for TAF8 in nucleating the complex. X-ray crystallography reveals a non-canonical arrangement of the TAF8-TAF10 histone fold domains. TAF2 binds to multiple motifs within the TAF8 C-terminal region, and these interactions dictate TAF2 incorporation into a core-TFIID complex that exists in the nucleus. Our results provide evidence for a stepwise assembly pathway of nuclear holo-TFIID, regulated by nuclear import of preformed cytoplasmic submodules.
 ...
PMID:Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules. 2558 96