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

Retinoids play a fundamental role in regulating normal cell proliferation and differentiation. The most spectacular effects of retinoids in vitro can be observed with embryonal carcinoma (EC) cells that can be induced to differentiate into endodermal, mesodermal and neuroectodermal lineages. An early and essential step in the differentiation process is the activation of the retinoic acid receptor-beta 2 (RAR beta 2) promoter that requires a co-operation between RAR, the EC-cell specific adenovirus early gene product 1A (E1A)-like activity and the TATA-binding protein (TBP). In differentiated cells, this signalling pathway can be mimicked by ectopic expression of the adenoviral E1A protein. Here we show that E1A13S but not E1A12S augments the level of transcription. Analysis of the binding kinetics of E1A13S to TBP by the surface plasmon resonance (SPR) technique reveals that the affinity of TBP for a consensus TATA-box sequence is significantly and specifically increased by E1A13S only. Intriguingly, a specific interaction can only be obtained with crude TBP overexpressed in HeLa cells via vaccinia virus as opposed to bacterially expressed TBP, suggesting a cofactor requirement for the interaction. Co-immunoprecipitation experiments show that E1A13S is an integral component of the RNA polymerase II-specific TBP-containing complex in adenovirus transformed embryonal kidney 293 cells. Taken together the results suggest that E1A13S mediates transcriptional activation by providing a physical bridge between TBP/transcription factor IID (TFIID) and retinoic acid receptor.
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PMID:Retinoid-dependent transcription: the RAR/RXR-TBP-EIA/EIA-LA connection. 897 43

Infection of HeLa cells with poliovirus leads to rapid shut-off of host cell transcription by RNA polymerase II. Previous results have suggested that both the basal transcription factor TBP (TATA-binding protein) and transcription activator proteins such as CREB (cyclic AMP-responsive element-binding protein) and Oct-1 (the octamer-binding factor) are cleaved by the viral-encoded protease, 3C(Pro). Here we demonstrate that the transcriptional activator (and tumor suppressor) p53 is degraded by the viral protease 3C both in vivo and in vitro. Unlike other transcription factors that are directly cleaved by 3C(pro), degradation of p53 requires a HeLa cell activity in addition to 3C(Pro). The degradation of p53 by 3C(Pro) does not appear to involve the ubiquitin pathway of protein degradation. Vaccinia virus infection of HeLa cells leads to inactivation of the cellular activity required for 3C(Pro)-mediated degradation of p53. The vaccinia-encoded protein (CrmA) is known to inhibit caspase I (ICE protease) that converts inactive IL-1beta to an active secreted form. Incubation of HeLa cells with caspase I inhibitor Z-VAD-fmk does not interfere with 3C(Pro)-mediated degradation of p53. The cellular activity present in extracts of HeLa cells can be fractionated through phosphocellulose. A partially purified fraction that elutes at 0.6 M KCl from phosphocellulose contains the activity that degrades p53 in a 3C(Pro)-dependent manner. These results suggest that both poliovirus-encoded protease 3C(Pro) and a cellular activity are required for the degradation of p53 observed in cells infected with poliovirus.
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PMID:Poliovirus 3C protease-mediated degradation of transcriptional activator p53 requires a cellular activity. 1187 95

Vaccinia virus replicates in the cytoplasm of the host cell and encodes its own RNA polymerase and transcription factors. The proteins that target the poxvirus RNA polymerase to intermediate- and late-class promoters have not been identified. In this study, representatives of the intermediate and late promoters were characterized at the nucleotide level to identify essential motifs. Both intermediate and late viral promoters are shown to have an essential element suggestive of TATA boxes, which are potential targets for the TATA-binding protein (TBP). Several approaches were used to test for TBP requirement in vaccinia virus transcription, including overexpression of TBP, expression of a dominant negative mutant of TBP, RNA interference, and expression of adenovirus E1A protein, which inactivates TBP. In each case, the results support an essential role for TBP in vaccinia virus intermediate- and late-gene transcription. These findings indicate that poxviruses have integrated TBP as a central feature into an otherwise heterologous transcription system. A model for transcriptional switching, in which both intermediate and late promoter elements are targeted by TBP that recruits viral transcription factors to assemble a functional complex on their cognate promoters and a dysfunctional, repressed complex on the other class, is proposed.
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PMID:Vaccinia virus intermediate and late promoter elements are targeted by the TATA-binding protein. 1680 84