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)

The herpesvirus saimiri open reading frame (ORF) 50 produces two transcripts. The first is spliced, contains a single intron, and is detected at early times during the productive cycle, whereas the second is expressed later and is produced from a promoter within the second exon. Analysis of their gene products has shown that they function as sequence specific transactivators. In this report, we demonstrate that the carboxy terminus of ORF 50b contains an activation domain which is essential for transactivation. This domain contains positionally conserved hydrophobic residues found in a number of activation domains, including the herpes simplex virus VP16 and the Epstein-Barr virus R proteins. Mutational analysis of this domain demonstrates that these conserved hydrophobic residues are essential for ORF 50 transactivation capability. Furthermore, this domain is required for the interaction between the ORF 50 proteins and the basal transcription factor TATA-binding protein.
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PMID:The activation domain of herpesvirus saimiri R protein interacts with the TATA-binding protein. 1055 85

A key component of the polymerase II transcription machinery is the transcription factor TFIID, a complex that contains the TATA-box binding protein and several (10-12) associated factors designated as TAFs (TBP-associated factors). ts13 cells, which contain a temperature-sensitive mutant in TAF250, the largest subunit of TFIID, exhibit promoter-specific defects in gene expression at the nonpermissive temperature, suggesting that individual TAFs are required for transcription of specific subsets of eukaryotic genes. Herpes simplex virus 1 (HSV-1) does not replicate in ts13 cells at the nonpermissive temperature, but the point at which the replicative process is blocked is not known. We used the TAF250 defect in ts13 cells to investigate the role of TAF250 in the expression of HSV-1 genes of each temporal class. At a low m.o.i., expression of most immediate-early mRNAs is reduced at the nonpermissive temperature, and consequently, there is little expression of early genes and no viral DNA replication. In contrast, at high m.o.i., expression of immediate-early genes is unaffected by the TAF250 defect and is not dependent on de novo viral protein synthesis. Early genes and early proteins are produced under these conditions, and viral DNA replication ensues, albeit at somewhat reduced levels. In contrast, late gene expression and late protein synthesis are severely restricted, even in the presence of appreciable viral DNA replication. Thus the lack of late protein synthesis is responsible for the inability of HSV-1 to replicate in ts13 cells at the nonpermissive temperature. Further, it appears that late viral gene expression may be preferentially inhibited by the TAF250 mutation in ts13 cells.
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PMID:Herpes simplex virus 1 late gene expression is preferentially inhibited during infection of the TAF250 mutant ts13 cell line. 1077 91

As a critical step of the preinitiation complex assembly in transcription, the general transcription factor TFIIB forms a complex with the TATA-box binding protein (TBP) bound to a promoter element. Transcriptional activators such as the herpes simplex virus VP16 facilitate this complex formation through conformational activation of TFIIB, a focal molecule of transcriptional initiation and activation. Here, we used fluorescence resonance energy transfer to investigate conformational states of human TFIIB fused to enhanced cyan fluorescent protein and enhanced yellow fluorescent protein at its N- and C-terminus, respectively. A significant reduction in fluorescence resonance energy transfer ratio was observed when this fusion protein, hereafter named CYIIB, was mixed with promoter-loaded TBP. The rate for the TFIIB-TBP-DNA complex formation is accelerated drastically by GAL4-VP16 and is also dependent on the type of promoter sequences. These results provide compelling evidence for a 'closed-to-open' conformational change of TFIIB upon binding to the TBP-DNA complex, which probably involves alternation of the spatial orientation between the N-terminal zinc ribbon domain and the C-terminal conserved core domain responsible for direct interactions with TBP and a DNA element.
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PMID:FRET evidence for a conformational change in TFIIB upon TBP-DNA binding. 1476 96

Models of mechanisms of transcriptional activation in eukaryotes frequently invoke direct interactions of transcriptional activation domains with target proteins including general transcription factors or coactivators such as chromatin modifying complexes. The potent transcriptional activation domain (AD) of the VP16 protein of herpes simplex virus has previously been shown to interact with several general transcription factors including the TATA-binding protein (TBP), TBP-associated factor 9 (TAF9), TFIIA, and TFIIB. In surface plasmon resonance assays, a module of the VP16 AD designated VP16C (residues 452-490) bound to TBP with an affinity notably stronger than to TAF9, TFIIA or TFIIB. Moreover, the interaction of VP16C with TBP correlated well with transcriptional activity for a panel of VP16C substitution variants. These results support models in which the interactions of ADs with TBP play an important role in transcriptional activation.
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PMID:Quantitative assessment of in vitro interactions implicates TATA-binding protein as a target of the VP16C transcriptional activation region. 1508 96

During infection by herpes simplex virus type 1 (HSV-1), the virion protein VP16 activates the transcription of viral immediate-early (IE) genes. Genetic and biochemical assays have shown that the potent transcriptional activation domain of VP16 can associate with general transcription factors and with chromatin-modifying coactivator proteins of several types. The latter interactions are particularly intriguing because previous reports indicate that HSV-1 DNA does not become nucleosomal during lytic infection. In the present work, chemical cross-linking and immunoprecipitation assays were used to probe the presence of activators, general transcription factors, and chromatin-modifying coactivators at IE gene promoters during infection of HeLa cells by wild-type HSV-1 and by RP5, a viral strain lacking the VP16 transcriptional activation domain. The presence of VP16 and Oct-1 at IE promoters did not depend on the activation domain. In contrast, association of RNA polymerase II, TATA-binding protein, histone acetyltransferases (p300 and CBP), and ATP-dependent remodeling proteins (BRG1 and hBRM) with IE gene promoters was observed in wild-type infections but was absent or reduced in cells infected by RP5. In contrast to the previous evidence for nonnucleosomal HSV-1 DNA, histone H3 was found associated with viral DNA at early times of infection. Interestingly, histone H3 was underrepresented on IE promoters in a manner dependent on the VP16 activation domain. Thus, the VP16 activation domain is responsible for recruiting general transcription factors and coactivators to IE promoters and also for dramatically reducing the association of histones with those promoters.
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PMID:VP16-dependent association of chromatin-modifying coactivators and underrepresentation of histones at immediate-early gene promoters during herpes simplex virus infection. 1533 1

Host RNA polymerase II (RNAP II) is responsible for viral transcription of the herpes simplex virus type 1 (HSV-1) genome and is relocalized to viral DNA replication compartments. Thus, we investigated whether TATA-binding protein (TBP) and TBP-associated factors (TAFs) are recruited to sites of viral transcription and replication and whether TBP/TAF expressions are influenced upon infection. The protein levels of TBP, hsTAF1/TAF(II)250, hsTAF4/TAF(II)135, and hsTAF5/TAF(II)100 were constant during the early phase of infection and started to decrease late during infection. Only for hsTAF7/TAF(II)55 we sometimes observed a decrease already at 4-8h postinfection (p.i.). Concomitantly with the relocalization of RNAP II, TBP and hsTAFs were redistributed to sites of viral DNA replication and transcription. In the absence of viral DNA replication TBP/hsTAFs were present in distinct nuclear dots, however, enlargement of the nuclear structures did not take place. Our results show that HSV-1 infection has no influence on the protein levels of TFIID components and leads to a redistribution of TBP and hsTAFs to prereplicative sites that enlarge to viral DNA replication compartments.
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PMID:TATA-binding protein and TBP-associated factors during herpes simplex virus type 1 infection: localization at viral DNA replication sites. 1627 Dec 77

The binding of herpes simplex virus type 1 ICP4, TATA-binding protein (TBP), and RNA polymerase II (polII) to the promoter regions of representative immediate-early (IE) (ICP0), early (E) (thymidine kinase [tk]), and late (L) (glycoprotein C [gC]) genes on the viral genome was examined as a function of time postinfection, viral DNA replication, cis-acting sites for TFIID in the tk and gC promoters, and genetic background of ICP4. The binding of TBP and polII to the IE ICP0 promoter was independent of the presence of ICP4, whereas the binding of TBP and polII to the tk and gC promoters occurred only when ICP4 also bound to the promoters, suggesting that the presence of ICP4 at the promoters of E and L genes in virus-infected cells is crucial for the formation of transcription complexes on these promoters. When the TATA box of the tk promoter or the initiator element (INR) of the gC promoter was mutated, a reduction in the amount of TBP and polII binding was observed. However, a reduction in the amount of ICP4 binding to the promoters was also observed, suggesting that the binding of TBP-containing complexes and ICP4 is cooperative. The binding of ICP4, TBP, and polII was also observed on the gC promoter at early times postinfection or when DNA synthesis was inhibited, suggesting that transcription complexes may be formed early on L promoters and that additional events or proteins are required for expression. The ability to form these early complexes on the gC promoter required the DNA-binding domain but in addition required the carboxyl-terminal 524 amino acids of ICP4, which is missing the virus n208. This region was not required to form TBP- and polII-containing complexes on the tk promoter. n208 activates E but not L genes during viral infection. These data suggest that a region of ICP4 may differentiate between forming TBP- and polII-containing complexes on E and L promoters.
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PMID:Binding of ICP4, TATA-binding protein, and RNA polymerase II to herpes simplex virus type 1 immediate-early, early, and late promoters in virus-infected cells. 1809 62


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