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Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes TBP, the TATA-binding protein. A distinctive feature of TBP is a long string of glutamines in the N-terminal. This region of the protein modulates the DNA binding activity of the C terminus, and modulation of DNA binding affects the rate of transcription complex formation and initiation of transcription. Mutations that expand the number of CAG repeats encoding this polyglutamine tract, and thus increase the length of the polyglutamine string, are associated with spinocerebellar ataxia 17, a neurodegenerative disorder classified as a polyglutamine disease. Analysis of Spinocerebellar ataxia type 17 (SCA17) locus in a group of ataxic patients excluded on other known SCAs. Data show that TATA-binding protein labelling was relatively more abundant than huntingtin labelling in the brains of Huntington disease patients, and increased with the grade of the disease. Data show that human TATA box binding protein (TBP) can use a shared surface to interact with two different transcription factor IIB (TFIIB) family members to initiate transcription by different RNA polymerases. Data suggest that the accumulation or misfolding of the polyQ-containing TATA binding protein may be a contributing factor in Alzheimer's disease. Developmental specificity of recruitment of TBP to the TATA box of the human gamma-globin gene. Human papillomavirus-16 E7 protein inhibits the DNA interaction of the TATA binding transcription factor. NC2 controls TBP binding and maintenance on DNA that is largely independent of a canonical TATA sequence. Our data provides biochemical evidence that Mediator functions by facilitating activator-mediated recruitment of pol II and also promoter recognition by TBP, both of which can occur in the absence of TBP-associated factors in TFIID. Results present the X-ray structures of human and yeast TATA box-binding protein /transcription factor IIA/DNA complexes at 2.1A and 1.9A resolution, respectively. Sequence-dependent solution structure and motions of TBP complexes were studied. TBP binds to ZNF76, allowing it to function as a transcriptional repressor. TBP can bind the TATA box through a regulated two-step mechanism, involving a transition from unbent complex to bent complex. TBP expression is elevated in human colon carcinomas relative to normal colon epithelium. Both Ras-dependent and Ras-independent mechanisms mediate increases in TBP expression in colon carcinoma cell lines. We report on the clinical manifestation of spinocerebellar ataxia 17 (SCA17) in 3 members of a German family, in whom the pathological repeat expansion in the TATA-binding protein gene ranged from 53 to 55 repeats. Abnormal expansions of an allele in SCA8 and SCA17 genes were detected in patients with both Parkinson's disease and spinocerebellar ataxia. An induced-fit mechanism gives structure to the glucocorticoid receptor AF1 domain when it encounters TATA box binding protein. Constitutive association of TBP with mitotic chromosomes. Genotype-phenotype correlations in white patients with Huntington's disease-like phenotype. In addition to its role in regulating TBP binding to a TATA box, the TBP surface is unexpectedly involved in TBP association with all three TFIIB family members. P300 plays a role in formation of the TBP-TFIIA-containing basal transcription complex, TAC. Physical cooperation between BTAF1 and NC2alpha in TBP regulation. Simultaneously binds and bends promoter DNA without a slow isomerization step or TFIIB requirement. Spatial positioning of the DNA-bound activation domain is important for efficient activation, possibly by maximizing its interactions with the transcriptional machinery including the TBP-TFIIA-TFIIB-promoter quaternary complex. The function of NRL-MTD is to activate transcription by recruiting or stabilizing TBP (and consequently other components of the general transcription complex) at the promoter of target genes.
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