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We began analyzing https://www.nature.com/articles/nn2011, but it redirected us to https://www.nature.com/articles/nn2011. The analysis below is for the second page.

Title[redir]:
Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration | Nature Neuroscience
Description:
Expansion of the polyglutamine (polyQ) tract in human TATA-box binding protein (TBP) causes the neurodegenerative disease spinocerebellar ataxia 17 (SCA17). It remains unclear how the polyQ tract regulates normal protein function and induces selective neuropathology in SCA17. We generated transgenic mice expressing polyQ-expanded TBP. These mice showed weight loss, progressive neurological symptoms and neurodegeneration before early death. Expanded polyQ tracts reduced TBP dimerization but enhanced the interaction of TBP with the general transcription factor IIB (TFIIB). In SCA17 transgenic mice, the small heat shock protein HSPB1, a potent neuroprotective factor, was downregulated, and TFIIB occupancy of the Hspb1 promoter was decreased. Overexpression of HSPB1 or TFIIB alleviated mutant TBP-induced neuritic defects. These findings implicate the polyQ domain of TBP in transcriptional regulation and provide insight into the molecular pathogenesis of SCA17.

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Keywords {🔍}

article, google, scholar, cas, nature, protein, sca, access, polyglutamine, ataxia, tbp, spinocerebellar, cell, mol, transcriptional, genet, content, mice, heat, shock, neurosci, cookies, function, disease, transgenic, transcription, expression, tatabinding, hsp, privacy, data, domain, interaction, expanded, mutant, open, rev, biol, neurol, repeat, gene, nat, information, implications, neurodegeneration, expansion, polyq, human, death, tfiib,

Topics {✒️}

nature portfolio permissions reprints privacy policy author information authors advertising nature 431 nature axonal charcot-marie-tooth disease social media tata-binding protein gene caa/cag repeat oligonucleotide mutant n-terminal fragment xiao-jiang li induces cone-rod dystrophy require vertebrate-specific sequences eukaryotic protein-coding genes repetitive c-terminal domain tata-tbp-tfiib array glutamine-rich activation motif springerlink instant access spinocerebellar ataxia mutations fundamental cellular processes tata-binding protein permissions transgenic mice expressing personal data spinocerebellar ataxias trinucleotide repeat expansion progressive neurological symptoms human genetics analyzed data cag repeat expansion characterized transgenic mice data protection kainate-induced seizures polyglutamine domain modulates rna-binding proteins unstable repeat expansion privacy established transgenic mice spinocerebellar ataxia 17 plm mechanosensory neurons transcriptional activation modulated preclude transcriptional activation amino-terminal region neurological disease caused polyglutamine neurodegenerative diseases huntington disease protein shihua li issue learn

Questions {❓}

A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease?
Basal components of the transcription apparatus (RNA polymerase II, TATA-binding protein) contain activation domains: is the repetitive C-terminal domain (CTD) of RNA polymerase II a “portable enhancer domain”?
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?

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