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TATA-binding protein

The TATA-binding protein (TBP) is a highly conserved general transcription factor essential for the initiation of transcription in eukaryotic cells, where it specifically binds to the TATA box—a core promoter DNA sequence with the consensus motif TATAWAWR typically positioned 25–35 base pairs upstream of the transcription start site.^[1] Upon binding, TBP inserts phenylalanine residues into the minor groove of the DNA, inducing an ~80–90° bend that facilitates the recruitment of other transcription factors and RNA polymerase II to form the preinitiation complex (PIC).^[2] This DNA distortion is a critical step in promoter recognition and positioning the start site for accurate transcription.^[1] Structurally, TBP is a saddle-shaped monomeric protein whose length varies across species (typically 180–400 amino acids), featuring a variable N-terminal domain involved in species-specific regulatory interactions and a highly conserved C-terminal core domain of ~180 amino acids that mediates DNA binding.^[3]^[4] The core domain consists of two structurally similar lobes, each comprising a curved antiparallel β-sheet flanked by α-helices, forming a concave undersurface that cradles the DNA and a convex upper surface for protein-protein interactions.^[5] This architecture, first revealed by X-ray crystallography in 1992 for the yeast apo form and 1993 for the DNA-bound complex, enables TBP's sequence-specific recognition despite the absence of base-specific hydrogen bonds, relying instead on hydrophobic interactions and deformation.^[5]^[1] TBP functions as the central subunit of the multi-subunit complex TFIID for RNA polymerase II-dependent transcription of protein-coding genes, but it is also required for polymerase I (via SL1/TIF-IB) and polymerase III (via TFIIIB) activities, unifying basal transcription across all nuclear RNA polymerases.^[6] In TATA-less promoters, which constitute the majority in higher eukaryotes, TBP is recruited indirectly through initiator elements, downstream promoter elements, or TBP-associated factors (TAFs).^[7] TBP interacts with a diverse array of co-regulators, including TFIIA and TFIIB for PIC stabilization, as well as activators, repressors, and chromatin remodelers like NC2 and Mot1, allowing it to integrate signals for gene-specific regulation.^[8] Dysregulation of TBP, such as through polyglutamine expansions in its coding sequence, is linked to neurodegenerative diseases including spinocerebellar ataxia type 17.^[9]

Genetics and Evolution

TBP Gene Family

The human TBP gene is located on chromosome 6q27 and spans approximately 18.5 kb of genomic DNA, consisting of eight exons interrupted by seven introns, with the coding sequence divided by six introns and the 5'-untranslated region containing a 2.5-kb intron.^[10]^[11] The primary transcript, variant 1 (NM_003194.5), produces a mature mRNA of 1,857 nucleotides that encodes the canonical 339-amino-acid isoform.^[12] Alternative splicing of the TBP pre-mRNA generates at least two isoforms, including a shorter variant (NM_001172085.2) lacking the first 20 N-terminal residues, which exhibits ubiquitous but potentially modulated expression across tissues, though no highly tissue-specific longer variant like TBP-L has been prominently documented in humans.^[13]^[10] The TBP gene family includes paralogs known as TBP-related factors (TRFs), which arose from gene duplication events and exhibit specialized functions distinct from the ubiquitous role of TBP in general transcription. In humans and other vertebrates, key paralogs are TBPL1 (also called TRF2) and TBPL2 (TRF3); TRF2 shares about 40% identity with the TBP core domain and supports transcription from TATA-less promoters, particularly in spermatogenesis and neuronal genes, while TRF3, with 95% core domain similarity to TBP, is involved in oocyte maturation and early embryonic development.^[14] In insects like Drosophila melanogaster, additional paralogs such as TRF1 and TRF4 exist; TRF1 directs RNA polymerase III transcription in the central nervous system and germ cells, whereas TRF4 contributes to chromatin assembly and transcriptional regulation in higher eukaryotes.^[14]^[15] These TRFs generally lack strong TATA-box binding affinity compared to TBP and are recruited to specific promoters via unique interactions, enabling diversified transcriptional control.^[14] Evolutionarily, the TBP gene originated as a single-copy locus in the last archaeo-eukaryotic common ancestor, with its saddle-shaped core domain evolving from an ancient DNA-binding motif present across archaea and eukaryotes, dating back approximately 2,000 million years.^[16] Duplication events, particularly in metazoans, generated the TRF paralogs, allowing for subfunctionalization; for instance, TRF2 and TRF3 emerged through vertebrate-specific duplications to support developmental and tissue-specific transcription, while TRF1 and TRF4 arose earlier in arthropod lineages.^[16]^[14] This expansion of the TBP family reflects broader eukaryotic innovations in promoter selectivity and RNA polymerase specificity.^[16]

Evolutionary Conservation

The TATA-binding protein (TBP) exhibits remarkable sequence conservation in its core domain across eukaryotes, with greater than 80% amino acid identity between human and yeast orthologs, underscoring its essential role in transcription initiation.^[17] This core domain, comprising the C-terminal two-thirds of the protein, is responsible for DNA binding and interaction with other transcription factors, and it has remained highly preserved since the divergence of major eukaryotic lineages. In contrast, the N- and C-terminal regions flanking the core domain show greater variability in length and sequence, reflecting species-specific adaptations that do not compromise the protein's fundamental functions.^[18] Such bipartite architecture allows TBP to maintain evolutionary stability in its mechanistic core while permitting regulatory diversification at the termini.^[19] TBP orthologs are universally present in all eukaryotes, where they serve as basal transcription factors for RNA polymerases I, II, and III. In archaea, TBP-like proteins perform analogous roles in transcription initiation, highlighting a shared archaeo-eukaryotic heritage. However, TBP is notably absent in bacteria, which rely on sigma factors for promoter recognition instead of TBP-mediated mechanisms. This distribution pattern indicates that TBP emerged in the archaeal lineage and was retained and elaborated upon during eukaryotic evolution.^[16] Phylogenetic analyses of the TBP gene family reveal that TBP diverged from its paralogs in the TBP-related factor (TRF) family approximately 1.5 billion years ago, coinciding with the early stages of eukaryotic diversification. This ancient split likely arose from gene duplication events in the proto-eukaryotic ancestor, enabling the specialization of TBP for broad transcriptional roles while TRFs adapted to niche functions such as specific RNA polymerase III or developmental processes. The conservation of the core domain across these branches further supports TBP's primordial origin in the last archaeo-eukaryotic common ancestor. Functional conservation of TBP is exemplified by cross-species complementation experiments, where human TBP can partially rescue growth defects in yeast mutants lacking functional endogenous TBP, particularly for RNA polymerase II-dependent transcription. Such interchangeability demonstrates that the core mechanisms of TBP-DNA interaction and preinitiation complex assembly are preserved despite billions of years of divergence. However, full complementation is often limited for polymerase III-specific functions, highlighting subtle nonconserved elements in species-specific regulation.

Molecular Structure

Overall Architecture

The TATA-binding protein (TBP) is a small eukaryotic transcription factor comprising 240–340 amino acids depending on the species, with the conserved core domain spanning approximately 180 residues responsible for its essential functions. In humans, TBP consists of 339 amino acids and has a molecular weight of 37.6 kDa, while the yeast ortholog (Saccharomyces cerevisiae) contains 240 amino acids and a molecular weight of 26.8 kDa.^[13]^[20] TBP exists as a monomer in solution, adopting a distinctive saddle-shaped tertiary structure that positions it ideally for DNA recognition.^[21] The crystal structure of TBP was first elucidated in 1992 by Nikolov et al. at 2.6 Å resolution using the core domain from yeast, deposited as PDB entry 1TBP, which revealed a highly symmetric α/β fold resembling a molecular saddle.^[5]^[22] This architecture features two structurally similar domains connected by a short hinge, forming a curved, antiparallel 10-stranded β-sheet that constitutes the concave underside for DNA binding and four α-helices on the convex upper surface.^[5]^[21] The overall fold is stabilized by an extensive hydrophobic core, including buried nonpolar residues that maintain the saddle's rigidity and enable its deformability upon substrate interaction.^[5] Post-translational modifications, such as phosphorylation and acetylation, modulate TBP's stability and activity, though specific sites and effects vary by context; for instance, phosphorylation events can influence its conformational dynamics without altering the core architecture.^[23]

Key Domains and Motifs

The core domain of the TATA-binding protein (TBP), spanning the conserved C-terminal approximately 185 residues (residues 155–339 in humans), consists of two symmetric repeats, each formed by a five-stranded antiparallel β-sheet that collectively creates a saddle-shaped architecture essential for DNA binding.^[21] These repeats enclose a concave β-sheet surface that contacts the minor groove of DNA, while the convex underside features stirrup-like loops that facilitate intercalation.^[21] The N-terminal region of TBP, comprising the first ~154 residues (residues 1–154) in humans, is highly variable across species and lacks defined secondary structure, adopting an unstructured conformation that contributes to species-specific regulatory functions, such as modulating transcription rates or interactions in mammalian placental development.^[24]^[25] In TBP-related factors (TRFs), which share the core domain but diverge in function, C-terminal extensions often include alpha-helical motifs that enable specialized promoter recognition and interactions distinct from canonical TBP.^[26] Key structural motifs within the core domain include pairs of conserved phenylalanine residues positioned in the stirrups—Phe57 and Phe74 in the N-terminal repeat, and Phe148 and Phe165 in the C-terminal repeat (core numbering)—that partially intercalate between base pairs at the TATA box edges, inducing ~90° DNA bending critical for transcription initiation.^[21] These hydrophobic intercalations distort base stacking and widen the minor groove, stabilizing the protein-DNA complex without sequence-specific hydrogen bonding to bases.^[27]

DNA and Protein Interactions

Binding to Promoter DNA

The TATA-binding protein (TBP) recognizes the TATA box, a core promoter element with the consensus sequence TATAWAWR, typically located 25-35 base pairs upstream of the transcription start site in eukaryotic genes transcribed by RNA polymerase II.^[28] TBP binds this sequence with high affinity, exhibiting a dissociation constant (Kd) in the range of 1-10 nM, which enables stable association under physiological conditions.^[29] This recognition is essential for positioning the preinitiation complex at TATA-containing promoters. The binding mechanism follows an induced fit model, in which TBP's saddle-shaped core domain intercalates into the minor groove of the DNA, causing an 80-90 degree bend toward the major groove and partial unwinding of the helix.^[30] This distortion is facilitated by two pairs of conserved phenylalanine residues (e.g., Phe193 and Phe284 in human TBP) that act as wedges, inserting between adjacent base pairs at the TATA box edges to splay the bases apart and widen the minor groove by approximately 10 Å. The bending exposes the DNA backbone for additional interactions and facilitates subsequent conformational changes in the promoter. Sequence-specific recognition by TBP occurs through an indirect readout mechanism, where the inherent deformability of A/T-rich sequences facilitates the pronounced DNA bending and unwinding required for stable complex formation, without direct base-specific hydrogen bonds.^[1] Hydrophobic interactions between the protein's β-sheet surface and the minor groove walls, along with non-specific electrostatic and van der Waals contacts with the DNA phosphate backbone, stabilize the complex and contribute to overall specificity without requiring major groove access.^[1] Kinetically, TBP-DNA association proceeds in a two-step manner: an initial rapid, low-affinity step forms an unbent partial complex (Kd ~100 nM), followed by a slower conformational transition involving phenylalanine intercalation and DNA bending to yield the stable bent complex (Kd ~1 nM).^[31] This regulated process ensures precise timing in transcription initiation. The bent TBP-TATA complex promotes promoter opening by facilitating DNA melting near the transcription start site, allowing RNA polymerase II to access the template strand.^[32]

Interactions with Transcription Factors

The TATA-binding protein (TBP) interacts with transcription factor IIA (TFIIA) primarily through contacts involving the N-terminal domain of TFIIA, which stabilizes the TBP-DNA complex and enhances its specificity for promoter elements.^[33] Similarly, TBP binds to transcription factor IIB (TFIIB) via the core domain of TFIIB, with the N-terminal zinc ribbon domain of TFIIB contributing to overall complex stability; the B-reader motif (BRM) in the TFIIB linker region further reinforces this interaction by facilitating promoter recognition and bending.^[34]^[35] These protein-protein interfaces collectively prevent dissociation of TBP from DNA and promote ordered recruitment in transcription initiation. Within the TFIID complex, TBP engages multiple TBP-associated factors (TAFs) through distinct contact sites on its saddle-shaped core domain, forming a stable multiprotein assembly essential for promoter selectivity.^[36] Notably, the N-terminal domain of TAF1 (TAND) binds to the concave underside of TBP, inhibiting its DNA-binding activity in the absence of activators; this autoinhibitory interaction is relieved upon activator binding, allowing TBP release for promoter engagement.^[37] Other TAFs, such as TAF11 and TAF13, form histone-like modules that anchor TBP and modulate its conformation for regulated transcription.^[38] TBP also interfaces with co-activator complexes, including the Mediator, via specific residues on its N-terminal stirrup region, which contacts the N-terminal domain of Mediator subunit Med8 in the head module; this interaction bridges TBP to RNA polymerase II and facilitates activator-dependent PIC formation. Conversely, negative regulators such as negative cofactor 2 (NC2) and Mot1 exert inhibitory control: NC2 binds TBP's basic linker region to block TFIIA/TFIIB access and stabilize non-productive TBP-DNA complexes, while the ATPase Mot1 displaces TBP from DNA through ATP-dependent remodeling, preventing aberrant initiation.^[39]^[40] As a central hub in these networks, TBP typically forms 1:1 stoichiometric complexes with TFIIA and TFIIB to stabilize early intermediates, but integrates into higher-order assemblies like TFIID (one TBP per complex with multiple TAFs) or PICs, where its avidity for partners dictates context-specific regulation.^[41]

Role in Transcriptional Machinery

Assembly of Preinitiation Complex

The assembly of the preinitiation complex (PIC) for RNA polymerase II (Pol II) transcription initiation begins with the binding of TFIID, a multi-subunit complex containing the TATA-binding protein (TBP) and TBP-associated factors (TAFs), to the TATA box in the core promoter region.^[32] This initial recognition step positions TBP to insert its concave surface into the minor groove of the TATA sequence, inducing a sharp bend in the DNA helix of approximately 80 degrees.^[42] Following TFIID binding, TFIIA and TFIIB associate sequentially with the TBP-DNA complex; TFIIA stabilizes the TBP-DNA interaction by preventing non-specific dissociation, while TFIIB bridges the promoter-bound TBP to the incoming Pol II-TFIIF module.^[43] Next, the Pol II-TFIIF complex joins, followed by TFIIE and TFIIH, completing the PIC architecture that positions Pol II at the transcription start site.^[32] A key rate-limiting step in this sequential assembly is the formation of the TBP-TFIIB-Pol II bridge, which facilitates the recruitment of Pol II to the promoter and is often the slowest phase in vitro.^[43] This bridging interaction involves the core domain of TFIIB docking onto the dock region of Pol II, stabilizing the complex and enabling subsequent incorporation of TFIIE and TFIIH.^[43] Once assembled, TFIIH's XPB helicase subunit uses ATP hydrolysis to remodel the DNA, unwinding ~14 base pairs downstream of the transcription start site to form the open promoter complex (OPC), which allows promoter escape and initiation.^[32] Cryo-electron microscopy (cryo-EM) structures have provided atomic-level insights into PIC assembly, revealing a clamp-like architecture where Pol II's clamp domain grips the promoter DNA, with TBP and TFIIB forming a central scaffold.^[44] For instance, a 2017 cryo-EM study of the complete Mediator-Pol II PIC at ~8 Å resolution highlighted how TFIIH integrates into this clamp to drive DNA opening, confirming the sequential buildup from TFIID anchoring.^[44] These structures underscore the dynamic conformational changes, such as TFIIB's reader domain inserting into the Pol II active site cleft, that propagate from TBP binding to OPC formation.^[43] While the canonical PIC relies on TBP for TATA-containing promoters, variations exist in TATA-less promoters, where assembly can proceed independently of TBP through factors like TBP-related factor 2 (TRF2). TRF2 recruits analogous general transcription factors to initiate PIC formation at these promoters, bypassing TBP-mediated DNA bending and enabling transcription of genes lacking a TATA box, such as those in housekeeping or developmental contexts.^[45]

Functions Across RNA Polymerases

The TATA-binding protein (TBP) plays a conserved role in transcription initiation across all three eukaryotic RNA polymerases, serving as a scaffold that bends promoter DNA and recruits polymerase-specific factors to form preinitiation complexes (PICs).^[46] In RNA polymerase II (Pol II) transcription, TBP functions as a basal factor within the multi-subunit TFIID complex, which recognizes TATA boxes or TATA-less promoters on protein-coding genes to initiate mRNA synthesis.^[47] TFIID, comprising TBP and TBP-associated factors (TAFs), anchors the PIC assembly on mRNA gene promoters, facilitating the recruitment of Pol II and other general transcription factors like TFIIB, as elaborated in the stepwise formation of the Pol II PIC.^[48] For RNA polymerase I (Pol I) transcription of ribosomal RNA (rRNA) genes, TBP integrates into the SL1 complex alongside Pol I-specific TAFs (such as TAF1A, TAF1B, TAF1C, and TAF1D), which directs PIC formation at rRNA promoters lacking a canonical TATA box.^[49] The SL1 complex, in cooperation with the upstream binding factor (UBF), binds to the upstream control element (UCE) and core promoter region of rDNA, stabilizing Pol I recruitment and enabling high-level rRNA production essential for ribosome biogenesis.^[50] This TBP-dependent interaction positions the PIC upstream of the transcription start site, promoting efficient initiation despite the absence of a TATA motif.^[51] In RNA polymerase III (Pol III) transcription of small non-coding RNAs like tRNAs and 5S rRNA, TBP assembles into the TFIIIB complex with the TFIIB-related factor BRF1 (or BRF2 for select promoters) and the BDP1 subunit, which positions the PIC upstream of the start site on genes often featuring internal or upstream TATA-like elements.^[52] TFIIIB is recruited by upstream factors such as TFIIIC for tRNA genes, where TBP's binding induces DNA bending to orient Pol III for accurate start site selection and basal initiation.^[53] This configuration supports the compact transcription units typical of Pol III genes, ensuring precise and frequent initiation.^[54] TBP's DNA-binding mechanism, characterized by a conserved ~80–90° bend in the minor groove, is adapted across polymerases through interactions with distinct TFIIB homologs—TFIIB for Pol II, TAF1B in SL1 for Pol I, and BRF1 in TFIIIB for Pol III—allowing polymerase-specific efficiency in PIC stabilization and promoter opening.^[46] These adaptations enable comparable basal transcription rates, with structural variations in associated factors modulating DNA distortion and polymerase recruitment to suit each system's promoter architecture.^[55] Recent cryo-EM studies post-2020 have revealed TBP's contribution, via TFIID, to Pol II promoter-proximal pausing, where TBP-containing complexes stabilize early elongation intermediates (~20–60 nucleotides downstream), preventing premature release until regulatory signals like NELF and DSIF are resolved; replacing TFIID with TBP alone disrupts this pause.^[48] Such insights highlight TBP's dynamic role in transitioning from initiation to productive elongation in Pol II systems.^[56]

Biological and Clinical Relevance

Regulation and Non-Transcriptional Roles

The activity of TATA-binding protein (TBP) is tightly regulated through post-translational modifications that influence its stability and function. This dynamic balance ensures appropriate TBP abundance in response to developmental cues. Additionally, activator-dependent de-repression mechanisms counteract TBP inhibition; in yeast, the ATPase Mot1 removes TBP from non-productive DNA sites to repress transcription, but activators like those in the SAGA complex promote TBP retention and preinitiation complex assembly at target promoters. In chromatin contexts, nucleosomes pose a barrier to TBP binding at promoters, necessitating histone chaperones for effective recruitment. The facilitates chromatin transcription (FACT) complex facilitates TBP access to TATA boxes within nucleosome-bound DNA by destabilizing nucleosomes and promoting their transient disassembly, thereby enabling transcription initiation at chromatin templates. This role of FACT is essential for overcoming chromatin-mediated repression at inducible promoters. Beyond transcription, TBP contributes to non-transcriptional processes. In yeast, TBP binds autonomously replicating sequence (ARS) consensus elements and supports the initiation of DNA replication at chromosomal origins, as evidenced by TBP mutants that impair origin firing in vivo. TBP also modulates apoptosis through interactions with p53; wild-type p53 binds TBP to repress transcription from the bcl-2 promoter, thereby downregulating the anti-apoptotic Bcl-2 protein and promoting cell death pathways.

Associations with Diseases

Mutations in the TATA-binding protein (TBP) gene are associated with spinocerebellar ataxia type 17 (SCA17), a rare autosomal dominant neurodegenerative disorder characterized by cerebellar ataxia, psychiatric symptoms, and chorea. SCA17 results from CAG trinucleotide repeat expansions in the TBP coding region, with pathogenic alleles typically containing more than 40 repeats, leading to an elongated polyglutamine (polyQ) tract in the TBP protein.^[57] These expansions cause polyQ-mediated toxicity through mechanisms including protein aggregation, transcriptional dysregulation, and impaired neuronal function, particularly in the cerebellum and basal ganglia.^[58] Intermediate CAG expansions in TBP (41-46 repeats) have been linked to late-onset Parkinson's disease (PD), particularly in cases with parkinsonian features overlapping with SCA17 phenotypes. These expansions enhance TBP's interaction with transcription factor IIB (TFIIB), leading to transcriptional dysregulation in dopaminergic neurons, which contributes to selective vulnerability in the substantia nigra.^[59]^[60] In cancer, TBP overexpression is observed in various aggressive tumors, where it enhances RNA polymerase III (Pol III) transcriptional activity, promoting the expression of Pol III-dependent genes involved in cell proliferation and survival, such as tRNAs and 5S rRNA.^[61] TBP also plays a role in viral oncogenesis, for instance, in human papillomavirus (HPV)-associated cancers, where TBP facilitates basal transcription of the viral E6 and E7 oncogenes; the HPV E2 protein represses this transcription by interfering with TBP-mediated promoter recognition, and E2 disruption in integrated viral genomes leads to oncogene derepression.^[62] Therapeutic strategies targeting TBP dysregulation include histone deacetylase (HDAC) inhibitors, which restore TBP acetylation levels in polyQ-expanded models of neurodegeneration. In SCA17 cellular and animal models, HDAC inhibitors such as suberoylanilide hydroxamic acid (SAHA) increase histone acetylation, mitigate polyQ aggregation, and improve motor function by counteracting transcriptional repression caused by mutant TBP.^[63] Recent studies up to 2024 confirm that class I/II HDAC inhibitors alleviate polyQ toxicity in dopaminergic neurons, suggesting potential for treating TBP-related PD and SCA17 through enhanced protein acetylation and gene expression.^[64]

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TBP-TAF Complex SL1 Directs RNA Polymerase I Pre-initiation ...
Aug 19, 2005 · We demonstrate that human SL1 can direct accurate Pol I transcription in the absence of UBF and can interact with the rDNA promoter ...
[46]
Recruitment of TATA-Binding Protein–TAFI Complex SL1 to ... - NIH
UBF is a DNA binding protein with multiple HMG domains that binds directly to the CORE and UCE elements of the ribosomal DNA promoter.
[47]
Reconstitution of Transcription Factor SL1: Exclusive Binding of TBP ...
In addition, these TAFIs interact with each other to form a stable TBP-TAF complex. When TBP was bound first by either TAFI110, 63, or 48, subunits of TFIID ...
[48]
Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA ...
Jul 25, 2017 · Our study provides a structural insight on how Bdp1 is assembled into TFIIIB complexes, reveals structural and functional similarities between Bdp1 and Pol II ...
[49]
A common site on TBP for transcription by RNA polymerases II and III
TFIIIB is brought to its location in pol III promoters, upstream of the start site of transcription, by its assembly factor TFIIIC, but can also bind ...
[50]
Transcription factor TFIIIB and transcription by RNA polymerase III
Oct 25, 2006 · The three subunits of TFIIIB, which have been a focus of our research, are TBP (TATA-box-binding protein), Brf1 and Bdp1. The 596-amino-acid ...
[51]
Stepwise Bending of DNA by a Single TATA-Box Binding Protein - NIH
When TBP binds to and bends the DNA, the conformation of the DNA changes and the amplitude of Brownian motion of the tethered bead is reduced compared to that ...
[52]
https://www.nature.com/articles/s41467-017-00126-1
[53]
SCA17, a novel autosomal dominant cerebellar ataxia caused by an ...
Several lines of evidence support our conclusion that polyglutamine expansion in the TBP is pathogenic and the causative agent of a novel type of disease ...1c2 Antibody Immunoscreening... · Pcr Screening Of Expanded... · Acknowledgements
[54]
Molecular mechanisms underlying Spinocerebellar Ataxia 17 ... - NIH
We believe that impaired transcriptional activities caused by mutant TBP with polyQ expansion is a major form of toxicity contributing to SCA17 pathogenesis, ...
[55]
Trinucleotide repeat expansion of TATA-binding protein gene ...
Low-range TBP expansions are linked to Parkinson's, with a high prevalence of PD in carriers of 41-45 repeats, especially at advanced ages. A 41 repeat seems ...Missing: TFIIB | Show results with:TFIIB
[56]
Evidence of TAF1 dysfunction in peripheral models of X-linked ... - NIH
Similarly, altered interaction of TATA-box binding protein (TBP) to TFIIB has been shown as the molecular mechanism underlying neurodegeneration in ...
[57]
RNA polymerase III transcription in cancer: the BRF2 connection
Apr 25, 2011 · Activation of TFIIIB activity has been noted in a variety of cancers types. Increased TBP expression has been observed in a clinically ...
[58]
TFIIB-RNA polymerase II-TFIIF preinitiation complex - PubMed
E2 appears to function as an active repressor that directly inhibits HPV transcription at steps after TATA recognition by TBP or TFIID.Missing: oncogenesis | Show results with:oncogenesis
[59]
Polyglutamine neurodegenerative diseases and regulation of ...
SCA 17: neurodegeneration and the TATA-box-binding protein (TBP). Expansion of ... Protective effects of HDAC inhibitors have been reported for other ...
[60]
Polyglutamine (PolyQ) Diseases: Navigating the Landscape of ...
Jul 12, 2024 · Therefore, histone hyperacetylation triggered by inhibition of HDACs has neuroprotective effect and HDAC inhibitors have been suggested as a ...