Functional divergence of TBP homologs through distinct DNA binding dynamics
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1183408 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR31273500_1.fastq.gz | Fastqsanger.gz | |||
| SRR31273500_2.fastq.gz | Fastqsanger.gz | |||
| SRR31273501_1.fastq.gz | Fastqsanger.gz | |||
| SRR31273501_2.fastq.gz | Fastqsanger.gz | |||
| SRR31273502_1.fastq.gz | Fastqsanger.gz |
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Project description:The TATA box-binding protein (TBP) is an evolutionarily conserved basal transcription factor common in the pre-initiation complex of all three eukaryotic RNA polymerases (RNA Pols). Despite their high conservation, homologous TBPs exhibit species- and tissue-specific functions that may contribute to the increasingly complex gene expression regulation across evolutionary time. To determine the molecular mechanisms of species- and tissue-specificity for homologous TBPs, we examined the ability of yeast TBP and murine TBP paralogs to replace the endogenous TBP in mouse embryonic stem cells. We show that, despite the high conservation in the DNA binding domain among the homologs, they cannot fully rescue the lethality of TBP depletion in mESCs, largely due to their inability to support RNA Pol III transcription. Furthermore, we show that the homologs differentially support stress-induced transcription reprogramming, with the divergent N-terminal domain playing a role in modulating changes in transcriptional response. Lastly, we show that the homologs have vastly different DNA binding dynamics, suggesting a potential mechanism for the distinct functional behavior observed among the homologs. Taken together, these data show a remarkable balance between flexibility and essentiality for the different functions of homologous TBP in eukaryotic transcription.
2025-04-16 | GSE281338 | GEO
Project description:We performed a comprehensive ChIP-on-chip analysis for 28 transcription factors on a large set of known and novel TBP binding sites experimentally identified via ChIP-cloning. A large fraction of identified TBP binding sites is located in introns or lacks a gene/mRNA annotation and found to direct transcription. Distinct profiles for general transcription factors and TAF-containing complexes were uncovered for RNAP II promoters located in CpG- and non-CpG islands suggesting distinct transcription initiation pathways. Keywords: TBP, Promoter, ChIP-on-chip, transcription factor profiling
2007-01-17 | GSE6738 | GEO
Project description:During mitosis, TATA-binding protein(TBP), which remains bound to DNA during mitosis, recruits PP2A and also interacts with a subunit of the condensin complex to allow efficient dephosphorylation and inactivation of condensin near these promoters to inhibit their compaction. These result suggest that TBP function is not only important for expression of genes transcribed bDuring mitosis, TATA-binding protein(TBP), which remains bound to DNA during mitosis, recruits PP2A and also interacts with a subunit of the condensin complex to allow efficient dephosphorylation and inactivation of condensin near these promoters to inhibit their compaction. These result suggest that TBP function is not only important for expression of genes transcribed by all three RNA polymerase during interphase, but also for transmitting the memory of gene activity through mitosis to daughter cellsy all three RNA polymerase during interphase, but also for transmitting the memory of gene activity through mitosis to daughter cells We use ChIP-chip approach to identify TBP-bindind sites in mitotic Jurkat cells at genome-wide level. Input DNA fragments and DNA fragments immunoprecipitated by TBP antibodies by ChIP assay on mitotic Jurkat cells were used to probe the Affymetrix Genechip human tiling 2.0c to identift TBP-binding sites in mitotic Jurkat cells. Input and ChIP sample were replicated three times as following: Input rep1, TBP ChIP1, Input rep2, TBP ChIP2, Input rep3, TBP ChIP3.
2010-04-03 | E-GEOD-12256 | biostudies-arrayexpress
Project description:The Swi2/Snf2-family ATPase Mot1 displaces TBP from DNA in vitro, but the global relationship between Mot1 and TBP in vivo has been unclear. We therefore mapped the distribution of Mot1 and TBP on native chromatin at base-pair resolution. Mot1 and TBP binding sites coincide throughout the genome, and depletion of TBP results in a global decrease in Mot1 binding. Using midpoint-versus-length mapping to assess the spatial relationship of Mot1 and TBP on chromatin, we find evidence that Mot1 approaches TBP from the upstream direction, consistent with its in vitro mode of action. Strikingly, inactivation of Mot1 leads to both increases and decreases in TBP-genome association. Sites of TBP gain tend to contain robust TATA boxes, while sites of TBP loss contain poly(dA:dT) tracts that may contribute to nucleosome exclusion. We propose that the action of Mot1 is required to clear TBP from intrinsically preferred (TATA-containing) binding sites, ensuring sufficient soluble TBP to bind intrinsically disfavored (TATA-less) sites.
2013-10-21 | GSE44200 | GEO
Project description:The Swi2/Snf2-family ATPase Mot1 displaces TBP from DNA in vitro, but the global relationship between Mot1 and TBP in vivo has been unclear. We therefore mapped the distribution of Mot1 and TBP on native chromatin at base-pair resolution. Mot1 and TBP binding sites coincide throughout the genome, and depletion of TBP results in a global decrease in Mot1 binding. Using midpoint-versus-length mapping to assess the spatial relationship of Mot1 and TBP on chromatin, we find evidence that Mot1 approaches TBP from the upstream direction, consistent with its in vitro mode of action. Strikingly, inactivation of Mot1 leads to both increases and decreases in TBP-genome association. Sites of TBP gain tend to contain robust TATA boxes, while sites of TBP loss contain poly(dA:dT) tracts that may contribute to nucleosome exclusion. We propose that the action of Mot1 is required to clear TBP from intrinsically preferred (TATA-containing) binding sites, ensuring sufficient soluble TBP to bind intrinsically disfavored (TATA-less) sites. We have analyzed the genomic distributions of yeast TBP and Mot1 using Occupied Regions of Genomes from Affinity-purified Naturally Isolated Chromatin and sequencing (ORGANIC-seq).
2013-10-21 | E-GEOD-44200 | biostudies-arrayexpress
Project description:During mitosis, TATA-binding protein(TBP), which remains bound to DNA during mitosis, recruits PP2A and also interacts with a subunit of the condensin complex to allow efficient dephosphorylation and inactivation of condensin near these promoters to inhibit their compaction. These result suggest that TBP function is not only important for expression of genes transcribed bDuring mitosis, TATA-binding protein(TBP), which remains bound to DNA during mitosis, recruits PP2A and also interacts with a subunit of the condensin complex to allow efficient dephosphorylation and inactivation of condensin near these promoters to inhibit their compaction. These result suggest that TBP function is not only important for expression of genes transcribed by all three RNA polymerase during interphase, but also for transmitting the memory of gene activity through mitosis to daughter cellsy all three RNA polymerase during interphase, but also for transmitting the memory of gene activity through mitosis to daughter cells
2009-05-28 | GSE12256 | GEO
Project description:Using CUT&Tag, a chromatin profiling technique, we show that TBP depletion via IAA surprisingly does not affect RNA Pol II transcription but affects RNA Pol III transcription. Additionally, induction of genes via heat shock and retinoic acid treatment does not require TBP. We also show that a metazoan specific paralog TRF2 does not compensate for TBP for RNA Pol II transcription and that the TFIID subunit of the Pre-initiation Complex can still form with specific subunits still binding onto DNA when TBP is depleted.
2023-04-12 | GSE206694 | GEO
Project description:We sequenced cDNA prepared from ribosomal RNA depleted total RNA of 10-10 embryos co-injected with TBP-,TBP2- and TLF-AS antisense oligonucleotides and with water to create expression profiles of triple knockdown of TBP/TBP-related factors (TKD) and control, respectively, in Xenopus laevis at early developmental stage 10.5. (according to Nieuwkoop and Faber). We executed differential expression analysis of sequence count data (DEseq).
2016-03-07 | GSE76994 | GEO
Project description:In eukaryotes, gene expression is performed by three RNA polymerases that are targeted to promoters by molecular complexes. A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription. Herein, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP. We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA. Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9 edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes. Lack of O-GlcNAcylation at T114 is associated with a striking reprograming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
2020-04-14 | GSE130309 | GEO
Project description:General transcription factor TFIID is a key component of RNA polymerase II transcription initiation in eukaryotic nuclei. Human TFIID is a megadalton-sized multiprotein complex comprising TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs). TBP binds to core promoter DNA, recognizing the TATA-box. A number of transcription regulatory factors were found to compete with DNA for TBP binding. We identified a ternary complex formed by TBP and the histone fold (HF) domain containing TFIID subunits TAF11 and TAF13. We demonstrate that TAF11/TAF13 competes for TBP binding with TATA-box DNA, and also with the N-terminal domain of TAF1. In an integrative approach combing crystal coordinates, biochemical analyses and data from cross-linking mass-spectrometry (CLMS), we determine the architecture of the TAF11/TAF13/TBP complex, revealing TAF11/TAF13 interaction with the DNA binding surface of TBP. Our results thus suggest a novel regulatory state for TFIID function.
2017-11-15 | PXD005676 | Pride