Mus musculus
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA259205 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR1556196_1.fastq.gz | Fastqsanger.gz | |||
| SRR1556196_2.fastq.gz | Fastqsanger.gz | |||
| SRR1556197_1.fastq.gz | Fastqsanger.gz | |||
| SRR1556197_2.fastq.gz | Fastqsanger.gz |
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Project description:DNA methylation at transcription start sites blocks TBP binding and transcription onset by RNApolII
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Project description:DNA methylation at transcription start sites blocks TBP binding and transcription onset by RNApolII [MeDIP]
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Project description:Aim: To determine the state of methylation of DNA molecules that are physically engages with either poised or active enhancers. Methods: We used ChIP-bisulfite-sequencing with H3K4me1 antibody to map the methylation of DNA bound to enhancer. We used ChIP-sequencing with RNApolII-PS5 antibody to map actively transcribing transcription start sites. We used reduced representation bisulfite sequencing (RRBS) to map total DNA methylation. Results - conclusion: DNA molecules that are physically found in H3K4me1 chromatin are hypomethylated while DNA found in enhancers that are associated with active transcription is further demethylated.
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Project description:The TATA binding protein (TBP) is a transcription factor that binds specifically to a DNA sequence called the TATA box upstream of the transcription start site. To gain insight into the genes occupied by TBP, chromatin immunoprecipitation coupled with massive parallel sequencing (ChIP-seq) was performed to determine the genome-wide binding targets. DNA was enriched by chromatin immunoprecipitation (ChIP) and analyzed by Solexa sequencing. ChIP was performed using an antibody against TBP.
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Project description:The TATA binding protein (TBP) is a transcription factor that binds specifically to a DNA sequence called the TATA box upstream of the transcription start site. To gain insight into the genes occupied by TBP, chromatin immunoprecipitation coupled with massive parallel sequencing (ChIP-seq) was performed to determine the genome-wide binding targets.
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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.
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Project description:Transcription preinitiation complex assembly on the promoters of protein encoding genes is nucleated in vivo by TFIID composed of the TATA-box Binding Protein (TBP) and 13 TBP-associate factors (Tafs) providing regulatory and chromatin binding functions. We used CXMS to study the organization and structure of the purified TFIID complex from Komagataella phaffii. Together with Cryo-EM, We confirm the unique subunit stoichiometry prevailing in TFIID and uncover a hexameric arrangement of Tafs containing a HF domain. Interaction with promoter DNA highlights two non-selective binding sites consistent with a DNA scanning mode.
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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.
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