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Gene expression analysis of hepatocyte-specific Taf2 conditional knockout mice

ABSTRACT: Taf2 is a transcription co-factor and a member of TFIID complex. To better understand gene regulation of Taf2 we generated a hepatocyte-specific Taf2 conditional knockout mouse. RNA-seq was performed in hepatocytes isolated from these mice as well as WT mice. It shows that Taf2 deletion in hepatocytes induces cell death and compensatory proliferation which contributes to inflammation and fibrosis in the liver.

ORGANISM(S): Mus musculus

PROVIDER: GSE287050 | GEO | 2025/12/12

REPOSITORIES: GEO

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Gene expression analysis of HepG2 cells overexpressing TAF2

Project description:Taf2 is a transcription co-factor and a member of TFIID complex. To better understand gene regulation of Taf2 we generated stable clones of HepG2 cells overexpressing either eGFP or TAF2-V5. The analysis shows that overexpression of TAF2 activates several pro-tumorigenic pathways and inhibits tumor suppressor pathways.

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TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing factors [CUT&RUN]

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Project description:The assembly and function of the yeast general transcription factor TFIID complex requires specific contacts between its Taf14 and Taf2 subunits, however, the mechanism underlying these contacts remains unclear. Here, we determined the molecular and structural basis by which the YEATS and ET domains of Taf14 bind to the C-terminal tail of Taf2 and identified a unique DNA-binding activity of the linker region connecting the two domains. We show that in the absence of ligands the linker region of Taf14 is occluded by the surrounding domains, and therefore the DNA binding function of Taf14 is autoinhibited. Binding of Taf2 promotes a conformational rearrangement in Taf14, resulting in a release of the linker for the engagement with DNA and the nucleosome. Genetic in vivo data indicate that the association of Taf14 with both Taf2 and DNA is essential for transcriptional regulation. Our findings provide a basis for deciphering the role of individual TFIID subunits in mediating gene transcription.

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Cytoplasmic complex comprising TAF2, TAF8, TAF10 provides evidence for nuclear holo-TFIID assembly from preformed submodules

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TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing

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2025-03-04 | PXD056095 | Pride

TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing

Project description:TFIID is an essential eukaryotic transcription factor, which is required for RNA polymerase II promoter recognition and activation. As a multiprotein complex, TFIID contains several intrinsically disordered regions (IDRs), but the functions of these IDRs are unknown. Here, we show that a conserved IDR drives the TFIID subunit TAF2 to nuclear speckles, where it forms biomolecular condensates, separate from the TFIID complex. Quantitative mass spectrometry analyses reveal that the TAF2 IDR is required for the interaction with the nuclear speckle and spliceosome-associated protein SRRM2, which is thereby recruited to TFIID. The formation of SRRM2-free TFIID complexes elicits a set of unique alternative splicing events. These include events in RNAs coding for proteins involved in transcription and transmembrane transport. Together, these data identify an IDR of the basal transcription machinery as a molecular switch between nuclear compartments to control protein complex composition and pre-mRNA splicing.

2024-04-26 | PXD049117 | Pride

TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing – data-independent acquisition MS

Project description:TFIID is an essential basal transcription factor, crucial for RNA polymerase II (pol II) promoter recognition and transcription initiation. The TFIID complex consists of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs) that contain intrinsically disordered regions (IDRs) with currently unknown functions. Here, we show that a conserved IDR drives TAF2 condensation in nuclear speckles, independently of other TFIID subunits. Quantitative mass spectrometry analyses reveal that TAF2 exhibits close proximities to RNA-binding proteins, but that the TAF2 IDR specifically interacts with the splicing factor SRRM2. Modulation of TAF2 protein levels elicits alternative splicing (AS) events in RNAs coding for proteins involved in transcription and transmembrane transport, some of which overlap with SRRM2-regulated AS events. This study identifies an IDR of the basal transcription machinery as a molecular guide for protein partitioning into nuclear compartments, controlling protein complex composition and pre-mRNA splicing.

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