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TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing [RNA-Seq]

ABSTRACT: TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing [RNA-Seq]

PROVIDER: PRJNA1068462 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27709201_1.fastq.gz	Fastqsanger.gz
	SRR27709201_2.fastq.gz	Fastqsanger.gz
	SRR27709202_1.fastq.gz	Fastqsanger.gz
	SRR27709202_2.fastq.gz	Fastqsanger.gz
	SRR27709203_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing [RNA-Seq]

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 the TAF2 IDR specifically interacts with the nuclear speckle and spliceosome-associated protein SRRM2. Consequently, TAF2 recruits SRRM2 to TFIID to form non-canonical TFIID-SRRM2 complexes. Reduced SRRM2 recruitment elicits alternative splicing events in RNAs coding for proteins involved in transcription and transmembrane transport. Further, genome-wide binding analyses suggest TAF2 shuttling between nuclear speckles and pol II promoters. 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.

2024-02-06 | GSE254060 | GEO

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

2024-02-06 | GSE254080 | GEO

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

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

| PRJNA1068517 | ENA

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 [CUT&RUN]

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

| PRJNA1068524 | ENA

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

Project description:This SuperSeries is composed of the SubSeries listed below.

2024-02-06 | GSE254081 | GEO

Chaperonin CCT Checkpoint Function in Basal Transcription Factor TFIID Assembly

Project description:TFIID is a cornerstone of eukaryotic gene regulation. Distinct TFIID complexes with unique subunit composition exist and several TFIID subunits are shared with other complexes, conveying intricate cellular decision making to control subunit allocation and functional assembly of this essential transcription factor. However, the underlying molecular mechanisms remain poorly understood. Here, we used quantitative proteomics to examine TFIID submodules and assembly mechanisms in human cells. Structural and mutational analysis of the cytoplasmic TAF5/TAF6/TAF9 submodule identified novel interactions crucial for TFIID integrity, and for allocating TAF9 to TFIID or the SAGA co-activator complex. We discover a key checkpoint function for the chaperonin CCT, which specifically associates with nascent TAF5 for subsequent handover to TAF6/TAF9 and ultimate holo-TFIID formation. Our findings illustrate at the molecular level how multisubunit complexes are crafted in the cell, involving checkpoint decisions facilitated by a chaperone machine.

2019-01-07 | PXD011293 | Pride

Chaperonin CCT Checkpoint Function in Basal Transcription Factor TFIID Assembly

2022-03-02 | PXD011211 | Pride

Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID

Project description:Large heteromeric multiprotein complexes play pivotal roles at every step of gene expression in eukaryotic cells. Among them, the 20-subunits basal transcription factor TFIID nucleates RNA polymerase II preinitiation complex at gene promoters. Here, by combining systematic RNA-immunoprecipitation experiments, single-molecule imaging, proteomics and structure-function analyses, we show that TFIID is built using co-translational assembly. We discovered that all early steps of TFIID assembly, involving protein heterodimerization, happen during protein synthesis. Strikingly, we identify TAF1 – the largest protein in the complex – as a flexible scaffold subunit that co-translationally recruits preassembled TFIID submodules found populating the cytoplasm of cells. Consequently, TAF1 depletion leads to a cytoplasmic accumulation of TFIID building blocks. Altogether, our data suggest a multistep hierarchical model for TFIID biogenesis that culminates with the co-translational assembly on nascent TAF1 polypeptide, that works as a ‘driver’ subunit. We envision that this assembly strategy could be shared with other large heteromeric protein complexes.

2023-07-04 | PXD036358 | Pride

ZFC3H1 prevents RNA trafficking into nuclear speckles through condensation.

Project description:Controlling proper RNA pool for nuclear export is important for accurate gene expression. ZFC3H1 is a key controller that not only facilitates nuclear exosomal degradation, but also retains its bound polyadenylated RNAs in the nucleus upon exosome inactivation. However, how ZFC3H1 retains RNAs and how its roles in RNA retention and degradation are related remain largely unclear. Here, we found that upon degradation inhibition, ZFC3H1 forms nuclear condensates to prevent RNA trafficking to nuclear speckles (NSs) where many RNAs gain export competence. Systematic mapping of ZFC3H1 revealed that it utilizes distinct domains for condensation and RNA degradation. Interestingly, ZFC3H1 condensation activity is required for preventing RNA trafficking to NSs, but not for RNA degradation. Considering that no apparent ZFC3H1 condensates are formed in normal cells, our study suggests that nuclear RNA degradation and retention are two independent mechanisms with different preference for controlling proper export RNA pool-degradation is preferred in normal cells, and condensation retention is activated upon degradation inhibition.

| S-EPMC8501945 | biostudies-literature

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