Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

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

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

PROVIDER: PRJNA1068462 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			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

Items per page:

1 - 5 of 18

Similar Datasets

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

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.

2025-03-04 | PXD056095 | Pride

TAF2 condensation in nuclear speckles links basal transcription factor TFIID to RNA splicing factors [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 to nuclear speckle condensates independently of other TFIID subunits. Quantitative mass spectrometry analyses reveal TAF2 proximity to RNA splicing factors including specific interactions of the TAF2 IDR with SRRM2 in nuclear speckles. Deleting the IDR from TAF2 does not majorly impact global gene expression but results in changes of alternative splicing events. Further, genome-wide binding analyses suggest that the TAF2 IDR impedes TAF2 promoter association by guiding TAF2 to nuclear speckles. This study demonstrates that an IDR within the large multiprotein complex TFIID controls nuclear compartmentalization and thus links distinct molecular processes, namely transcription initiation and RNA splicing.

2024-02-06 | GSE254060 | GEO

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

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 to nuclear speckle condensates independently of other TFIID subunits. Quantitative mass spectrometry analyses reveal TAF2 proximity to RNA splicing factors including specific interactions of the TAF2 IDR with SRRM2 in nuclear speckles. Deleting the IDR from TAF2 does not majorly impact global gene expression but results in changes of alternative splicing events. Further, genome-wide binding analyses suggest that the TAF2 IDR impedes TAF2 promoter association by guiding TAF2 to nuclear speckles. This study demonstrates that an IDR within the large multiprotein complex TFIID controls nuclear compartmentalization and thus links distinct molecular processes, namely transcription initiation and RNA splicing.

2024-02-06 | GSE254080 | GEO

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

2025-03-04 | PXD056099 | 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 factors

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

| PRJNA1068517 | ENA

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

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

| PRJNA1068524 | ENA

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

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