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Effect of the intrinsically disordered region (IDR) within the CLK2 (T343A) mutant in the regulation of intron retention

ABSTRACT: Effect of the intrinsically disordered region (IDR) within the CLK2 (T343A) mutant in the regulation of intron retention

PROVIDER: PRJNA1037522 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26779293_1.fastq.gz	Fastqsanger.gz
	SRR26779293_2.fastq.gz	Fastqsanger.gz
	SRR26779294_1.fastq.gz	Fastqsanger.gz
	SRR26779294_2.fastq.gz	Fastqsanger.gz
	SRR26779295_1.fastq.gz	Fastqsanger.gz

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Effect of the intrinsically disordered region (IDR) within the CLK2 (T343A) mutant in the regulation of intron retention

Project description:We established the HeLa cells expressing the GFP (control) or CLK2 (T343A) with deletion of the IDR [T343A (dIDR)]. These cells were subjected to RNA-seq for the alternative splicing analysis.

2023-11-09 | GSE247419 | GEO

Effect of CLK2 expression in the regulation of intron retention during heat shock [RNA-seq]

Project description:Intron retention (IR) constitutes a less explored form of alternative splicing, wherein introns are retained within mature mRNA transcripts. Our investigation demonstrates that the CDC-like kinase 2 (CLK2) undergoes liquid-liquid phase separation (LLPS) within nuclear speckles in response to heat shock (HS). The formation of CLK2 condensates depends on the intrinsically disordered region (IDR) located within the N-terminal amino acids 1-148. Phosphorylation at residue T343 sustains CLK2 kinase activity and facilitates autophosphorylation, thus inhibiting the LLPS activity of the IDR. These CLK2 condensates initiate the reorganization of nuclear speckles, transforming them into larger, rounded structures. Moreover, these condensates facilitate the recruitment of splicing factors into these compartments, potentially restricting their access to mRNA for intron splicing. Consequently, the formation of CLK2 condensates promotes the IR.

2024-07-15 | GSE271918 | GEO

Effect of CLK2 expression in the regulation of intron retention during heat shock

Project description:We established the HeLa cells expressing the GFP (control) or CLK2 (WT) and subjected them to heat shock. These cells were subjected to RNA-seq for the alternative splicing analysis.

2023-11-09 | GSE247417 | GEO

Replication licensing regulated by an intrinsically disordered region of origin recognition complex

Project description:In eukaryotes, the hetero-hexameric origin recognition complex (ORC) is responsible for assembling Mcm2-7 complex into a head-to-head double hexamer (DH), forming pre-replicative complex (pre-RC) that licenses origin DNA for replication initiation. This process is tightly controlled throughout the cell cycle to ensure accurate duplication of the genome. Here we show that the N-terminal intrinsically disordered region (IDR) of the yeast Orc2 subunit plays a critical role in promoting pre-RC assembly. We found that removing a short segment (residues 175-200) from Orc2-IDR or mutating a key isoleucine (194) in this region significantly inhibits replication initiation across the genome and causes cell death. Although the Orc2-IDR mutants can still assemble the ORC-Cdc6-Cdt1-Mcm2-7 (OCCM) intermediate on DNA, the assembled mutant OCCM exhibits impaired ATP hydrolysis, preventing its conversion into Mcm2-7-ORC (MO) complex and subsequent DH formation. Interestingly, our in vitro assays showed that adding the Orc2-IDR peptide in the pre-RC reactions can rescue this defect. Furthermore, phosphorylation of this Orc2-IDR motif by S-cyclin dependent kinase (S-CDK) blocks its binding to Mcm2, leading to defective pre-RC assembly. Our findings provide crucial mechanistic insights into the multifaceted roles of ORC in modulating MCM loading to support origin licensing during the G1 phase and its regulation to restrict origin firing within the S phase.

2024-09-18 | GSE262693 | GEO

An Intrinsically Disordered Region Controlling Condensation of a Circadian Clock Component and Rhythmic Transcription in the Liver [ChIP-seq]

Project description:Circadian gene transcription is fundamental to metabolic physiology. Here we report that the nuclear receptor REV-ERBalpha, a repressive component of the molecular clock, forms circadian condensates in the nuclei of mouse Liver. These condensates are dictated by an intrinsically disordered region (IDR) located in the protein’s hinge region which specifically concentrates nuclear receptor corepressor 1 (NCOR1) at the genome. IDR deletion diminishes the recruitment of NCOR1 and disrupts rhythmic gene transcription in vivo. REV-ERBalpha condensates are located at high-order transcriptional repressive hubs in the Liver genome that are highly correlated with circadian gene repression. Deletion of the IDR disrupts transcriptional repressive hubs and diminishes silencing of target genes by REV-ERBalpha. This work demonstrates physiological circadian protein condensates containing REV-ERBalpha whose IDR is required for hub formation and the control of rhythmic gene expression.

2024-11-05 | GSE242901 | GEO

Intrinsically disordered regions of transcription factor encode multiple functions using interwoven sequence grammars (ChEC-seq)

Project description:Intrinsically disordered regions (IDRs) are abundant within eukaryotic proteins, but their sequence-function relationship remains poorly understood. IDRs of transcription factors (TFs) can direct promoter selection and recruit coactivators, as exemplified by the budding-yeast TF- Msn2. To examine how low-complexity IDRs encode multiple functions, we compared genomic binding preferences, gene induction, and coactivator recruitment amongst a large set of designed Mns2-IDR mutants. We show that multiple regions across the >500AA IDR contribute to both functions. Yet, transcription activity was readily disrupted by variants having no consequences on Msn2 binding. Our data attribute this differential sensitivity to the integration of relaxed, composition-based code directing binding preferences with a more stringent, motif-based code controlling the recruitment of coactivators and transcription activity. Interwoven sequence grammar may present a general paradigm through which low-complexity IDRs encode multiple functions.

2023-11-19 | GSE239882 | GEO

Intrinsically disordered regions of transcription factor encode multiple functions using interwoven sequence grammars (RNA-Seq)

2023-11-19 | GSE239883 | GEO

Hierarchical antagonistic regulatory elements in the TRPV4 intrinsically disordered N-terminus modulate lipid binding and channel activity through transient long-range interactions

Project description:Intrinsically disordered regions (IDRs) are important for the functional regulation of membrane receptors. Among the TRP Vanilloid channels involved in thermo- and osmosensation, TRPV4 features the largest N-terminal IDR of ~150 residues. Here, we elucidate the structural ensemble of the TRPV4 IDR through an integrated structural biology approach. Novel structural and functional properties can be assigned to distinct IDR regions. Along the length of the entire IDR, a hierarchical interaction network of structurally and functionally coupled antagonistic regulatory modules can be mapped. Long-range transient crosstalk between these regulatory elements mediates channel responses to osmotic stimuli. Most notably, a highly conserved regulatory patch in the N-terminal IDR asserts dominant negative control over lipid binding and channel activity by acting on a sensitizing PIP2 binding site in the C-terminal IDR. This work demonstrates the importance of IDRs and “IDR cartography” for understanding TRP channel function and regulation.

2023-08-01 | PXD038153 | Pride

Intrinsically disordered regions regulate RhlE RNA helicase functions in bacteria

Project description:RNA helicases—central enzymes in RNA metabolism— often feature intrinsically disordered regions (IDRs) that enable phase separation and complex interactions with other proteins and/or RNA molecules. IDRs are varied and fast evolving, which makes their function hard to predict. In the bacterial pathogen Pseudomonas aeruginosa, two non-redundant RNA helicases, RhlE1 and RhlE2, share a conserved REC catalytic core but have different C-terminal extensions (CTEs) composed of IDRs of diverse length and amino acid composition. Here, we show how the IDR diversity defines RhlE RNA helicase specificity of function. Both CTEs facilitate RNA binding and phase separation in vitro, leading to the in vivo localization of proteins in clusters within the cytoplasm. However, the CTE of RhlE2 is more efficient in enhancing REC core RNA unwinding, exhibits a greater tendency for phase separation, and interacts with the RNase E endonuclease, a crucial player in mRNA degradation. Swapping CTEs results in chimeric proteins that are biochemically active but functionally distinct as compared to their native counterparts. The RECRhlE1-CTERhlE2 chimera improves cold growth of a rhlE1 mutant, gains interaction with RNase E and affects a subset of both RhlE1 and RhlE2 RNA targets. The RECRhlE2-CTERhlE1 chimera instead hampers bacterial growth at low temperatures in the absence of RhlE1, with its detrimental effect linked to aberrant RNA droplets. By showing that IDRs modulate both protein core activities and subcellular localization, our study defines the impact of IDR diversity on the functional differentiation of RNA helicases.

2024-05-30 | GSE253333 | GEO

Intrinsically Disordered Regions Steer the Function Coordination of the Traveling Chromatin Modifier During Pol II Elongation (RNA-Seq)

Project description:The Rpd3S histone deacetylase complex suppresses cryptic initiation and maintains genomic integrity by deacetylating transcribed nucleosomes subsequent to RNA Pol II passage. Recent cryo-EM structure analysis of Rpd3S emphasized the significance of two asymmetrical Rco1/Eaf3 dimers in nucleosome binding. However, the mechanism by which Rpd3S interacts with nucleosomal substrates while traveling with elongating Pol II remains elusive. In this study, we elucidate the crucial role of the Rco1 N-terminal Intrinsically Disordered Region (IDR) in regulating Pol II association. Mutations within the K/R cluster of Rco1 IDR significantly impede Rpd3S binding to CTD, while leaving the overall complex integrity and nucleosome recognition unaffected. Moreover, we identify the Rco1-PHD1 and Eaf3-CHD domains as the minimal module responsible for specific interaction with Ser5-phosphorylated CTD. The Rco1 IDR functions by relieving autoinhibition from its C-terminal regions, enabling the binding of PHD-CHD to CTD. Additionally, we uncover an evolutionarily conserved mechanism governing the distinct roles of the asymmetrical Rco1/Eaf3 dimers, which coordinate nucleosome engagement and Pol II binding. These findings offer valuable new perspectives on the functional dynamics of mobile epigenetic modifying complexes that accompany processive machinery.

2024-11-13 | GSE254579 | GEO

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