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Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription (ChiP-Seq)

ABSTRACT: Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription (ChiP-Seq)

PROVIDER: PRJNA1059028 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27384363_1.fastq.gz	Fastqsanger.gz
	SRR27384363_2.fastq.gz	Fastqsanger.gz
	SRR27384364_1.fastq.gz	Fastqsanger.gz
	SRR27384364_2.fastq.gz	Fastqsanger.gz
	SRR27384365_1.fastq.gz	Fastqsanger.gz

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Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription

Project description:Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription

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Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription (RNA-Seq)

Project description:Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription (RNA-Seq)

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Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription (RNA-Seq)

Project description:The C-terminal domain of RPB1 (CTD) orchestrates transcription by recruiting regulators to RNA Pol II upon phosphorylation. Recent insights highlight CTD’s pivotal role in driving condensate formation on gene loci. Yet, the molecular mechanism behind how CTD-mediated recruitment of transcriptional regulators influences condensates formation remains unclear. Our study unveils that phosphorylation reversibly dissolves phase separation induced by the unphosphorylated CTD. Phosphorylated CTD, upon specific association with transcription regulatory proteins, forms distinct condensates from unphosphorylated CTD. Function studies demonstrate CTD variants with diverse condensation properties in vitro exhibit difference in promoter binding and mRNA co-processing in cells. Notably, varying CTD lengths lead to alternative splicing outcomes impacting cellular growth, linking the evolution of CTD variation/length with the complexity of splicing from yeast to human. These findings provide compelling evidence for a model wherein post-translational modification enables the transition of functionally specialized condensates, highlighting a co-evolution link between CTD condensation and splicing.

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Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription (ChiP-Seq)

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Variation of C-terminal domain governs RNA polymerase II genomic locations and alternative splicing in eukaryotic transcription

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2024-02-09 | GSE252261 | GEO

Transcriptional program of terminal granulocytic differentation

2009-12-19 | GSE19556 | GEO

Transcriptional program of terminal granulocytic differentation

Project description:To characterize the transcriptional program that governs terminal granulocytic differentation in vivo, we performed comprehensive microarray analysis of human bone marrow population highly enriched for promyelocytes, myelocytes / metamyelocytes and neotrophils. Bone marrow and peripheral blood samples were collected from healthy individuals in parallel. Cell populations representing successive stages of terminal granulocytic differentation were isolated from human bone marrow samples by 2-layer density gradient centrifugation, neutrophils were collected from peripheral blood using 1-layer density gradient centrifugation. All populations were depleted of nongranulocytic cells by immunomagnetic sorting.

2009-12-19 | E-GEOD-19556 | biostudies-arrayexpress

Bio-molecular architects: a scaffold provided by the C-terminal domain of eukaryotic RNA polymerase II.

Project description:In eukaryotic cells, the transcription of genes is accurately orchestrated both spatially and temporally by the C-terminal domain of RNA polymerase II (CTD). The CTD provides a dynamic platform to recruit different regulators of the transcription apparatus. Different posttranslational modifications are precisely applied to specific sites of the CTD to coordinate transcription process. Regulators of the RNA polymerase II must identify specific sites in the CTD for cellular survival, metabolism, and development. Even though the CTD is disordered in the eukaryotic RNA polymerase II crystal structures due to its intrinsic flexibility, recent advances in the complex structural analysis of the CTD with its binding partners provide essential clues for understanding how selectivity is achieved for individual site recognition. The recent discoveries of the interactions between the CTD and histone modification enzymes disclose an important role of the CTD in epigenetic control of the eukaryotic gene expression. The intersection of the CTD code with the histone code discloses an intriguing yet complicated network for eukaryotic transcriptional regulation.

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Integrator-PP2A complex dephosphorylates the C-terminal repeat domain of RNA Polymerase II

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The Set1 N-terminal domain and Swd2 interact with the RNA polymerase II CTD to recruit COMPASS

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