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PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - SLAM - seq

ABSTRACT: PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - SLAM - seq

PROVIDER: PRJEB32284 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR3291930.fastq.gz	Fastqsanger.gz
	ERR3291940.fastq.gz	Fastqsanger.gz
	ERR3291950.fastq.gz	Fastqsanger.gz
	ERR3291960.fastq.gz	Fastqsanger.gz
	ERR3291970.fastq.gz	Fastqsanger.gz

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PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - Targeted SLAM-seq

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PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - Targeted SLAM-seq

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PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - RNAseq

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Project description:PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - PROseq

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PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - RNAseq

Project description:Total RNA sequencing of WT, PHF3 KO and dSPOC, HEK293 cells

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PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - PRO-seq Timecourse

Project description:PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - PRO-seq Timecourse

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PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - PolII ChIP-seq

Project description:PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - PolII ChIP-seq

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PHF3 binds RNA polymerase II via the SPOC domain and regulates transcription of neuronal genes - PRO-seq Timecourse

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The SPOC proteins DIDO3 and PHF3 co-regulate gene expression and neuronal differentiation - RNAseq

Project description:Transcription is regulated by a multitude of activators and repressors, which bind to the RNA polymerase II (Pol II) machinery and modulate its progression. Death-inducer obliterator (DIDO) and PHD finger protein 3 (PHF3) are paralogue proteins that regulate transcription elongation by docking onto phosphorylated serine-2 in the C-terminal domain (CTD) of Pol II through their SPOC domains. Here we show that DIDO3 and PHF3 form a complex that bridges the Pol II elongation machinery with chromatin and RNA processing factors, and tethers Pol II in a phase-separated microenvironment. Their SPOC domains and C-terminal intrinsically disordered regions are critical for transcription regulation. PHF3 and DIDO exert cooperative and antagonistic effects on the expression of neuronal genes and are both essential for neuronal differentiation. The dataset contains RNAseq of HEK293 cells with various perturbations of PHF3 and DIDO1 genes.

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