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CTDP1 and RPB7 stabilize and license Pol II termination to reinitiation [PRO-seq]

ABSTRACT: CTDP1 and RPB7 stabilize and license Pol II termination to reinitiation [PRO-seq]

PROVIDER: PRJNA1074091 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27888266_1.fastq.gz	Fastqsanger.gz
	SRR27888266_2.fastq.gz	Fastqsanger.gz
	SRR27888267_1.fastq.gz	Fastqsanger.gz
	SRR27888267_2.fastq.gz	Fastqsanger.gz
	SRR27888268_1.fastq.gz	Fastqsanger.gz

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CTDP1 and RPB7 stabilize and license Pol II termination to reinitiation [PRO-seq]

Project description:The regulations of RNA Pol II initiation, elongation, and termination have been extensively investigated in mammalian cells, but how RNA Pol II terminates and then reinitiates a new round of transcription remains elusive. Here, we found that RPB7 loss triggers the degradation of RNA Pol II. Strikingly, RPB7 degradation combines knock out of E3 ligase Cullin 3 led to the accumulation of phosphorylated Pol II in the soluble fractions and Pol II reinitiation failure. The stability of recycled Pol II is dependent on the loop domain of RPB7 and the dephosphorylation of Pol II CTD. Termination-reinitiation recycling requires RPB7, CTD phosphatase subunit 1 (CTDP1), and stabilization of Pol II. Our study demonstrates that RPB7/CTDP1 controls the dephosphorylation and stabilization of RNA Pol II to permit RNA Pol II termination to reinitiation recycle in mammalian cells.

2025-02-05 | GSE255170 | GEO

CTDP1 and RPB7 stabilize and license Pol II termination to reinitiation [Micro-C]

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CTDP1 and RPB7 Stabilize Pol II and Permit Reinitiation

Project description:The mechanisms governing the termination and subsequent reinitiation of RNA polymerase II (Pol II) remain poorly understood. Here we found that depletion of RPB7 leads to the destabilization of Pol II’s largest subunit, RPB1. This destabilization is influenced by the loop regions of RPB7, CDK9, the C-terminal domain (CTD) of RPB1, and its linker region. The stabilization process of RPB1 is regulated by the E3 ubiquitin ligase Cullin 3. Additionally, RPB7 interacts with the phosphatase CTDP1, which is crucial for maintaining RPB1 stability. RPB7 is also vital for the reinitiation of Pol II, engages with RNA processing factors, and is localized to the RNA exit channel of the Pol II complex. The absence of RPB7 compromises RNA processing. We propose that RPB7 recruits CTDP1 to dephosphorylate Pol II, enhancing its stability and facilitating efficient reinitiation, adding a new dimension to transcriptional regulation.

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CTDP1 and RPB7 stabilize and license Pol II termination to reinitiation [Micro-C]

Project description:CTDP1 and RPB7 stabilize and license Pol II termination to reinitiation [Micro-C]

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RPB7/CTDP1 stabilizes and licenses Pol II termination to reinitiation [ChIP-Seq]

Project description:The regulations of transcription process have been extensively investigated, but how RNA Pol II terminates and reinitiates a new round of transcription remains elusive. Here, we found that RPB7 loss triggers the degradation of RNA Pol II. RPB7 degradation combing knock out of E3 ligase Cullin 3 led to the accumulation of phosphorylated Pol II in the soluble fractions and Pol II reinitiation failure. The stability of recycled Pol II is dependent on the loop-region and dimerization of RPB7 and the phosphorylation state of Pol II CTD. Site-specific cancer mutations in the RPB7 loop-region caused the dysregulations of specific gene expression. Moreover, the loss of RPB7 or CTD phosphatase subunit 1 (CTDP1) result in the defects in Pol II termination-reinitiation recycle. Together, our study demonstrates that RPB7/CTDP1 controls the dephosphorylation and stabilization of RNA Pol II to permit RNA Pol II termination to reinitiation recycle in mammalian cells.

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RPB7/CTDP1 stabilizes and licenses Pol II termination to reinitiation [ChAR-Seq]

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RPB7/CTDP1 stabilizes and licenses Pol II termination to reinitiation [RNA-Seq]

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RPB7/CTDP1 stabilizes and licenses Pol II termination to reinitiation

Project description:RPB7/CTDP1 stabilizes and licenses Pol II termination to reinitiation

| PRJNA926491 | ENA

CTDP1 and RPB7 stabilize Pol II and permit reinitiation.

Project description:The mechanisms governing the termination and subsequent reinitiation of RNA polymerase II (Pol II) remain poorly understood. Here we find that depletion of RPB7 leads to the destabilization of Pol II's largest subunit, RPB1. This destabilization is influenced by the loop regions of RPB7, CDK9, the C-terminal domain (CTD) of RPB1, and its linker region. The stabilization process of RPB1 is regulated by the E3 ubiquitin ligase Cullin 3. Additionally, RPB7 interacts with the phosphatase CTDP1, which is crucial for maintaining RPB1 stability. RPB7 is also vital for the reinitiation of Pol II, engages with RNA processing factors, and is localized to the RNA exit channel of the Pol II complex. The absence of RPB7 compromises RNA processing. We propose that RPB7 recruits CTDP1 to dephosphorylate Pol II, enhancing its stability and facilitating efficient reinitiation, adding an emerging dimension to transcriptional regulation.

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RPB7/CTDP1 stabilizes and licenses Pol II termination to reinitiation [ChIP-Seq]

Project description:RPB7/CTDP1 stabilizes and licenses Pol II termination to reinitiation [ChIP-Seq]

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