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A BRD4-mediated elongation control point primes transcribing RNA polymerase II for 3'-processing and termination

ABSTRACT: A BRD4-mediated elongation control point primes transcribing RNA polymerase II for 3'-processing and termination

PROVIDER: PRJNA667097 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12766519.fastq.gz	Fastqsanger.gz
	SRR12766520.fastq.gz	Fastqsanger.gz
	SRR12766521.fastq.gz	Fastqsanger.gz
	SRR12766522.fastq.gz	Fastqsanger.gz
	SRR12766523.fastq.gz	Fastqsanger.gz

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A BRD4-mediated elongation control point primes transcribing RNA polymerase II for 3'-processing and termination [nascONT-seq]

Project description:In this study, we reveal that BRD4 underlies a general 5'-elongation checkpoint that primes transcribing RNA polymerase II for 3'-RNA processing and transcription termination. BRD4-specific degradation impairs Pol II pause release, induces massive readthrough transcription, and RNA cleavage defects. Acute loss of BRD4 disrupts the recruitment of 3'-RNA processing factors.

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A BRD4-mediated elongation control point primes transcribing RNA polymerase II for 3'-processing and termination [nascONT-seq]

Project description:A BRD4-mediated elongation control point primes transcribing RNA polymerase II for 3'-processing and termination [nascONT-seq]

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A BRD4-mediated elongation control point primes transcribing RNA polymerase II for 3'-processing and termination

Project description:This SuperSeries is composed of the SubSeries listed below.

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CTD tyrosine phosphorylation impairs termination factor recruitment to transcribing RNA polymerase II

Project description:ChIP-chip was performed to identify the genomic binding locations for the termination factors Nrd1, and Rtt103, and for RNA polymerase (Pol) II phosphorylated at the tyrosine 1 and threonine 4 position of its C-terminal domain (CTD). In different phases of the transcription cycle, Pol II recruits different factors via its CTD, which consists of heptapeptide repeats with the sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7. Here we show that the CTD of transcribing yeast Pol II is phosphorylated at Tyr1, and that this impairs recruitment of termination factors. Tyr1 phosphorylation levels rise downstream of the transcription start site (TSS), and decrease before the polyadenylation (pA) site. Tyr1-phosphorylated gene bodies are depleted of CTD-binding termination factors Nrd1, Pcf11, and Rtt103. Tyr1 phosphorylation blocks CTD binding by these termination factors, but stimulates binding of elongation factor Spt6. These results show that CTD modifications can not only stimulate but also block factor recruitment, and lead to an extended CTD code for transcription cycle coordination.

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