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Stress-induced multimerization of MYC shields stalled replication forks from RNA Polymerase

ABSTRACT: Stress-induced multimerization of MYC shields stalled replication forks from RNA Polymerase

PROVIDER: PRJNA759183 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15677311.fastq.gz	Fastqsanger.gz
	SRR15677312.fastq.gz	Fastqsanger.gz
	SRR15677313.fastq.gz	Fastqsanger.gz
	SRR15677314.fastq.gz	Fastqsanger.gz
	SRR15677315.fastq.gz	Fastqsanger.gz

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Multimerization of MYC shields stalled replication forks from RNA polymerase

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Multimerization of MYC shields stalled replication forks from RNA polymerase

Project description:Oncoproteins of the MYC family drive the development of numerous human tumors. In unperturbed cells, MYC proteins bind to virtually all active promoters and control transcription by RNA Polymerase II (RNAPII). MYC proteins can also coordinate transcription with DNA replication and promote the repair of transcription-associated DNA damage, but how they exert these mechanistically diverse functions is unknown. Here we show that MYC dissociates from many of its binding sites in active promoters and forms multimeric, often sphere-like structures in response to perturbation of transcription elongation, mRNA splicing or inhibition of the proteasome. Multimerization is accompanied by a global change in the MYC interactome towards proteins involved in transcription termination and RNA processing. MYC multimers accumulate on chromatin immediately adjacent to stalled replication forks and surround FANCD2, ATR and BRCA1 proteins, which are located at stalled forks. MYC multimerization is triggered in a HUWE1 and ubiquitylation-dependent manner. At active promoters, MYC multimers block antisense transcription and stabilize FANCD2 association with chromatin. This limits DNA double-strand break formation during S-phase and allows rapid recovery from replication stress, suggesting that multimerization of MYC enables tumor cells to proliferate under stressful conditions

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Multimerization of MYC shields stalled replication forks from RNA polymerase [4sU-seq]

Project description:Multimerization of MYC shields stalled replication forks from RNA polymerase [4sU-seq]

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Multimerization of MYC shields stalled replication forks from RNA polymerase [BLISS]

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Multimerization of MYC shields stalled replication forks from RNA polymerase [4sU-seq]

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Multimerization of MYC shields stalled replication forks from RNA polymerase [CUT&RUN, ChIP-seq]

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Multimerization of MYC shields stalled replication forks from RNA polymerase [CUT&RUN, ChIP-seq]

Project description:Multimerization of MYC shields stalled replication forks from RNA polymerase [CUT&RUN, ChIP-seq]

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Stress-induced multimerization of MYC shields stalled replication forks from RNA Polymerase

Project description:Oncoproteins of the MYC family drive the development of numerous human tumors1-4. In unperturbed cells, MYC proteins bind to virtually all active promoters and control transcription by RNA Polymerase II (RNAPII)2,3,5,6. MYC proteins can also coordinate transcription with DNA replication7-9 and promote the repair of transcription-associated DNA damage10, but how they exert these mechanistically diverse functions is unknown. Here we show that MYC dissociates from most of its binding sites in promoters and forms stable multimeric shell-like structures in response to perturbation of transcription elongation, mRNA splicing, or DNA replication. MYC multimers recruit interacting proteins that can promote transcription termination into their shells. Intriguingly, MYC multimers accumulate on chromatin immediately adjacent to stalled replication forks and surround the FANCD2, ATR and BRCA1 proteins, which are located at stalled forks11,12. MYC multimers accumulate ubiquitylated proteins and their formation depends on the HUWE1 ubiquitin ligase10,13. In response to replication stress, HUWE1 and MYC limit phosphorylation of the single-strand binding protein, RPA. We propose that localised multimerisation of MYC creates a transcription termination zone around stalled replication forks that limits checkpoint signalling in response to transcriptional and replication stress, allowing tumor cells to actively proliferate under stressful conditions

2022-09-08 | GSE183094 | GEO

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