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Protein UFMylation regulates ribosomal DNA double-stranded break repair

ABSTRACT: Protein UFMylation regulates ribosomal DNA double-stranded break repair

PROVIDER: PRJNA1067156 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27669141.fastq.gz	Fastqsanger.gz
	SRR27669142.fastq.gz	Fastqsanger.gz
	SRR27669143.fastq.gz	Fastqsanger.gz
	SRR27669144.fastq.gz	Fastqsanger.gz
	SRR27669145.fastq.gz	Fastqsanger.gz

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Protein UFMylation regulates ribosomal DNA double-stranded break repair

Project description:Ribosomal DNA (rDNA) arrays are highly repetitive regions of the genome which encode essential genes required to produce ribosomes. DNA double-stranded breaks (DSBs) generated within rDNA genes elicit a unique cellular response involving robust transcriptional silencing and nucleolar reorganization into ‘cap’ structures at the nucleolar periphery. This process is coordinated by the nucleolar scaffolding protein TCOF1, which functions to recruit the DNA repair proteins NBS1 and TOPBP1 that activate the ATM and ATR kinases, resulting in ribosomal RNA (rRNA) transcriptional silencing and nucleolar segregation. However, the DNA damage and repair response at rDNA arrays remains incompletely understood. Here, we investigate the cellular response to rDNA DSBs using proteomics and genetic CRISPR-Cas9 screening. We show that the protein UFMylation pathway and the HUSH complex are important for cell viability and survival in response to rDNA DSBs, and that the E3 UFM1-ligase UFL1 and its heterodimer DDRGK1 are associated with TCOF1 at nucleolar caps. Loss of UFL1 leads to impaired ATM activation, reduced rRNA transcriptional silencing, and an overall reduction in nucleolar segregation. We identified ATM, UNC45A and SMC6 as UFMylated proteins, in which UFMylation may facilitate ATM activation and segregation of damaged rDNA to the nucleolar periphery. Altogether, our findings provide the first evidence for a role for UFMylation in rDNA DSB repair.

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Protein UFMylation regulates ribosomal DNA double-stranded break repair

2024-09-16 | PXD048568 | Pride

Ribosomal protein RPL26 is the principal target of UFMylation

Project description:UFM1 is a small, metazoan-specific, ubiquitin-like protein modifier that is essential for embryonic development. Although loss-of-function mutations in UFM1 conjugation are linked to ER stress, neither the biological function nor the relevant cellular targets of this protein modifier are known. Here we show that a largely uncharacterized ribosomal protein, RPL26, is the principal target of UFM1 conjugation. RPL26 UFMylation and deUFMylation is catalyzed by enzyme complexes tethered to the cytoplasmic surface of the ER and UFMylated RPL26 is highly enriched on ER membrane-bound ribosomes and polysomes. Biochemical analysis and structural modeling establish that UFMylated RPL26 and the UFMylation machinery are in close proximity to the SEC61 translocon, suggesting that this modification plays a direct role in cotranslational protein translocation into the ER. These data suggest that UFMylation is a ribosomal modification specialized to facilitate metazoan-specific protein biogenesis at the ER.

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UFMylation orchestrates chromatin engagement of core NHEJ components to promote DNA double-strand break repair

Project description:DNA double-strand breaks (DSBs) are highly cytotoxic lesions that – if misrepaired – can lead to genomic instability, cancer, and developmental disorders. While ubiquitin and select ubiquitin-like proteins (UBLs) are established regulators of DSB repair, many UBLs remain understudied. Here, through systematic UBL screening, we identify UFM1 as a novel regulator of non-homologous end-joining (NHEJ). Using a photo-crosslinkable UFM1 probe, we uncover core NHEJ components, including XRCC4, as downstream UFM1 receptors. Complementary proximity screening reveals UFMylated Ku70 as a key upstream target recognised by XRCC4. Mechanistically, UFMylation facilitates chromatin recruitment and assembly of NHEJ factors, establishing a central role in end-joining repair. Our findings link hereditary UFMylation disorders to defective NHEJ processes, contributing to our molecular understanding of diseases biology. Beyond this, our bottom-up screening strategy reveals broader networks of UFM1-regulated factors, featuring diverse roles in genome maintenance and cellular homeostasis.

2026-07-31 | PXD069185 | Pride

Ribosomal protein RPL26 is the principal target of UFMylation

Project description:Ribosomal protein RPL26 is the principal target of UFMylation

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RAD51 proximity mapping reveals spatial constraints on homology search during DNA double-stranded break repair

Project description:RAD51 proximity mapping reveals spatial constraints on homology search during DNA double-stranded break repair

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RAD51 proximity mapping reveals spatial constraints on homology search during DNA double-stranded break repair

Project description:RAD51 proximity mapping reveals spatial constraints on homology search during DNA double-stranded break repair

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RAD51 proximity mapping reveals spatial constraints on homology search during DNA double-stranded break repair

Project description:RAD51 proximity mapping reveals spatial constraints on homology search during DNA double-stranded break repair