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Protease-mediated processing of Argonaute proteins controls small RNA association [small RNA RIP-seq]

ABSTRACT: Protease-mediated processing of Argonaute proteins controls small RNA association [small RNA RIP-seq]

PROVIDER: PRJNA658311 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12482648.fastq.gz	Fastqsanger.gz
	SRR12482649.fastq.gz	Fastqsanger.gz
	SRR12482650.fastq.gz	Fastqsanger.gz
	SRR12482651.fastq.gz	Fastqsanger.gz
	SRR12482652.fastq.gz	Fastqsanger.gz

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Protease-mediated processing of Argonaute proteins controls small RNA association [small RNA RIP-seq]

Project description:Small RNA pathways defend the germlines of animals against selfish genetic elements and help to maintain genomic integrity. At the same time, their activity needs to be well-controlled to prevent silencing of ‘self’ genes. Here, we reveal a proteolytic mechanism that controls endogenous small interfering (22G) RNA activity in the Caenorhabditis elegans germline to protect genome integrity and maintain fertility. We find that WAGO-1 and WAGO-3 Argonaute proteins are produced as pro-proteins that are matured through proteolytic processing of their unusually proline-rich N-termini. In the absence of DPF-3, a P-granule-localized N-terminal dipeptidase orthologous to mammalian DPP8/9, processing fails, causing a change of identity of 22G RNAs bound to these WAGO proteins. Accumulation of repeat- and transposon-derived transcripts, DNA damage and sterility ensue. We propose that DPF-3 acts as a licensing factor for 22G RNA activity.

2021-04-15 | GSE156540 | GEO