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Germ granule association drives small RNA specificity for a nuclear Argonaute protein [sRNA-seq]

ABSTRACT: Germ granule association drives small RNA specificity for a nuclear Argonaute protein [sRNA-seq]

PROVIDER: PRJNA998763 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25428228.fastq.gz	Fastqsanger.gz
	SRR25428229.fastq.gz	Fastqsanger.gz
	SRR25428230.fastq.gz	Fastqsanger.gz
	SRR25428231.fastq.gz	Fastqsanger.gz
	SRR25428232.fastq.gz	Fastqsanger.gz

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Germ granule association drives small RNA specificity for a nuclear Argonaute protein [sRNA-seq]

Project description:RNA interference (RNAi) is a conserved gene silencing process that exists in diverse organisms to protect genome integrity and regulate gene expression. In C. elegans, majority of RNAi components are located in phase-separated perinuclear germ granules, including P granule, Mutator foci, Z granule, and SIMR foci. However, the protein components and function of the newly discovered SIMR foci are unknown. Here we identified HRDE-2 as a SIMR foci component, which interacts with the germline nuclear RNAi Argonaute HRDE-1. We found that unloaded HRDE-1 localizes to SIMR foci and this localization depends on HRDE-2. In addition, HRDE-2 contributes to HRDE-1 small RNAs binding specificity and, in the absence of HRDE-2, HRDE-1 exclusively loads CSR-class 22G-RNAs rather than WAGO-class 22G-RNAs, promotes H3K9me3 deposition on CSR-targets, but does not silence these CSR-target genes. Thus, our study demonstrates that HRDE-2 is critical to ensure correct small RNAs are used to guide nuclear RNA silencing in the C. elegans germline.

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Germ granule association drives small RNA specificity for a nuclear Argonaute protein

Project description:Germ granule association drives small RNA specificity for a nuclear Argonaute protein

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Germ granule association drives small RNA specificity for a nuclear Argonaute protein [mRNA-seq]

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Germ granule association drives small RNA specificity for a nuclear Argonaute protein [CUT&Tag]

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Germ granule association drives small RNA specificity for a nuclear Argonaute protein [mRNA-seq]

Project description:Germ granule association drives small RNA specificity for a nuclear Argonaute protein [mRNA-seq]

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Germ granule association drives small RNA specificity for a nuclear Argonaute protein [CUT&Tag]

Project description:Germ granule association drives small RNA specificity for a nuclear Argonaute protein [CUT&Tag]

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Germ granule association drives small RNA specificity for a nuclear Argonaute protein

Project description:RNA interference (RNAi) is a conserved gene silencing process that exists in diverse organisms to protect genome integrity and regulate gene expression. In C. elegans, the majority of RNAi pathway proteins localize to perinuclear, phase-separated germ granules, which are comprised of sub-domains referred to as P granules, Mutator foci, Z granules, and SIMR foci. However, the protein components and function of the newly discovered SIMR foci are unknown. Here we demonstrate that HRDE-2 localizes to SIMR foci and interacts with the germline nuclear RNAi Argonaute HRDE-1. Furthermore, HRDE-1 also localizes to SIMR foci, dependent on HRDE-2, but only in its small RNA unbound state. This germ granule localization is critical to promote the small RNA binding specificity of HRDE-1 and, in the absence of HRDE-2, HRDE-1 exclusively loads CSR-class 22G-RNAs rather than WAGO-class 22G-RNAs, resulting in H3K9me3 deposition on CSR-target genes. Thus, our study demonstrates that HRDE-2 is critical to ensure that the correct small RNAs are used to guide nuclear RNA silencing in the C. elegans germline.

2023-07-27 | MSV000092546 | MassIVE

Germ granule association drives small RNA specificity for a nuclear Argonaute protein

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

2023-08-01 | GSE239291 | GEO

Distinct Functions of Argonaute Slicer in siRNA Maturation and Heterochromatin Formation

Project description:Small-RNA (sRNA)-guided transcriptional gene silencing by Argonaute (Ago)-containing complexes is fundamental to genome integrity and epigenetic inheritance. The RNA cleavage (“Slicer”) activity of Argonaute has been implicated in both sRNA maturation and target RNA cleavage. Typically, Argonaute slices and releases the passenger strand of duplex sRNA to generate active silencing complexes, but it remains unclear whether slicing of target nascent RNAs, or other RNAi components, also contributes to downstream transcriptional silencing. Here, we develop a strategy for loading the fission yeast Ago1 with a single-stranded sRNA guide, which bypasses the requirement for slicer activity in generation of active silencing complexes. We show that slicer-defective Ago1 can mediate secondary sRNA generation, H3K9 methylation, and silencing similar to or better than wild-type and associates with chromatin more efficiently. The results define an ancient and minimal sRNA-mediated chromatin silencing mechanism, which resembles the germline-specific sRNA-dependent transcriptional silencing pathways in Drosophila and mammals. This SuperSeries is composed of the SubSeries listed below.

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Reprograming of sRNA target specificity by the leader peptide peTrpL in response to antibiotic exposure

Project description:Trans-acting regulatory RNAs have the capacity to base pair with more mRNAs than experimentally detected under given conditions. This raises the question whether the sRNA target specificity can change upon metabolic or environmental changes. In Sinorhizobium meliloti, the sRNA rnTrpL is derived from a tryptophan (Trp) transcription attenuator, which is located upstream of the Trp biosynthesis gene trpE(G) and harbors the small ORF trpL. When Trp is available, efficient trpL translation causes transcription termination and liberation of rnTrpL, which then downregulates the trpDC operon. On the other hand, the trpL-encoded leader peptide peTrpL has a Trp-independent role in posttranscriptional regulation of antibiotic resistance. Here, we show that upon tetracycline (Tc) exposure, rnTrpL accumulates independently of Trp availability. Further, we provide evidence that both rnTrpL and peTrpL act together in the Tc-dependent destabilization of rplUrpmA mRNA encoding ribosomal proteins L21 and L27. rnTrpL, peTrpL and rplUrpmA mRNA were copurified in an antibiotic- dependent ribonucleoprotein complex (ARNP). In vitro ARNP reconstitution with competing trpD and rplU transcripts revealed that peTrpL and Tc reprogram the rnTrpL specificity in favor of rplU. In vivo, this probably supports bacterial adaptation to antibiotics. Our findings provide evidence for sRNA reprograming in response to antibiotic exposure.

2021-08-10 | PXD019516 | Pride

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