Tdrd6a recruits Ziwi-bound piRNAs and coordinates deposition of germ plasm mRNAs into primordial germ cells [small RNA]
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA421016 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR6345660.fastq.gz | Fastqsanger.gz | |||
| SRR6345655.fastq.gz | Fastqsanger.gz | |||
| SRR6345656.fastq.gz | Fastqsanger.gz | |||
| SRR6345657.fastq.gz | Fastqsanger.gz | |||
| SRR6345658.fastq.gz | Fastqsanger.gz |
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Project description:Tdrd6a recruits Ziwi-bound piRNAs and coordinates deposition of germ plasm mRNAs into primordial germ cells
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Project description:Germ plasm, the Balbiani body and nuage are evolutionary conserved structures essential for germ cell specification and maintenance. We describe Tdrd6a as a component of these structures with two distinct molecular functions. First, Tdrd6a facilitates the accumulation of the typical antisense-bias of piRNAs, without having effects on piRNA biogenesis signatures. Second, we show that Tdrd6a is required for Balbiani body and germ plasm integrity, and associates with RNA-binding proteins and germ plasm mRNAs. On the cell-biological level, maternally contributed Tdrd6a strongly impacts germ cell formation, but is dispensable for fertility. Using single-cell RNA-sequencing we demonstrate that Tdrd6a promotes early germ cell development and regulates the stoichiometry of germ plasm mRNAs. We propose that Tdrd6a functions as a scaffold to recruit correct ratios of germ plasm transcripts and to accumulate antisense piRNA complexes in order to ensure both specification and maintenance of germ cells.
2018-07-24 | GSE107682 | GEO
Project description:Germ plasm, the Balbiani body and nuage are evolutionary conserved structures essential for germ cell specification and maintenance. We describe Tdrd6a as a component of these structures with two distinct molecular functions. First, Tdrd6a facilitates the accumulation of the typical antisense-bias of piRNAs, without having effects on piRNA biogenesis signatures. Second, we show that Tdrd6a is required for Balbiani body and germ plasm integrity, and associates with RNA-binding proteins and germ plasm mRNAs. On the cell-biological level, maternally contributed Tdrd6a strongly impacts germ cell formation, but is dispensable for fertility. Using single-cell RNA-sequencing we demonstrate that Tdrd6a promotes early germ cell development and regulates the stoichiometry of germ plasm mRNAs. We propose that Tdrd6a functions as a scaffold to recruit correct ratios of germ plasm transcripts and to accumulate antisense piRNA complexes in order to ensure both specification and maintenance of germ cells.
2018-07-24 | GSE79283 | GEO
Project description:Germ plasm, the Balbiani body and nuage are evolutionary conserved structures essential for germ cell specification and maintenance. We describe Tdrd6a as a component of these structures with two distinct molecular functions. First, Tdrd6a facilitates the accumulation of the typical antisense-bias of piRNAs, without having effects on piRNA biogenesis signatures. Second, we show that Tdrd6a is required for Balbiani body and germ plasm integrity, and associates with RNA-binding proteins and germ plasm mRNAs. On the cell-biological level, maternally contributed Tdrd6a strongly impacts germ cell formation, but is dispensable for fertility. Using single-cell RNA-sequencing we demonstrate that Tdrd6a promotes early germ cell development and regulates the stoichiometry of germ plasm mRNAs. We propose that Tdrd6a functions as a scaffold to recruit correct ratios of germ plasm transcripts and to accumulate antisense piRNA complexes in order to ensure both specification and maintenance of germ cells.
2018-07-24 | GSE79161 | GEO
Project description:Aub protein guided by piRNAs ensures genome integrity by cleaving retrotransposons and genome propagation by trapping mRNAs to form the germ plasm that instructs germ cell formation. The amino terminus of Aub (Aub-NT) is rich in arginines (Aub-NTRs), which are symmetrically dimethylated (sDMAs), and interacts with Tudor protein and other Tudor domain containing proteins (Tdrds). Aub-Tdrd interactions play critical roles in suppressing active retrotransposons via piRNA amplification and in germ plasm formation via generation of Aub-Tudor ribonucleoproteins. Here we show that Aub-NTRs are dispensable for primary piRNA biogenesis but essential for piRNA amplification and transposon control and that sDMAs in Aub-NT are essential for germ plasm formation and germ cell specification, but largely dispensable for piRNA amplification and transposon control.
2020-12-14 | GSE155874 | GEO
Project description:The formation of germ cells is a critical issue for the continuation of species. A large group of animals follow a preformation strategy to generate their primordial germ cells (PGCs). They produce a set of localized maternal mRNAs and proteins to form phase-separated germ plasm that functions as the PGC determinants, but the mechanisms underlying the assembly of germ plasm is poorly understood. This study identifies Rbm24a as an enssential localized germ plasm protein component that controls the formation of large and functional germ plasm granules. Rbm24a is complexed with Buc and interacts with germ plasm mRNAs, which determines the specific grasp of germ plasm mRNAs into the phase-separated aggregates. Rbm24a-absent granules fail to undergo kinesin-dependent transport towards the cleavage furrows, where small particles fuse into large ones. The loss of maternal rbm24a causes the complete degradation of germ plasm components and the disappearance of PGCs, resulting in totally sterile animals. Our work establishes that Rbm24 is a critical nucleating organizer component of germ plasm, highlighting an emerging common mechanism to read and recruit RNA component into phase-separated condensates.
2025-01-24 | GSE267406 | GEO
Project description:Ribonucleoprotein (RNP) granules are the most common membrane-less biomolecular condensates. However, the mechanisms underlying their assembly are largely unknown. The aggregation of germ plasm determines the fate of primordial germ cells (PGCs) and serves as a model for RNP granule assembly. Here, we show that maternal RNA binding protein Rbm24a is the key factor governing specific sorting of mRNAs. Mechanistically, Rbm24a complexes with Buc and interacts to dictate the specific grasp of germ plasm mRNAs into phase-separated condensates. Germ plasm particles lacking Rbm24a and mRNAs fail to undergo kinesin-dependent transport towards the cleavage furrows where small granules fuse into large aggregates. Therefore, the loss of maternal Rbm24a causes a complete degradation of germ plasm and the disappearance of PGCs. These findings demonstrate that Rbm24a functions as a nucleating organizer of the germ plasm, highlighting an emerging mechanism for RNA-binding proteins in reading and recruiting RNA components into the phase-separated protein scaffold.
2024-10-27 | GSE279756 | GEO
Project description:The formation of germ cells is a critical issue for the continuation of species. A large group of animals follow a preformation strategy to generate their primordial germ cells (PGCs). They produce a set of localized maternal mRNAs and proteins to form phase-separated germ plasm that functions as the PGC determinants, but the mechanisms underlying the assembly of germ plasm is poorly understood. This study identifies Rbm24a as an enssential localized germ plasm protein component that controls the formation of large and functional germ plasm granules. Rbm24a is complexed with Buc and interacts with germ plasm mRNAs, which determines the specific grasp of germ plasm mRNAs into the phase-separated aggregates. Rbm24a-absent granules fail to undergo kinesin-dependent transport towards the cleavage furrows, where small particles fuse into large ones. The loss of maternal rbm24a causes the complete degradation of germ plasm components and the disappearance of PGCs, resulting in totally sterile animals. Our work establishes that Rbm24 is a critical nucleating organizer component of germ plasm, highlighting an emerging common mechanism to read and recruit RNA component into phase-separated condensates.
2025-02-01 | GSE288109 | GEO
Project description:Tdrd6a recruits Ziwi-bound piRNAs and coordinates deposition of germ plasm mRNAs into primordial germ cells [RIP-Seq]
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Project description:Tdrd6a recruits Ziwi-bound piRNAs and coordinates deposition of germ plasm mRNAs into primordial germ cells [scRNA-Seq]
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