Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Drosophila melanogaster

ABSTRACT: Antisense piRNA amplification, but not piRNA production or nuage assembly, requires the tudor domain protein Qin.

PROVIDER: PRJNA198015 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR891294.fastq.gz	Fastqsanger.gz
	SRR891295.fastq.gz	Fastqsanger.gz
	SRR891296.fastq.gz	Fastqsanger.gz
	SRR891297.fastq.gz	Fastqsanger.gz
	SRR891298.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 11

Similar Datasets

Characterization of expression changes in qin by tiling array

2011-11-18 | GSE30061 | GEO

Characterization of expression changes in qin by tiling array

Project description:Qin, a novel protein comprising amino-terminal E3 ligase and five carboxy terminal Tudor domains, silences transposons and ensures genome stability in the Drosophila germline by promoting antisene piRNA amplification via Aubergine:Ago3 Ping-Pong and preventing futile Aubergine:Aubergine interactions. Extract total ovary RNAs, and using tiling array to test transposon as well as gene expression in wild-type and qin mutant flies. Three biological replicates are used.

2011-11-18 | E-GEOD-30061 | biostudies-arrayexpress

Zuc or Armi IP proteome from DTME-crosslinked Drosophila ovaries

Project description:The proteome of target protein (Armi or Zuc) immunoprecipitation and control immunoprecipitation performed in parallel in three biological replicates, as described in Ge et al., 2019, The RNA-binding ATPase, Armitage, Couples piRNA Amplification in Nuage to Phased piRNA Production on Mitochondria, published in Molecular Cell.

2019-03-26 | MSV000083634 | MassIVE

The tudor domain protein Kumo is required to assemble the nuage and to generate germline piRNAs in Drosophila

Project description:We are submitting two small RNA libraries derived from ovarian tissue of mutant and heterozygous for the Kumo/Qin gene, required for the piRNA production in germline cells. In absence of Kumo/Qin, piRNA production is reduced and transposons are derepressed. Analysis of piRNA production in Kumo/Qin mutants

2011-12-31 | E-GEOD-34728 | biostudies-arrayexpress

Modulation of Aub–Tdrd interactions elucidates piRNA amplification and germ plasm formation

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

The tudor domain protein Kumo is required to assemble the nuage and to generate germline piRNAs in Drosophila

2011-12-31 | GSE34728 | GEO

Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members

Project description:In germ cells, Piwi proteins interact with a specific class of small non-coding RNAs, piwi-interacting RNAs (piRNAs). Together, these form a pathway that represses transposable elements, thus safeguarding germ cell genomes. While basic models describe the operation of piRNA pathways, neither the protein compositions of Piwi complexes, the critical protein-protein interactions that drive small RNA production and target recognition, or the precise molecular consequences of conserved localization to germline structures, call nuage, is well understood. We purified the three murine Piwi family proteins, Mili, Miwi, and Miwi2, from mouse germ cells and characterized their interacting protein partners. Piwi proteins were found in complex with Prmt5/Wdr77, an enzyme that di-methylates arginine residues. By immunoprecipitation with specific antibodies and by mass spectrometry, we found that Piwi proteins are arginine methylated at conserved positions in their amino termini. These modifications are essential to direct complex formation with specific Tudor-domain proteins, whose interactions with Piwis can be required for localization of RNP complexes in cytoplasmic nuage, proper piRNA expression, and transposon silencing. Considered together, our findings indicate that arginine methylation drives the assembly of multi-protein machines whose integrity and specific sub-cellular localization is necessary for efficient function of the piRNA pathway. Keywords: gene regulation study Total small RNA in embryonic and post-birth mouse testes of tdrd1 and tdrd6 mutants

2009-07-25 | E-GEOD-17319 | biostudies-arrayexpress

piRNA libraries from Drosophila melanogaster ovaries

Project description:Drosophila Piwi-family proteins have been implicated in transposon control. Here, we examine piwi-interacting RNAs (piRNAs) associated with each Drosophila Piwi protein and find that Piwi and Aubergine bind RNAs that are predominantly antisense to transposons, whereas Ago3 complexes contain predominantly sense piRNAs. As in mammals, the majority of Drosophila piRNAs are derived from discrete genomic loci. These loci comprise mainly defective transposon sequences, and some have previously been identified as master regulators of transposon activity. Our data suggest that heterochromatic piRNA loci interact with potentially active, euchromatic transposons to form an adaptive system for transposon control. Complementary relationships between sense and antisense piRNA populations suggest an amplification loop wherein each piRNA-directed cleavage event generates the 5’ end of a new piRNA. Thus, sense piRNAs, formed following cleavage of transposon mRNAs, may enhance production of antisense piRNAs, complementary to active elements, by directing cleavage of transcripts from master control loci. Keywords: small RNA libraries from Drosophila ovaries

2007-03-08 | GSE6734 | GEO

RNA clamping by Vasa assembles a piRNA Amplifier complex on transposon transcripts

Project description:Germline-specific Piwi-interacting RNAs (piRNAs) protect the genome against selfish genetic elements and are essential for fertility in animals. piRNAs targeting active transposons are amplified by a feed-forward loop known as the Ping-pong cycle, which links endonucleolytic slicing of target RNAs by Piwi proteins to biogenesis of new piRNAs. However, the biochemical framework for this pathway remains elusive. Here, we describe the identification of a transient Amplifier complex mediating the biogenesis of secondary piRNAs in insect cells. This complex is nucleated by the RNA helicase Vasa and contains the two Piwi proteins participating in the Ping-pong loop, the Tudor protein Qin/Kumo and antisense piRNA guides. These components assemble on the surface of Vasa's helicase domain, which functions as an RNA clamp to anchor Amplifier onto transposon transcripts. We show that ATP-dependent RNP remodelling by Vasa facilitates the transfer of 5'-sliced piRNA precursors between the Ping-pong partners, and failure to achieve this results in Drosophila female sterility. Immunoprecipitated small RNA were purified from untransfected or transfected Bmn4 cells for preparation of high-throughput sequencing libraries.

2014-06-04 | E-GEOD-57420 | biostudies-arrayexpress

Drosophila melanogaster

Project description:piRNA production requires heterochromatin formation in Drosophila

| PRJNA143921 | ENA