Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The DUF3715 domain has a conserved role in RNA-directed transposon silencing

ABSTRACT: The DUF3715 domain has a conserved role in RNA-directed transposon silencing

PROVIDER: PRJNA982821 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR24900223.fastq.gz	Fastqsanger.gz
	SRR24900224.fastq.gz	Fastqsanger.gz
	SRR24900225.fastq.gz	Fastqsanger.gz
	SRR24900226.fastq.gz	Fastqsanger.gz
	SRR24900227.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 16

Similar Datasets

The DUF3715 domain has a conserved role in RNA-directed transposon silencing

Project description:RNA-directed transposon silencing operates in the mammalian soma and germline tosafeguard genomic integrity. The piRNA pathway and the HUSHcomplex identify activetransposons through recognition of their nascent transcripts, but mechanisticunderstanding of how these distinct pathways evolved is lacking. TASOR is anessential component of the HUSH complex. TASOR’s DUF3715 domain adopts apseudo-PARP structure and is required for transposon silencing in a mannerindependent of complex assembly. TEX15, an essential piRNA pathway factor, alsocontains the DUF3715 domain. Here, we show that TASOR’s and TEX15’s DUF3715domain share extensive structural homology. We found that the DUF3715 domain arosein early eukaryotes and that in vertebrates it is restricted to TEX15, TASOR, andTASORB orthologues. While TASOR-like proteins are found throughout metazoa,TEX15 is vertebrate specific. The branchingof TEX15 and TASOR-like DUF3715 domainlikely occurred in early metazoan evolution. Remarkably, despite this vast evolutionarydistance, the DUF3715 domain from divergent TEX15 sequences can functionallysubstitute for the same domain in TASOR and mediates transposon silencing. We havethus termed this domain of unknown function as the RNA-directed pseudo-PARPtransposon silencing (RDTS) domain. In summary, we show an unexpected functionallink between these critical transposon silencing pathways.

2023-10-26 | GSE234730 | GEO

CLSY docking to Pol IV requires a conserved domain critical for small RNA biogenesis and transposon silencing.

Project description:CLSY docking to Pol IV requires a conserved domain critical for small RNA biogenesis and transposon silencing.

| PRJNA1011929 | ENA

CLSY docking to Pol IV requires a conserved domain critical for small RNA biogenesis and transposon silencing

Project description:CLSY docking to Pol IV requires a conserved domain critical for small RNA biogenesis and transposon silencing

| PRJNA1165818 | ENA

Dimerisation of the PICTS complex via LC8/Cut-up drives co-transcriptional transposon silencing in Drosophila

Project description:In animal gonads, the PIWI-interacting RNA (piRNA) pathway guards genome integrity in part through the co-transcriptional gene silencing of transposon insertions. In Drosophila ovaries, piRNA-loaded Piwi detects nascent transposon transcripts and instructs heterochromatin formation through the Panoramix-induced co-transcriptional silencing (PICTS) complex, containing Panoramix, Nxf2 and Nxt1. Here, we report that the highly conserved dynein light chain LC8/Cut-up (Ctp) is an essential component of the PICTS complex. Loss of Ctp results in transposon de-repression and a reduction in repressive chromatin marks specifically at transposon loci. In turn, Ctp can enforce transcriptional silencing when artificially recruited to RNA and DNA reporters. We show that Ctp drives dimerisation of the PICTS complex through its interaction with conserved motifs within Panoramix. Artificial dimerisation of Panoramix bypasses the necessity for its interaction with Ctp, demonstrating that conscription of a protein from a ubiquitous cellular machinery has fulfilled a fundamental requirement for a transposon silencing complex.

2021-01-26 | PXD022103 | Pride

Dimerisation of the PICTS complex via LC8/Cut-up drives co-transcriptional transposon silencing in Drosophila

2021-01-26 | PXD022105 | Pride

TEX15 is an essential executor of MIWI2-directed transposon DNA methylation and silencing.

Project description:TEX15 is an essential executor of MIWI2-directed transposon DNA methylation and silencing.

| PRJNA631836 | ENA

TEX15 is an essential executor of MIWI2-directed transposon DNA methylation and silencing.

Project description:TEX15 is an essential executor of MIWI2-directed transposon DNA methylation and silencing.

| PRJEB38393 | ENA

TEX15 is an essential executor of MIWI2-directed transposon DNA methylation and silencing.

Project description:The PIWI protein MIWI2 and its associated PIWI-interacting RNAs (piRNAs) instruct DNA methylation of young active transposable elements (TEs) in the male germline. Here we show that MIWI2 associates with TEX15 in foetal gonocytes. TEX15 is predominantly a nuclear protein that is not required for piRNA biogenesis but is essential for piRNA-directed TE de novo methylation and silencing. In summary, TEX15 is an essential executor of mammalian piRNA-directed DNA methylation.

2020-06-18 | PXD019087 | Pride

A jumonji protein with E3 ligase and histone binding activities regulates transposon silencing in Arabidopsis

Project description:Transposable elements (TEs) make up a large proportion of eukaryotic genomes. As their mobilization creates genetic variation that threatens genome integrity, TEs are epigenetically silenced through several pathways and this may spread to neighboring sequences. JUMONJI (JMJ) proteins can function as anti-silencing factors and prevent silencing of genes next to TEs. Whether TE silencing is counterbalanced by the activity of anti-silencing factors is still unclear. Here, we characterize JMJ24 as a regulator of TE silencing. We show that loss of JMJ24 results in increased silencing of the DNA transposon AtMu1c, while overexpression of JMJ24 reduces silencing. JMJ24 has a JumonjiC (JmjC) domain and two RING domains. JMJ24 auto-ubiquitinates in vitro, demonstrating E3 ligase activity of the RING domain(s). JMJ24-JmjC binds the N-terminal tail of histone H3 and full-length JMJ24 binds histone H3 in vivo. JMJ24 activity is anti-correlated with histone H3 lysine 9 dimethylation (H3K9me2) levels at AtMu1c. Double mutant analyses with epigenetic silencing mutants suggest that JMJ24 antagonizes histone H3K9me2, and requires H3K9 methyltransferases for its activity on AtMu1c. Genome-wide transcriptome analysis indicates that JMJ24 affects silencing at additional TEs. Our results suggest that the JmjC domain of JMJ24 has lost demethylase activity but has been retained as a binding domain for histone H3. This is in line with phylogenetic analyses indicating that JMJ24 [with the mutated JmjC domain] is widely conserved in angiosperms. Taken together, this study assigns a role in TE silencing to a conserved JmjC-domain protein with E3 ligase activity, but no demethylase activity.

2016-03-18 | GSE72954 | GEO

CLSY docking to Pol IV requires a conserved domain critical for small RNA biogenesis and transposon silencing

Project description:RNA polymerase IV (Pol IV) transcribes transposable elements (TEs) into precursors for small interfering RNAs (siRNAs) that guide DNA methylation to silence these potentially dangerious mobile elements in plants. Pol IV is recruited to TEs via SNF2-like CLASSY (CLSY) proteins. How Pol IV evolved to partner with the CLSYs is unknown. Using phylogenetics, we identified a conserved CYC-YPMF motif that is specific to Pol IV’s largest subunit. Modeling predicts that this motif coordinates a zinc ion and is exposed near Pol IV’s surface in a domain contacting downstream DNA. Via immunoprecipitation and mass spectrometry we found that this motif is essential for the association of all four CLSYs with Pol IV and hereby designate it as a CLSY-docking motif. Consistent with these biochemical results, mutations in the CLSY-docking motif or in neighboring sites of the Pol IV clamp domain, phenocopy pol iv null mutants and display a near-total loss of siRNA biogenesis, resulting in defects in DNA methylation and TE silencing. Together, our findings provide structural and functional insights into a critical protein feature that distinguishes Pol IV from other RNA polymerases, allowing Pol IV to target, transcribe and limit the expression of TE regions, thereby protecting genome integrity.

2024-11-28 | PXD047743 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data