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A structural role for histone methyltransferase MET-2 represses transcription independent of H3K9me catalysis [RNA-seq]

ABSTRACT: A structural role for histone methyltransferase MET-2 represses transcription independent of H3K9me catalysis [RNA-seq]

PROVIDER: PRJNA714608 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR13964554.fastq.gz	Fastqsanger.gz
	SRR13964555.fastq.gz	Fastqsanger.gz
	SRR13964556.fastq.gz	Fastqsanger.gz
	SRR13964557.fastq.gz	Fastqsanger.gz
	SRR13964558.fastq.gz	Fastqsanger.gz

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A structural role for histone methyltransferase MET-2 represses transcription independent of H3K9me catalysis

Project description:A structural role for histone methyltransferase MET-2 represses transcription independent of H3K9me catalysis

| PRJNA714603 | ENA

A structural role for histone methyltransferase MET-2 represses transcription independent of H3K9me catalysis [ChIP-seq]

Project description:Packaging genomic regions into silenced heterochromatin is critical to maintain organismal viability and tissue identity. Methylation of histone H3 on lysine 9 (H3K9me) marks heterochromatin. Here we show that in addition to catalyzing H3K9me, the C. elegans histone methyltransferase MET-2 (SETDB1-like) has a second non-catalytic function that can itself contribute to gene repression. We find that subnuclear concentrates, or foci, of MET-2 correlate with efficient HMT activity, yet foci composed of catalytic-deficient MET-2 are also able to mediate transcriptional silencing. Genetic ablation of met-2 or physiological disruption of MET-2 foci by heat stress results in loss of silencing coincident with an increase in histone acetylation. Restoration of catalytically deficient MET-2 foci mitigates H3K9 and H3K27 hyperacetylation, gene derepression, and infertility, demonstrating a structural role for foci of a conserved heterochromatic histone methyltransferase in gene silencing independent of its enzymatic activity.

2021-08-01 | GSE168923 | GEO

A structural role for histone methyltransferase MET-2 represses transcription independent of H3K9me catalysis [RNA-seq]

2021-08-01 | GSE168924 | GEO

A structural role for histone methyltransferase MET-2 represses transcription independent of H3K9me catalysis [ChIP-seq]

Project description:A structural role for histone methyltransferase MET-2 represses transcription independent of H3K9me catalysis [ChIP-seq]

| PRJNA714607 | ENA

A structural role for histone methyltransferase MET-2 represses transcription independent of H3K9me catalysis

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

2021-08-01 | GSE168925 | GEO

Argonaute protein binding Met-tRNAiMet represses translation initiation

Project description:Argonaute protein binding Met-tRNAiMet represses translation initiation

| PRJNA750397 | ENA

Argonaute protein binding Met-tRNAiMet represses translation initiation

Project description:Initiation factor 2 (eIF2) delivering the initiator methionine transfer RNA (Met-tRNAiMet) to the ribosome is a conserved key step in translation initiation. Argonaute (Ago) proteins were initially identified as eukaryotic translation initiation factor 2C,2 (EIF2C2). In the past 2 decades, Argonaute were extensively studied as a core component of RNA induced gene silencing, although various model raised the exact mechanism of Ago in translation repression remains elusive. Here we found Ago protein directly bind Met- tRNAiMet independent of miRNA binding, which interfere the formation of the ternary complex eIF2–GTP–Met- tRNAiMet. Ago proteins can solely inhibit protein synthesis via competing tRNAiMet with eIF2. Our findings elucidate a physical link between Ago and tRNAiMet and provide mechanistic insight into translation repression by Ago proteins.

2022-02-01 | GSE181004 | GEO

An unstructured MET-2/SETDB1 cofactor ensures H3K9me2, focus formation and perinuclear anchoring [RNA-seq]

Project description:The segregation of the genome into accessible euchromatin and histone H3 lysine 9 methylated (H3K9me) heterochromatin is essential for the repression of repetitive elements and tissue-specific genes. In C. elegans, the SETDB1 homolog MET-2 catalyzes H3K9me1 and me2. In worms as in vertebrates, the regulation of this crucial enzyme remains enigmatic. Contrary to the localization of overexpressed MET-2, we find endogenous MET-2 to be nuclear throughout development, enriched in perinuclear foci in a cell cycle-dependent manner. We show by mass spectrometry that MET-2 associates with a highly unstructured protein, LIN-65, and a conserved GTPase effector ARLE-14. All three colocalize at heterochromatic foci. Ablation of lin-65, but not arle-14, mislocalizes and destabilizes MET-2, resulting in decreased H3K9me2, derepression of MET-2 targets, and loss of fertility. Importantly, mutation of met-2 or lin-65 is sufficient to disrupt the perinuclear clustering of heterochromatin genome-wide. Thus, LIN-65 is an essential cofactor of MET-2 required for H3K9me2 deposition, heterochromatin clustering, perinuclear anchoring, and transcriptional repression.

2019-02-06 | GSE122339 | GEO

An unstructured MET-2/SETDB1 cofactor ensures H3K9me2, focus formation and perinuclear anchoring [ChIP-seq]

2019-02-06 | GSE122335 | GEO

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Project description:This SuperSeries is composed of the following subset Series: GSE32180: MIWI catalysis is required for piRNA amplification-independent LINE1 transposon silencing [microarray] GSE32184: MIWI catalysis is required for piRNA amplification-independent LINE1 transposon silencing [deep sequencing] Refer to individual Series

2011-11-30 | E-GEOD-32183 | biostudies-arrayexpress

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