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The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE116068 | GEO | 2018/06/21

REPOSITORIES: GEO

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The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing.

Project description:In eukaryotes, heterochromatin regions are typically subjected to transcriptional silencing. DNA methylation has an important role in such silencing and has been studied extensively. However, little is known about how methylated heterochromatin regions are subjected to silencing. We conducted a genetic screen and identified an epcr (enhancer of polycomb-related) mutant that releases heterochromatin silencing in Arabidopsis thaliana We demonstrated that EPCR1 functions redundantly with its paralog EPCR2 and interacts with PWWP domain-containing proteins (PWWPs), AT-rich interaction domain-containing proteins (ARIDs), and telomere repeat binding proteins (TRBs), thus forming multiple functionally redundant protein complexes named PEAT (PWWPs-EPCRs-ARIDs-TRBs). The PEAT complexes mediate histone deacetylation and heterochromatin condensation and thereby facilitate heterochromatin silencing. In heterochromatin regions, the production of small interfering RNAs (siRNAs) and DNA methylation is repressed by the PEAT complexes. The study reveals how histone deacetylation, heterochromatin condensation, siRNA production, and DNA methylation interplay with each other and thereby maintain heterochromatin silencing.

| S-EPMC6166130 | biostudies-literature

The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing

Project description:In eukaryotes, heterochromatin regions are typically subjected to transcriptional silencing. DNA methylation has an important role in such silencing, and has been studied extensively. However, little is known about how methylated heterochromatin regions are subjected to silencing. We conducted a genetic screen and identified an epcr (enhancer of polycomb-related) mutant that releases heterchromatin silencing in Arabidopsis thaliana. We demonstrated that EPCR1 functions redundantly with its paralog EPCR2 and interacts with PWWP domain-containing proteins (PWWPs), AT-rich interaction domain-containing proteins (ARIDs), and telomere repeat binding proteins (TRBs), thus forming multiple functionally redundant protein complexes named PEAT (PWWPs-EPCRs-ARIDs-TRBs). The PEAT complexes mediate histone deacetylation and heterochromatin condensation and thereby facilitate heterochromatin silencing. In heterochromatin regions, the production of small interfering RNAs (siRNAs) and DNA methylation are repressed by the PEAT complexes. The study reveals how histone deacetylation, heterochromatin condensation, siRNA production, and DNA methylation interplay with each other and thereby maintain heterochromatin silencing.

| S-SCDT-EMBOJ-2017-98770 | biostudies-other

The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing [smallRNA-Seq]

Project description:We found PEAT complexes mediate histone deacetylation and heterochromatin condensation and thereby facilitate heterochromatin silencing.

2018-06-21 | GSE116067 | GEO

The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing [RNA-Seq]

Project description:We found PEAT complexes mediate histone deacetylation and heterochromatin condensation and thereby facilitate heterochromatin silencing.

2018-06-21 | GSE116066 | GEO

The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing [ChIP-Seq]

Project description:We found PEAT complexes mediate histone deacetylation and heterochromatin condensation and thereby facilitate heterochromatin silencing.

2018-06-21 | GSE116065 | GEO

The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing [BS-Seq]

Project description:We found PEAT complexes mediate histone deacetylation and heterochromatin condensation and thereby facilitate heterochromatin silencing.

2018-06-21 | GSE116064 | GEO

The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing

Project description:The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing

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Histone deacetylation promotes transcriptional silencing at facultative heterochromatin.

Project description:It is important to accurately regulate the expression of genes involved in development and environmental response. In the fission yeast Schizosaccharomyces pombe, meiotic genes are tightly repressed during vegetative growth. Despite being embedded in heterochromatin these genes are transcribed and believed to be repressed primarily at the level of RNA. However, the mechanism of facultative heterochromatin formation and the interplay with transcription regulation is not understood. We show genome-wide that HDAC-dependent histone deacetylation is a major determinant in transcriptional silencing of facultative heterochromatin domains. Indeed, mutation of class I/II HDACs leads to increased transcription of meiotic genes and accumulation of their mRNAs. Mechanistic dissection of the pho1 gene where, in response to phosphate, transient facultative heterochromatin is established by overlapping lncRNA transcription shows that the Clr3 HDAC contributes to silencing independently of SHREC, but in an lncRNA-dependent manner. We propose that HDACs promote facultative heterochromatin by establishing alternative transcriptional silencing.

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The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing [BS-Seq]

Project description:The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing [BS-Seq]

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The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing [RNA-Seq]

Project description:The PEAT protein complexes are required for histone deacetylation and heterochromatin silencing [RNA-Seq]

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