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The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing [RNA-seq]

ABSTRACT: The mechanism by which MORPHEUS'MOLECULE1 (MOM1) contributes to transcriptional gene silencing remained elusive since the gene was first identified and characterized (Amedeo et al., 2000). Here, we report that two PIAS (PROTEIN INHIBITOR OF ACTIVATED STAT)-type SUMO E3 ligase-like proteins PIAL1 and PIAL2 function redundantly to mediate transcriptional silencing at MOM1 target loci. PIAL1 and PIAL2 physically interact with each other and with MOM1 to form a high-molecular-weight complex. In the absence of either PIAL2 or MOM1, the formation of the high-molecular-weight complex was disrupted. We identified a previously uncharacterized IND (interacting domain) in PIAL1 and PIAL2, and demonstrated that IND directly interacts with MOM1. The CMM2 (conserved MOM1 motif 2) domain of MOM1 was previously shown to be required for the dimerization of MOM1. We demonstrated that the CMM2 domain is also required for the interaction of MOM1 with PIAL1 and PIAL2. We found that although PIAL2 has a SUMO E3 ligase activity, the activity is dispensable for PIAL2 in transcriptional silencing. This study suggests that PIAL1 and PIAl2 act as components of the MOM1-containing complex to mediate transcriptional silencing at heterochromatin regions.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE80301 | GEO | 2016/04/15

SECONDARY ACCESSION(S): PRJNA318519

REPOSITORIES: GEO

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The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing [Bisulfite-seq]

Project description:The mechanism by which MORPHEUS'MOLECULE1 (MOM1) contributes to transcriptional gene silencing remained elusive since the gene was first identified and characterized (Amedeo et al., 2000). Here, we report that two PIAS (PROTEIN INHIBITOR OF ACTIVATED STAT)-type SUMO E3 ligase-like proteins PIAL1 and PIAL2 function redundantly to mediate transcriptional silencing at MOM1 target loci. PIAL1 and PIAL2 physically interact with each other and with MOM1 to form a high-molecular-weight complex. In the absence of either PIAL2 or MOM1, the formation of the high-molecular-weight complex was disrupted. We identified a previously uncharacterized IND (interacting domain) in PIAL1 and PIAL2, and demonstrated that IND directly interacts with MOM1. The CMM2 (conserved MOM1 motif 2) domain of MOM1 was previously shown to be required for the dimerization of MOM1. We demonstrated that the CMM2 domain is also required for the interaction of MOM1 with PIAL1 and PIAL2. We found that although PIAL2 has a SUMO E3 ligase activity, the activity is dispensable for PIAL2 in transcriptional silencing. This study suggests that PIAL1 and PIAl2 act as components of the MOM1-containing complex to mediate transcriptional silencing at heterochromatin regions.

2016-04-15 | GSE80302 | GEO

Sumoylation at Chromatin Governs Coordinated Repression of a Transcriptionnal Program Essential for Cell Growth and Proliferation

Project description:mRNA profiling of WI38 wild-type or overexpressiong the SUMO E3 ligase PIASy in human primary fibroblasts 24h post-infection. The goal of this study is to analyse transcriptional changes in cells over-expressing the SUMO E3 ligase PIASy and to compare them with ChIPseq data for several histones marks and proteins of the SUMO machinery including PIASy

2013-11-25 | E-MEXP-3776 | biostudies-arrayexpress

The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing

Project description:The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing

| PRJNA318515 | ENA

Arabidopsis thaliana

Project description:The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing [RNA-seq]

| PRJNA318519 | ENA

Arabidopsis thaliana

Project description:The SUMO E3 ligase-like proteins PIAL1 and PIAL2 interact with MOM1 and form a novel complex required for transcriptional silencing [Bisulfite-seq]

| PRJNA318520 | ENA

The MOM1 complex recruits the RdDM machinery via MORC6 to establish de novo DNA methylation.

Project description:MOM1 is an Arabidopsis factor previously shown to mediate transcriptional silencing independent of major DNA methylation changes. Here we found that MOM1 localizes with sites of RNA-directed DNA methylation (RdDM). Tethering MOM1 with artificial zinc finger to unmethylated FWA promoter led to establishment of DNA methylation and FWA silencing. This process was blocked by mutations in components of the Pol V arm of the RdDM machinery, as well as by mutation of MORC6. We found that at some endogenous RdDM sites, MOM1 is required to maintain DNA methylation and a closed chromatin state. In addition, efficient silencing of newly introduced FWA transgenes was impaired by mutation of MOM1 or mutation of genes encoding the MOM1 interacting PIAL1/2 proteins. In addition to RdDM sites, we identified a group of MOM1 peaks at active chromatin near genes that colocalized with MORC6. These findings demonstrate a multifaceted role of MOM1 in genome regulation.

2023-06-10 | PXD039991 | Pride

Saccharomyces cerevisiae

Project description:The E3 SUMO ligase Mms21 controls ribosome biogenesis

| PRJNA286877 | ENA

The E3 SUMO ligase Mms21 controls ribosome biogenesis

Project description:The budding yeast E3 SUMO ligase Mms21, a component of the Smc5-6 complex, regulates sister chromatid cohesion, DNA replication, and DNA repair. We identify a role for Mms21 in ribosome biogenesis. The mms21RINGD mutant exhibits reduced rRNA production, nuclear accumulation of 60S and 40S ribosomal proteins, and elevated Gcn4 translation. Genes involved in ribosome biogenesis and translation are down-regulated in the mms21RINGD mutant. Examining gene expression profile of mms21RINGD mutant compared to wild-type by RNA Seq using Ilumina sequencing

2015-06-13 | E-GEOD-69826 | biostudies-arrayexpress

The SUMO ligase Su(var)2-10 induces co-transcriptional repression of piRNA targets

Project description:In Drosophila, Piwi-induced transcriptional repression is associated with the establishment of repressive chromatin marks by the histone methyltrasferase SetDB1, however how the Piwi/piRNA complex recruits this effector to chromatin targets is poorly understood. We identified a new player in piRNA-guided transcriptional silencing encoded by the Su(var)2-10 gene. Su(var)2-10 is required for transcriptional silencing and deposition of repressive chromatin marks on transposons and it physically associates with the Piwi/piRNA target recognition complex. Recruitment of Su(var)2-10 to a target locus in a piRNA-independent fashion induces transcriptional repression and deposition of the H3K9 trimethyl mark by the histone methyltransferase dSetDB1/Eggless. Su(var)2-10 belongs to a conserved family of proteins that function as SUMO E3 ligases and we found that the SUMO pathway is essential for the repressive function of Su(var)2-10 and for transcriptional repression of transposons. Together, our data identifies Su(var)2-10 as an essential component of the piRNA-induced transcriptional silencing pathway that links the target recognition complex to the silencing effector and reveals a novel role of SUMO modification in the piRNA-induced repression.

2019-12-18 | GSE115277 | GEO

TRIM28-dependent SUMOylation protects the adult ovary from the male pathway (ChIP-Seq 2)

Project description:We study the role of the protein Trim28 in the maintenance of sexual identity of the adult ovary. With the help of conditional knock out (cKO) of Trim28 using the Nr5a1:Cre, we observed that deletion of the Trim28 gene in granulosa cells of the adult ovary induces their transdifferentiation into Sertoli cells, the supporting cell lineage of the testicular seminiferous tubules. FOXL2 expression has disappeared and follicles were completely remodeled into tubular structures with cells that expressed the Sertoli cell markers SOX8, SOX9 and DMRT1. Histological analysis confirmed the progressive reorganization of ovarian follicles into tubular structures and the and the transdifferentiation of granulosa cells by cells with a Sertoli cell morphology. TRIM28 acts as a SUMO-E3 ligase by interacting with the SUMO-E2 conjugating enzyme UBC9 (encoded by the Ube2i gene) via the Plant homeodomain (PHD), and can self-SUMOylate. To study in vivo the role of TRIM28-dependent SUMOylation, we generated a point mutation in exon 13 of mouse Trim28 within the PHD domain of the TRIM28 protein (C651F) that abrogates its SUMO-E3 ligase activity. We generated Trim28Phd/cKO mice (termed PHD mutant). Like in cKO ovaries, FOXL2 expression was undetectable, whereas we observed expression of the Sertoli cell markers SOX9, SOX8 and DMRT1 within structures organized in pseudo-tubules in PHD ovaries. Our results indicate that maintenance of the female pathway in the adult ovary depends on the E3-SUMO ligase activity of TRIM28.

2022-05-24 | GSE166384 | GEO

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