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LOTR-1 interacts with ZNFX-1 to balance epigenetic signals in the C. elegans germline

ABSTRACT: LOTR-1 interacts with ZNFX-1 to balance epigenetic signals in the C. elegans germline

PROVIDER: PRJNA793223 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14238417.fastq.gz	Fastqsanger.gz
	SRR14238418.fastq.gz	Fastqsanger.gz
	SRR14238419.fastq.gz	Fastqsanger.gz
	SRR14238420.fastq.gz	Fastqsanger.gz
	SRR14238421.fastq.gz	Fastqsanger.gz

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LOTR-1 interacts with ZNFX-1 to balance epigenetic signals in the C. elegans germline

Project description:Proteins containing LOTUS and Tudor domains have critical roles in the germline, including in small RNA biology. LOTR-1 is the only protein expressed in the germline of C. elegans which has LOTUS and Tudor domains. Here, to understand the influence of LOTR-1 in small RNA biology, we sequenced small RNAs of wild-type and lotr-1 mutant animals. This SuperSeries is composed of the SubSeries listed below.

2022-05-26 | GSE192794 | GEO

The TDRD5/7-like protein, LOTR-1, functions within Z granules to balance epigenetic signals in the Caenorhabditis elegans germline

Project description:LOTUS and Tudor domain containing proteins have critical roles in the germline. Proteins that contain these domains, such as Tejas/Tapas in Drosophila, help localize Vasa to the germ granules and facilitate piRNA transposon mediated silencing. The homologous proteins in mammals, TDRD5 and TDRD7, are required during spermiogenesis. Until now, LOTUS + Tudor domain proteins in C. elegans have remained elusive. Here we describe LOTR-1 (D1081.7), which derives its name from its LOTUS and Tudor domains. Interestingly, LOTR-1 docks next to P granules to colocalize with the Z-granule component ZNFX-1. LOTR-1’s Z-granule association requires its Tudor domain, but both LOTUS and Tudor deletions affect brood size when coupled with a knockdown of the Vasa homolog glh-1. LOTR-1 IP-mass spectrometry confirmed a Tudor-dependent association with Z-granule proteins ZNFX-1 and WAGO-1, but also with germ-granule proteins DEPS-1, the piRNA Argonaute PRG-1, and other WAGO-class Argonautes. Like znfx-1, lotr-1 mutants redistribute the coverage of 22G-RNAs toward the 5’ end of mutator targets and impact transgenerational epigenetic inheritance. Unlike znfx-1, the 5’ shift in 22G-RNA coverage does not extend to CSR-1 targets. Combined, these results suggest that LOTR-1 facilitates interactions between PRG-1/WAGO-class Argonautes, ZNFX-1 and target 3’UTRs to balance 22G-RNA distribution across mutator targets.

2022-05-28 | PXD025186 | Pride

ZNFX-1 Functions Within Perinuclear Nuage to Balance Epigenetic Signals

Project description:Animal cells have a remarkable capacity to adopt durable and heritable gene expression programs or epigenetic states that define the physical properties and diversity of somatic cell types. The maintenance of epigenetic programs depends on poorly understood pathways that prevent gain or loss of inherited signals. In the germline, epigenetic factors are enriched in liquid-like perinuclear condensates called nuage. Here we identify the deeply conserved helicase-domain protein, ZNFX-1, as an epigenetic regulator and component of nuage that interacts with Argonaute systems to balance epigenetic inheritance. Our findings suggest that ZNFX-1 promotes the 3’ recruitment of machinery that propagates the small RNA epigenetic signal and thus counteracts a tendency for Argonaute-targeting to shift 5’ along the mRNA. These functional insights support the idea that recently identified subdomains of nuage, including ZNFX-1 granules or “Z-granules,” may define spatial and temporal zones of molecular activity during epigenetic regulation.

2018-05-18 | GSE112708 | GEO

RNA-binding protein complex AMG-1/SLRP-1 mediates germline development and spermatogenesis by maintaining mitochondrial homeostasis in Caenorhabditis elegans [LACE-seq]

Project description:The mechanisms of RNA-binding proteins (RBPs)-mediated post-transcriptional regulation of pre-existing mRNAs, which is essential for spermatogenesis, remains poorly understood. Here, we identify a germline-specific mitochondrial RBP AMG-1, a homolog of mammalian LRPPRC, required for spermatogenesis in C. elegans. amg-1 mutation hinders germline development without affecting somatic development and leads to the aberrant mitochondrial morphology and structure associated with mitochondrial dysfunctions specifically in germline. We demonstrate that AMG-1 is most frequently bound to mtDNA-encoded 12S and 16S ribosomal RNA, the essential components of mitochondrial ribosome, and that 12S rRNA expression mediated by AMG-1 is crucial for germline mitochondrial protein homeostasis. Besides, mitochondrial dysfunction by AMG-1 mutation triggers sperm apoptosis in C. elegans. Furthermore, SLRP-1, the homolog of mammalian SLIRP in C. elegans, interacts with AMG-1 genetically to regulate germline development and reproductive success in C. elegans. Taken together, these findings reveal the novel function of mtRBP in specifically regulating germline development.

2023-01-16 | GSE222138 | GEO

RNA-binding protein complex AMG-1/SLRP-1 mediates germline development and spermatogenesis by maintaining mitochondrial homeostasis in Caenorhabditis elegans [RNA-seq]

2023-01-16 | GSE222137 | GEO

Regulation of germline gene expression in C. elegans germline stem cells.

Project description:ChIP-Seq study to understand regulation of germline stem cell gene expression by immunoprecipitation of stem-cell factor Notch and associated transcriptional cofactor LAG-1 in C. elegans.

2019-07-01 | GSE70426 | GEO

C. elegans germline-ablated (Z2-, Z3-) animals versus intact animals, N2 strain

Project description:Transcriptional profiling of C. elegans germline-ablated worms versus unablated intact animals, N2 strain One-condition experiment. C. elegans germline-ablated versus intact N2. 3 biological replicates, including 1 dye-swap.

2013-03-01 | E-GEOD-44702 | biostudies-arrayexpress

ZNFX-1 Functions Within Perinuclear Nuage to Balance Epigenetic Signals

Project description:ZNFX-1 Functions Within Perinuclear Nuage to Balance Epigenetic Signals

| PRJNA448765 | ENA

The Caenorhabditis elegans TDRD5/7-like protein, LOTR-1, interacts with the helicase ZNFX-1 to balance epigenetic signals in the germline.

Project description:LOTUS and Tudor domain containing proteins have critical roles in the germline. Proteins that contain these domains, such as Tejas/Tapas in Drosophila, help localize the Vasa helicase to the germ granules and facilitate piRNA-mediated transposon silencing. The homologous proteins in mammals, TDRD5 and TDRD7, are required during spermiogenesis. Until now, proteins containing both LOTUS and Tudor domains in Caenorhabditis elegans have remained elusive. Here we describe LOTR-1 (D1081.7), which derives its name from its LOTUS and Tudor domains. Interestingly, LOTR-1 docks next to P granules to colocalize with the broadly conserved Z-granule helicase, ZNFX-1. The Tudor domain of LOTR-1 is required for its Z-granule retention. Like znfx-1 mutants, lotr-1 mutants lose small RNAs from the 3' ends of WAGO and mutator targets, reminiscent of the loss of piRNAs from the 3' ends of piRNA precursor transcripts in mouse Tdrd5 mutants. Our work shows that LOTR-1 acts with ZNFX-1 to bring small RNA amplifying mechanisms towards the 3' ends of its RNA templates.

| S-EPMC9200344 | biostudies-literature

C. elegans establishes germline versus soma by balancing inherited histone methylation [ChIP-seq]

Project description:In C. elegans, the H3K4me2 demethylase, SPR-5, and the H3K9 methyltransferase, MET-2, are maternally deposited into the oocyte where they reprogram histone methylation to prevent somatic expression of germline genes. Here, we show that the progeny of spr-5; met-2 mutants display a severe developmental delay that is associated with the ectopic expression of germline genes targeted by the H3K36me2/3 methyltransferase, MES-4. Maternally deposited MES-4 maintains H3K36me2/3 at a subset of germline genes (hereafter referred to as MES-4 germline genes) in a transcription-independent manner, and this is required for germline proliferation in the subsequent generation. By performing ChIP-seq on L1 progeny from spr-5; met-2 mutants, we find that MES-4 germline genes ectopically accumulate H3K36me3 in somatic tissues. Additionally, knocking down MES-4 suppresses the ectopic expression of MES-4 germline genes and rescues the developmental delay. These data suggest a model where SPR-5, MET-2 and MES-4 carefully balance the inheritance of histone methylation from the parental germline to ensure the proper specification of germline versus soma in the progeny. Without SPR-5; MET-2 maternal reprogramming, somatic cells struggle to specify their proper cell fate amongst the background noise of inappropriate germline gene transcription, leading to a severe developmental delay.

2020-01-17 | GSE143838 | GEO

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