Sexual dimorphism in the meiotic requirement for PRDM9: a mammalian evolutionary safeguard
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA602882 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR12091146_1.fastq.gz | Fastqsanger.gz | |||
| SRR12091146_2.fastq.gz | Fastqsanger.gz | |||
| SRR12091147_1.fastq.gz | Fastqsanger.gz | |||
| SRR12091147_2.fastq.gz | Fastqsanger.gz | |||
| SRR12091148_1.fastq.gz | Fastqsanger.gz |
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Project description:The locations of mammalian recombination hotspots are determined by PRDM9, a zinc finger histone methyltransferase that locally trimethylates histone H3 at residues K4 and K36. Here we report Prdm9-EP, a glu365pro mutation that severely reduces catalytic activity in vivo. This mutation causes sterility with complete meiotic arrest in homozygous males, while homozygous females are able to produce live offspring in natural matings. These H3K4me3 ChIP-seq data from Prdm9-EP homozygous spermatocytes show the extent to which H3K4 methyltransferase activity is compromised by this mutation, while the DMC1 ChIP-seq data show its effect on meiotic double-strand breaks in spermatocytes. For comparison, we mapped previously reported H3K4me3 ChIP-seq data from wild-type C57BL/6J spermatocytes (GSE52628) to mm10, merging the two biological replicates (SRX381465 and SRX381466) before mapping, and proceeding with processing. We did the same with published DMC1 ChIP-seq data, merging three previously reported DMC1 ChIP-seq biological replicates, isolated from wild-type C57BL/6N males (GSE112110; SRX3825301, SRX3825302, and SRX3825303). Processed data files are presented here.
2020-10-23 | GSE144144 | GEO
Project description:In many mammals, genomic sites for recombination are determined by the histone methyltransferase PRMD9. Some mouse strains lacking PRDM9 are infertile, but instances of fertility or semifertility in the absence of PRDM9 have been reported in mice, canines, and a human female. Such findings raise the question of how the loss of PRDM9 is circumvented to maintain fertility. We show that genetic background and sex-specific modifiers can obviate the requirement for PRDM9 in mice. Specifically, the meiotic DNA damage checkpoint protein CHK2 acts as a modifier allowing female-specific fertility in the absence of PRDM9. We also report that, in the absence of PRDM9, a PRDM9-independent recombination system is compatible with female meiosis and fertility, suggesting sex-specific regulation of meiotic recombination, a finding with implications for speciation.
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Project description:The programmed formation of hundreds DNA double strand breaks (DSBs) is essential for proper meiosis and fertility. In mice and humans, the location of these breaks is determined by the meiosis-specific protein PRDM9, through the DNA binding specificity of its zinc finger domain. PRDM9 also has methyltransferase activity. Here, we show that this activity is required for H3K4me3 and H3K36me3 deposition and for DSB formation at PRDM9 binding sites. By analyzing mice that express two PRDM9 variants with distinct DNA binding specificities, we reveal severalthe basic principles of PRDM9-dependent DSB site determination, in which an excess of sites are designated through PRDM9 binding and subsequent histone methylation, from which a subset are selected for DSB formation.
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Project description:PRDM9 specifies the sites of meiotic DNA double strand break that initiate meiotic recombination in mice and humans. PRDM9 is known to bind to specific DNA sequences with its DNA binding domain, to induce H3K4me3 and H3K36me3 to adjacent nucleosomes through its methyltransferase activity, and to recruit or activate the meiotic DSB machinery. To understand how PRDM9 executes these various steps, we set up to identify its partners. This was performed by a proteomic approach where protein extracts from mouse testis were immunoprecipitated with anti-PRDM9 antibody for mass spectrometry analysis.
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Project description:Mammalian genetic recombination is concentrated at hotspots, specialized 1-2 Kb sites separated by long stretches of DNA lacking recombination. Mammalian hotspot locations depend on PRDM9, a zinc finger protein that binds at hotspots and uses its SET domain to locally trimethylate histone H3K4. Here we find that PRDM9 also locally trimethylates H3K36 at hotspots. Using ChIP-seq and immunoprecipitation data for H3K36me3 in murine spermatocytes, we show that H3K4me3 and H3K36me3 coincide only at hotspots in germ cells, and that this H3K4me3/H3K36me3-double-positive signature is almost entirely dependent on PRDM9. We performed ChIP-seq with an antibody against H3K36me3, using chromatin extracted from murine spermatocytes, and compared it to previously generated ChIP-seq data for H3K4me3 in the same cell type. ---------------------------------- This dataset represents the H3K36 component only
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Project description:Sexual dimorphism in osteogenic differentiation
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Project description:The aim of the present study was to carry out a high-throughput screening of proteins using proteomics tool to identify and quantify proteins and related biochemical pathways that orchestrate the sexual dimorphism in the liver of zebrafish. In addition, we tried to discover potential connections between the sex-biased levels of proteins in liver and hepatic diseases and regeneration via review of related literature.
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Project description:Managing aortic valve stenosis (AVS) is challenging because of the lack of pharmacotherapies to halt/revert stenosis, deeming aortic valve replacement (AVR) the only effective treatment. AVS management is further confronted with staggering sexual dimorphism; women display more extensive fibrosis, while men present remarkably higher valve calcification. To accelerate the development of effective and sex-personalised pharmacotherapies, deeper molecular insights are needed. Hence, we aimed to characterise AVS sexual dimorphism using proteomics. Aortic valves were obtained from surgical AVR. Disease severity was assessed by echocardiography. Fifty valves (50% women) were homogenised, and the proteins were quantified by LC-MS/MS. The relevance of differentially expressed proteins (DEPs) in sexual dimorphism was appraised using protein-protein interaction (PPI) and functional enrichment analyses (FEA). DEPs were validated using immunohistochemistry, qRT-PCR and ELISA, with the aid of 30 additional independent valves.
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