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Effect of meiosis specific cohesin subunit SMC1 on chromatin architecture in primary murine spermatocytes [RNA-Seq 2]

ABSTRACT: Effect of meiosis specific cohesin subunit SMC1 on chromatin architecture in primary murine spermatocytes [RNA-Seq 2]

PROVIDER: PRJNA961758 | ENA |

REPOSITORIES: ENA

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	SRR24302400.fastq.gz	Fastqsanger.gz

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Effect of meiosis specific cohesin subunit SMC1 on chromatin architecture in primary murine spermatocytes

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Project description:Effect of meiosis specific cohesin subunit SMC1 on chromatin architecture in primary murine spermatocytes [ATAC-Seq]

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Effect of meiosis specific cohesin subunit SMC1 on chromatin architecture in primary murine spermatocytes [RNA-Seq 1]

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Effect of meiosis specific cohesin subunit SMC1 on chromatin architecture in primary murine spermatocytes [ATAC-Seq]

Project description:To investigate the function of meiosis-specific SMC1beta on chromatin architecture near the telomeric end in primary murine spermatocytes we used a SMC1beta knockout mouse model.

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Effect of meiosis specific cohesin subunit SMC1 on chromatin architecture in primary murine spermatocytes [RNA-Seq 2]

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Effect of meiosis specific cohesin subunit SMC1 on chromatin architecture in primary murine spermatocytes [RNA-Seq 1]

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Effect of meiosis specific cohesin subunit SMC1 on chromatin architecture in primary murine spermatocytes

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

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Genome-wide binding of the meiosis specific Rec8 cohesin subunit in metaphase I

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Global phosphoproteomic analysis of mouse spermatocytes identified key kinases regulating meiosis

Project description:Protein phosphorylation, as one of the most important post-translational modifications, exerts crucial roles in regulating meiosis. However, there is a lack of systemic phosphoproteomic and functional analysis of phosphorylation in the meiosis of spermatocytes. To characterize the phosphorylation events in meiosis, we performed large-scale phosphoproteome profiling of purified spermatocytes undergoing meiosis, and identified 20,582 phosphorylation sites in 5,289 phosphoproteins, which were significantly enriched in cell cycle, autophagy, DNA repair, chromosome segregation. Kinase-substrate phosphorylation network analysis followed by in vitro meiosis study showed that CDK9 was a kinase with enriched substrate phosphorylation sites in spermatocytes, and was essential for meiosis progression to metaphase I. We also identified 15 new phosphorylation sites of histones, and 428 epigenetic factors, among which HASPIN was found to be essential for male fertility. Haspin knockout leaded to misalignment of chromosomes, apoptosis of metaphase spermatocytes and decreased number of sperm by deregulation of H3T3ph and Aurora-B kinase-containing chromosomal passenger complex. Our spermatocyte phosphoproteome will be a rich resource for future studies of phosphorylation signaling regulation of meiosis.

2022-03-07 | PXD032089 |

Genome-wide binding of the meiosis I-specific Spo13 in the presence and absence of cohesin

Project description:ChIP-seq profile of Spo13 binding sites arrested in prophase I by deletion of the meiotic transcription factor NDT80. Previous ChIP-ChIP data had indicated that Spo13 binding correlates with cohesin binding sites. Therefore, in addition to wild type cells, we also investigated cells deficient of the meiosis-specific cohesin subunit Rec8 to identify cohesin-dependent binding sites of Spo13.

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