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Mouse testis Co-IP LC-MSMS for studying HSF5 function

ABSTRACT: The pachynema progression, a crucial meiotic process, contributes to the completion of prophase I. Nevertheless, the regulation of this significant meiotic process remains poorly understood. In this study, we identified a novel testis-specific protein HSF5, which regulates pachynema progression during male meiosis in a chromatin-binding manner. Deficiency of HSF5 results in meiotic arrest and male infertility, characterized as unconventionally accumulated pachynema halting at the mid-to-late stage, with extensive spermatocyte apoptosis. Our scRNA-seq data confirmed consistent expressional alterations of certain driver genes(Sycp1, Msh4, Meiob, etc.) crucial for pachynema progression in Hsf5-/- individuals. Ulteriorly, HSF5 was revealed to primarily bind to promoter regions of such key divers by CUT&Tag analysis. Also, our results demonstrated that HSF5 biologically interacted with the chromatin-remodeling SWI/SNF complex, and it could function as a transcriptional factor for pachynema progression during meiosis. Therefore, our study underscored the importance of the chromatin-associated HSF5 for the differentiation of spermatocytes, improving the protein regulatory network of the pachynema progression.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Testis, Male Germ Cell

DISEASE(S): Male Infertility

SUBMITTER: ziqi Yu

LAB HEAD: Fei Sun

PROVIDER: PXD053613 | Pride | 2024-08-23

REPOSITORIES: Pride

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			Action	DRS
	Hsf5_knockout_rep1.raw	Raw
	Hsf5_knockout_rep2.raw	Raw
	Hsf5_knockout_rep3.raw	Raw
	Mass_spectrometry_peptides.xlsx	Xlsx
	Mass_spectrometry_proteins.xlsx	Xlsx

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Project description:In eukaryotes, chromosomal DNA is equally distributed to daughter cells during mitosis, whereas the number of chromosomes is halved during meiosis. Despite considerable progress in understanding the molecular mechanisms that regulate mitosis, there is currently a lack of complete understanding of the molecular mechanisms regulating meiosis. Here, we took advantage of the fission yeast Schizosaccharomyces pombe, for which highly synchronous meiosis can be induced, and performed quantitative proteomics and phosphoproteomics analyses to track changes in protein expression and phosphorylation during meiotic cell divisions. We compared the proteomes and phosphoproteomes of mitotic cells with cells harvested around meiosis I, or meiosis II in strains bearing either the temperature-sensitive pat1-114 allele or conditional ATP analog-sensitive pat1-as2 allele of the Pat1 kinase. Comparing pat1-114 with pat1-as2 also allowed us to investigate the impact of elevated temperature (25°C versus 34°C) on meiosis, an issue that sexually reproducing organisms face due to climate change. Using TMTpro 18plex labeling and phosphopeptide enrichment strategies, we performed quantification of a total of 4673 proteins and 7172 phosphosites in S. pombe. We found that the protein level of 2680 proteins and the rate of phosphorylation of 4005 phosphosites significantly changed during progression of S. pombe cells through meiosis. The proteins exhibiting changes in expression and phosphorylation during meiotic cell divisions were represented mainly by those involved in the meiotic cell cycle, meiotic recombination, meiotic nuclear division, meiosis I, centromere clustering, microtubule cytoskeleton organization, ascospore formation, organonitrogen compound biosynthetic process, carboxylic acid metabolic process, gene expression, and ncRNA processing, among others. In summary, our findings provide global overview of changes in the levels and phosphorylation of proteins during progression of S. pombe cells through meiosis at normal and elevated temperatures, laying the groundwork for further elucidation of the functions and importance of specific proteins and their phosphorylation in regulating meiotic cell divisions in this yeast.

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Mouse testis Co-IP LC-MSMS for studying HSF5 function

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