Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast Schizosaccharomyces pombe.

Schizosaccharomyces pombe Elevated temperature Meiosis Pat1 protein kinase Phosphoproteome Proteome Quantitative mass spectrometry

Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
04 Oct 2024
Historique:
received: 15 07 2024
accepted: 26 09 2024
medline: 5 10 2024
pubmed: 5 10 2024
entrez: 4 10 2024
Statut: epublish

Résumé

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 divisions. We compared the proteomes and phosphoproteomes of exponentially growing 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 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 divisions in this yeast.

Identifiants

pubmed: 39367033
doi: 10.1038/s41598-024-74523-0
pii: 10.1038/s41598-024-74523-0
doi:

Substances chimiques

Schizosaccharomyces pombe Proteins 0
Phosphoproteins 0
Proteome 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

23105

Subventions

Organisme : Operational Program Integrated Infrastructure
ID : 313011W428
Organisme : Operational Program Integrated Infrastructure
ID : 313011W428
Organisme : Austrian Science Fund
ID : P30516
Organisme : Slovak Research and Development Agency
ID : APVV-20-0141
Organisme : Slovak Grant Agency VEGA
ID : 2/0021/22

Informations de copyright

© 2024. The Author(s).

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Auteurs

Barbara Sivakova (B)

Department of Glycobiology, Institute of Chemistry, Slovak Academy of Sciences, Dubravska cesta 9, Bratislava, 845 38, Slovakia.
Department of Medical and Clinical Biophysics, Faculty of Medicine, Pavol Jozef Šafárik University in Košice, Trieda SNP 1, Košice, 040 11, Slovakia.

Anja Wagner (A)

Division of Pediatric Nephrology and Gastroenterology, Department of Pediatrics and Adolescent Medicine, Comprehensive Center for Pediatrics, Medical University Vienna, Währinger Gürtel 18-20, Vienna, 1090, Austria.
Christian Doppler Laboratory for Molecular Stress Research in Peritoneal Dialysis, Department of Pediatrics and Adolescent Medicine, Medical University Vienna, Währinger Gürtel 18-20, Vienna, 1090, Austria.

Miroslava Kretova (M)

Department of Genetics, Cancer Research Institute, Biomedical Research Center, Slovak Academy of Sciences, Dubravska cesta 9, Bratislava, 845 05, Slovakia.

Jana Jakubikova (J)

Department of Tumor Immunology, Cancer Research Institute, Biomedical Research Center, Slovak Academy of Sciences, Dubravska cesta 9, Bratislava, 845 05, Slovakia.

Juraj Gregan (J)

Department of Chromosome Biology, University of Vienna, Vienna Biocenter (VBC), Dr. Bohr-Gasse 9, Vienna, 1030, Austria.
Department of Applied Genetics and Cell Biology, Institute of Microbial Genetics, University of Natural Resources and Life Sciences, Vienna (BOKU), Konrad Lorenz Strasse 24, Tulln an der Donau, 3430, Austria.

Klaus Kratochwill (K)

Division of Pediatric Nephrology and Gastroenterology, Department of Pediatrics and Adolescent Medicine, Comprehensive Center for Pediatrics, Medical University Vienna, Währinger Gürtel 18-20, Vienna, 1090, Austria. klaus.kratochwill@meduniwien.ac.at.
Christian Doppler Laboratory for Molecular Stress Research in Peritoneal Dialysis, Department of Pediatrics and Adolescent Medicine, Medical University Vienna, Währinger Gürtel 18-20, Vienna, 1090, Austria. klaus.kratochwill@meduniwien.ac.at.

Peter Barath (P)

Department of Glycobiology, Institute of Chemistry, Slovak Academy of Sciences, Dubravska cesta 9, Bratislava, 845 38, Slovakia. peter.barath@savba.sk.
Medirex Group Academy, Novozamocka 67, Nitra, 949 05, Slovakia. peter.barath@savba.sk.

Lubos Cipak (L)

Department of Genetics, Cancer Research Institute, Biomedical Research Center, Slovak Academy of Sciences, Dubravska cesta 9, Bratislava, 845 05, Slovakia. lubos.cipak@savba.sk.

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