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Updated: Aug 20, 2026

Examination of Mitotic and Meiotic Fission Yeast Nuclear Dynamics by Fluorescence Live-cell Microscopy
Published on: June 24, 2019
The budding yeast mei5 and sae3 proteins act together with dmc1 during meiotic recombination
Hideo Tsubouchi1, G Shirleen Roeder
1Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520-8103, USA.
Abstract:
Here we provide evidence that the Mei5 and Sae3 proteins of budding yeast act together with Dmc1, a meiosis-specific, RecA-like recombinase. The mei5 and sae3 mutations reduce sporulation, spore viability, and crossing over to the same extent as dmc1. In all three mutants, these defects are largely suppressed by overproduction of Rad51. In addition, mei5 and sae3, like dmc1, suppress the cell-cycle arrest phenotype of the hop2 mutant. The Mei5, Sae3, and Dmc1 proteins colocalize to foci on meiotic chromosomes, and their localization is mutually dependent. The localization of Rad51 to chromosomes is not affected in either mei5 or sae3. Taken together, these observations suggest that the Mei5 and Sae3 proteins are accessory factors specific to Dmc1. We speculate that Mei5 and Sae3 are necessary for efficient formation of Dmc1-containing nucleoprotein filaments in vivo.
Insights
Mei5 and Sae3 proteins are essential accessory factors for Dmc1 function during yeast meiosis. These proteins, along with Dmc1, are crucial for DNA repair, recombination, and successful spore formation.
Area of Science:
- Cell Biology
- Genetics
- Molecular Biology
Background:
- Meiosis is a fundamental process for sexual reproduction, involving DNA replication, homologous recombination, and chromosome segregation.
- RecA-like recombinases, such as Dmc1, play critical roles in mediating homologous recombination during meiosis.
- Accessory proteins are often required to facilitate the function of key recombination enzymes.
Purpose of the Study:
- To investigate the functional relationship between Mei5, Sae3, and Dmc1 proteins in budding yeast.
- To determine the role of Mei5 and Sae3 in Dmc1-mediated DNA repair and recombination during meiosis.
- To elucidate the mechanism by which Mei5 and Sae3 influence Dmc1 activity.
Main Methods:
- Genetic analysis of mei5, sae3, and dmc1 mutants in budding yeast.
- Assessment of sporulation efficiency, spore viability, and crossing over rates.
- Analysis of cell-cycle progression and suppression of mutant phenotypes.
- Immunolocalization studies to determine protein co-localization and dependency on meiotic chromosomes.
Main Results:
- Mutations in mei5 and sae3 phenocopy dmc1 mutations, impairing sporulation, spore viability, and crossing over.
- Overproduction of Rad51 suppresses the meiotic defects observed in mei5, sae3, and dmc1 mutants.
- Mei5, Sae3, and Dmc1 proteins exhibit mutually dependent co-localization on meiotic chromosomes.
- Rad51 localization is unaffected in mei5 and sae3 mutants, indicating a specific role for Mei5/Sae3 with Dmc1.
Conclusions:
- Mei5 and Sae3 function as specific accessory factors for the Dmc1 recombinase during budding yeast meiosis.
- These proteins are likely essential for the efficient assembly of Dmc1-containing nucleoprotein filaments on meiotic chromosomes.
- The findings provide insights into the regulation of homologous recombination and genome stability during meiosis.
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