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Published on: July 18, 2025
Functional interactions of meiotic recombination factors Rdh54 and Dmc1
Peter Chi1, Youngho Kwon, Dana N Moses
1Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520, USA.
Abstract:
Genetic studies in budding and fission yeasts have provided evidence that Rdh54, a Swi2/Snf2-like factor, synergizes with the Dmc1 recombinase to mediate inter-homologue recombination during meiosis. Rdh54 associates with Dmc1 in the yeast two-hybrid assay, but whether the Rdh54-Dmc1 interaction is direct and the manner in which these two recombination factors may functionally co-operate to accomplish their biological task have not yet been defined. Here, using purified Schizosaccharomyces pombe proteins, we demonstrate complex formation between Rdh54 and Dmc1 and enhancement of the recombinase activity of Dmc1 by Rdh54. Consistent with published cytological and chromatin immunoprecipitation data that implicate Rdh54 in preventing the non-specific association of Dmc1 with chromatin, we show here that Rdh54 mediates the efficient removal of Dmc1 from dsDNA. These functional attributes of Rdh54 are reliant on its ATPase function. The results presented herein provide valuable information concerning the Rdh54-Dmc1 protein pair that is germane for understanding their role in meiotic recombination. The biochemical systems established in this study should be useful for the continuing dissection of the action mechanism of Rdh54 and Dmc1.
Insights
Rdh54 protein directly interacts with Dmc1 recombinase, enhancing its activity and promoting efficient removal from DNA. This interaction is crucial for meiotic recombination, as demonstrated in fission yeast studies.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Rdh54, a Swi2/Snf2-like factor, is known to synergize with Dmc1 recombinase in yeast meiosis.
- Previous studies suggested an association between Rdh54 and Dmc1, but the direct interaction and functional cooperation remained undefined.
Purpose of the Study:
- To investigate the direct interaction between purified Rdh54 and Dmc1 proteins from Schizosaccharomyces pombe.
- To elucidate the functional cooperation between Rdh54 and Dmc1 in meiotic recombination.
Main Methods:
- Purification of Schizosaccharomyces pombe Rdh54 and Dmc1 proteins.
- Biochemical assays to demonstrate complex formation and Dmc1 recombinase activity enhancement.
- Assays to show Rdh54-mediated removal of Dmc1 from double-stranded DNA (dsDNA).
Main Results:
- Demonstrated direct complex formation between purified Rdh54 and Dmc1.
- Showed that Rdh54 enhances the recombinase activity of Dmc1.
- Confirmed that Rdh54 mediates the efficient removal of Dmc1 from dsDNA, dependent on its ATPase function.
Conclusions:
- Rdh54 directly interacts with Dmc1, enhancing its recombinase activity and regulating its association with chromatin during meiosis.
- These findings provide critical insights into the functional mechanism of the Rdh54-Dmc1 protein pair in meiotic recombination.
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