ArticleCurrent genetics2010
Functional interactions among members of the meiotic initiation complex in fission yeast.
Article in Current genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Dimerization of thebioRxiv : the preprint server for biology · 2026Article
- Mitochondrial Translation Inhibition Triggers an Rst2-Controlled Transcriptional Reprogramming of Carbon Metabolism in Stationary-Phase Cells of Fission Yeast.Biomolecules · 2025Article
- Divergence and conservation of the meiotic recombination machinery.Nature reviews. Genetics · 2024Review
- Evolutionary conservation of the structure and function of meiotic Rec114-Mei4 and Mer2 complexes.Genes & development · 2023Article
- Computed structures of core eukaryotic protein complexes.Science (New York, N.Y.) · 2021Article
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- Article
- Mechanism and Control of Meiotic DNA Double-Strand Break Formation inFrontiers in cell and developmental biology · 2021Review
- Conserved HORMA domain-containing protein Hop1 stabilizes interaction between proteins of meiotic DNA break hotspots and chromosome axis.Nucleic acids research · 2019Article
- Advances Towards How Meiotic Recombination Is Initiated: A Comparative View and Perspectives for Plant Meiosis Research.International journal of molecular sciences · 2019Review
- Mouse REC114 is essential for meiotic DNA double-strand break formation and forms a complex with MEI4.Life science alliance · 2018Article
- The histone variant H2A.Z promotes initiation of meiotic recombination in fission yeast.Nucleic acids research · 2018Article
- Control of meiotic double-strand-break formation by ATM: local and global views.Cell cycle (Georgetown, Tex.) · 2018Review
- P31comet, a member of the synaptonemal complex, participates in meiotic DSB formation in rice.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mechanism and regulation of meiotic recombination initiation.Cold Spring Harbor perspectives in biology · 2014Review
- Functional interactions of Rec24, the fission yeast ortholog of mouse Mei4, with the meiotic recombination-initiation complex.Journal of cell science · 2011Article
- Meiotic recombination protein Rec12: functional conservation, crossover homeostasis and early crossover/non-crossover decision.Nucleic acids research · 2011Article
- Chiasmata promote monopolar attachment of sister chromatids and their co-segregation toward the proper pole during meiosis I.PLoS genetics · 2011Article
- Evolutionary conservation of meiotic DSB proteins: more than just Spo11.Genes & development · 2010Article
- Functional conservation of Mei4 for meiotic DNA double-strand break formation from yeasts to mice.Genes & development · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
DNA double-strand breaks (DSBs) initiate meiotic recombination in Schizosaccharomyces pombe and in other organisms. The Rec12 protein catalyzes the formation of these DSBs in concert with a multitude of accessory proteins the role of which in this process remains to be discovered. In an all-to-all yeast two-hybrid matrix analysis, we discovered new interactions among putative members of the meiotic recombination initiation complex. We found that Rec7, an axial-element associated protein with homologies to Saccharomyces cerevisiae Rec114, is interacting with Rec24. Rec7 and Rec24 also co-immunoprecipitate in S. pombe during meiosis. An amino acid change in a conserved, C-terminal phenylalanine in Rec7, F325A interrupts the interaction with Rec24. Moreover, rec7F325A shows a recombination deficiency comparable to rec7Delta. Another interaction was detected between Rec12 and Rec14, the orthologs of which in S. cerevisiae Spo11 and Ski8 interact accordingly. Amino acid changes Rec12Q308A and Rec12R309A disrupt the interaction with Rec14, like the according amino acid changes Spo11Q376A and Spo11RE377AA loose the interaction with Ski8. Both amino acid changes in Rec12 reveal a recombination deficient rec12 (-) phenotype. We propose that both Rec7-Rec24 and Rec12-Rec14 form subcomplexes of the meiotic recombination initiation complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.