ArticleNucleic acids research2021
The Pif1 helicase is actively inhibited during meiotic recombination which restrains gene conversion tract length.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Mismatch repair MLH complexes make distinct contributions to post-replicative mismatch repair versus trinucleotide repeat expansions.bioRxiv : the preprint server for biology · 2026Article
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- Mechanism of trinucleotide repeat expansion by MutSβ-MutLγ and contraction by FAN1.Nature communications · 2025Article
- Rad51, Rad54, and ZMM proteins antagonize the mismatch repair system to promote fertility of budding yeast intraspecies hybrid zygotes.Nucleic acids research · 2025Article
- Recombination-coupled DNA synthesis facilitates post-invasion steps in meiotic crossover and noncrossover formations.Nucleic acids research · 2025Article
- Proximity labeling reveals new functional relationships between meiotic recombination proteins in S. cerevisiae.PLoS genetics · 2024Article
- Article
- HLTF resolves G4s and promotes G4-induced replication fork slowing to maintain genome stability.Molecular cell · 2024Article
- HLTF disrupts Cas9-DNA post-cleavage complexes to allow DNA break processing.Nature communications · 2024Article
- An acidic loop in the FHA domain of the yeast meiosis-specific kinase Mek1 interacts with a specific motif in a subset of Mek1 substrates.bioRxiv : the preprint server for biology · 2024Article
- The molecular machinery of meiotic recombination.Biochemical Society transactions · 2024Review
- The Dmc1 recombinase physically interacts with and promotes the meiotic crossover functions of the Mlh1-Mlh3 endonuclease.bioRxiv : the preprint server for biology · 2023Article
- Dna2 removes toxic ssDNA-RPA filaments generated from meiotic recombination-associated DNA synthesis.Nucleic acids research · 2023Article
- Biochemical characterisation of Mer3 helicase interactions and the protection of meiotic recombination intermediates.Nucleic acids research · 2023Article
- Lessons from the meiotic recombination landscape of the ZMM deficient budding yeast Lachancea waltii.PLoS genetics · 2023Article
- Rad51-mediated interhomolog recombination during budding yeast meiosis is promoted by the meiotic recombination checkpoint and the conserved Pif1 helicase.PLoS genetics · 2022Article
- Efficient gene editing through an intronic selection marker in cells.Cellular and molecular life sciences : CMLS · 2022Article
- Repeated strand invasion and extensive branch migration are hallmarks of meiotic recombination.Molecular cell · 2021Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Meiotic recombination ensures proper chromosome segregation to form viable gametes and results in gene conversions events between homologs. Conversion tracts are shorter in meiosis than in mitotically dividing cells. This results at least in part from the binding of a complex, containing the Mer3 helicase and the MutLβ heterodimer, to meiotic recombination intermediates. The molecular actors inhibited by this complex are elusive. The Pif1 DNA helicase is known to stimulate DNA polymerase delta (Pol δ) -mediated DNA synthesis from D-loops, allowing long synthesis required for break-induced replication. We show that Pif1 is also recruited genome wide to meiotic DNA double-strand break (DSB) sites. We further show that Pif1, through its interaction with PCNA, is required for the long gene conversions observed in the absence of MutLβ recruitment to recombination sites. In vivo, Mer3 interacts with the PCNA clamp loader RFC, and in vitro, Mer3-MutLβ ensemble inhibits Pif1-stimulated D-loop extension by Pol δ and RFC-PCNA. Mechanistically, our results suggest that Mer3-MutLβ may compete with Pif1 for binding to RFC-PCNA. Taken together, our data show that Pif1's activity that promotes meiotic DNA repair synthesis is restrained by the Mer3-MutLβ ensemble which in turn prevents long gene conversion tracts and possibly associated mutagenesis.
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