ArticleThe Journal of biological chemistry2011
Mgm101 is a Rad52-related protein required for mitochondrial DNA recombination.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 41 citations in OpenAlex.
- Mechanism of single-strand annealing from native mass spectrometry and cryo-EM structures of RAD52 homolog Mgm101.Nucleic acids research · 2026Article
- Mechanism of single-strand annealing from native mass spectrometry and cryo-EM structures of RAD52 homolog Mgm101.bioRxiv : the preprint server for biology · 2025Article
- Repair of DNA double-strand breaks in plant meiosis: role of eukaryotic RecA recombinases and their modulators.Plant reproduction · 2023Review
- REC drives recombination to repair double-strand breaks in animal mtDNA.The Journal of cell biology · 2023Article
- Oligomeric complexes formed by Redβ single strand annealing protein in its different DNA bound states.Nucleic acids research · 2021Article
- Review
- Mapping and editing animal mitochondrial genomes: can we overcome the challenges?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- Structure and mechanism of the Red recombination system of bacteriophage λ.Progress in biophysics and molecular biology · 2019Review
- Unveiling the mystery of mitochondrial DNA replication in yeasts.Mitochondrion · 2018Review
- Inactivation of RAD52 and HDF1 DNA repair genes leads to premature chronological aging and cellular instability.Journal of biosciences · 2017Article
- The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes.Scientific reports · 2017Article
- Organization and dynamics of yeast mitochondrial nucleoids.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Mgm101: A double-duty Rad52-like protein.Cell cycle (Georgetown, Tex.) · 2016Article
- The structure and DNA-binding properties of Mgm101 from a yeast with a linear mitochondrial genome.Nucleic acids research · 2016Article
- Proteomic and Genomic Analyses of the Rvb1 and Rvb2 Interaction Network upon Deletion of R2TP Complex Components.Molecular & cellular proteomics : MCP · 2016Article
- Genetic instability in budding and fission yeast-sources and mechanisms.FEMS microbiology reviews · 2015Review
- Double-stranded DNA-dependent ATPase Irc3p is directly involved in mitochondrial genome maintenance.Nucleic acids research · 2014Article
- Mitochondrial form and function.Nature · 2014Review
- Mechanism of homologous recombination and implications for aging-related deletions in mitochondrial DNA.Microbiology and molecular biology reviews : MMBR · 2013Review
- Preparation of the Mgm101 recombination protein by MBP-based tagging strategy.Journal of visualized experiments : JoVE · 2013Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Homologous recombination is a conserved molecular process that has primarily evolved for the repair of double-stranded DNA breaks and stalled replication forks. However, the recombination machinery in mitochondria is poorly understood. Here, we show that the yeast mitochondrial nucleoid protein, Mgm101, is related to the Rad52-type recombination proteins that are widespread in organisms from bacteriophage to humans. Mgm101 is required for repeat-mediated recombination and suppression of mtDNA fragmentation in vivo. It preferentially binds to single-stranded DNA and catalyzes the annealing of ssDNA precomplexed with the mitochondrial ssDNA-binding protein, Rim1. Transmission electron microscopy showed that Mgm101 forms large oligomeric rings of ∼14-fold symmetry and highly compressed helical filaments. Specific mutations affecting ring formation reduce protein stability in vitro. The data suggest that the ring structure may provide a scaffold for stabilization of Mgm101 by preventing the aggregation of the otherwise unstable monomeric conformation. Upon binding to ssDNA, Mgm101 is remobilized from the rings to form distinct nucleoprotein filaments. These studies reveal a recombination protein of likely bacteriophage origin in mitochondria and support the notion that recombination is indispensable for mtDNA integrity.
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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.