ArticleNucleic acids research2018
The mitochondrial single-stranded DNA binding protein from S. cerevisiae, Rim1, does not form stable homo-tetramers and binds DNA as a dimer of dimers.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 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
- A bacterial expression cloning screen reveals single-stranded DNA-binding proteins as potent desicco-protectants.Cell reports · 2024Article
- Histidine-rich protein II nanoparticle delivery of heme iron load drives endothelial inflammation in cerebral malaria.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Crystal Structure of an SSB Protein fromInternational journal of molecular sciences · 2022Article
- Mechanisms of SSBP1 variants in mitochondrial disease: Molecular dynamics simulations reveal stable tetramers with altered DNA binding surfaces.DNA repair · 2021Article
- The LUFS domain, its transcriptional regulator proteins, and drug resistance in the fungal pathogen Candida auris.Protein science : a publication of the Protein Society · 2019Article
- Complementary roles of Pif1 helicase and single stranded DNA binding proteins in stimulating DNA replication through G-quadruplexes.Nucleic acids research · 2019Article
- A stable tetramer is not the only oligomeric state that mitochondrial single-stranded DNA binding proteins can adopt.The Journal of biological chemistry · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Rim1 is the mitochondrial single-stranded DNA binding protein in Saccharomyces cerevisiae and functions to coordinate replication and maintenance of mtDNA. Rim1 can form homo-tetramers in solution and this species has been assumed to be solely responsible for ssDNA binding. We solved structures of tetrameric Rim1 in two crystals forms which differ in the relative orientation of the dimers within the tetramer. In testing whether the different arrangement of the dimers was due to formation of unstable tetramers, we discovered that while Rim1 forms tetramers at high protein concentration, it dissociates into a smaller oligomeric species at low protein concentrations. A single point mutation at the dimer-dimer interface generates stable dimers and provides support for a dimer-tetramer oligomerization model. The presence of Rim1 dimers in solution becomes evident in DNA binding studies using short ssDNA substrates. However, binding of the first Rim1 dimer is followed by binding of a second dimer, whose affinity depends on the length of the ssDNA. We propose a model where binding of DNA to a dimer of Rim1 induces tetramerization, modulated by the ability of the second dimer to interact with ssDNA.
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