ArticleJournal of molecular biology2010
Helical filaments of human Dmc1 protein on single-stranded DNA: a cautionary tale.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 18 citations in OpenAlex.
- Human RAD51 rapidly forms intrinsically dynamic nucleoprotein filaments modulated by nucleotide binding state.Nucleic acids research · 2018Article
- Multifrequency Force Microscopy of Helical Protein Assembly on a Virus.Scientific reports · 2016Article
- Structure determination of helical filaments by solid-state NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Functional Relationship of ATP Hydrolysis, Presynaptic Filament Stability, and Homologous DNA Pairing Activity of the Human Meiotic Recombinase DMC1.The Journal of biological chemistry · 2015Article
- Connecting by breaking and repairing: mechanisms of DNA strand exchange in meiotic recombination.The FEBS journal · 2015Review
- Structural plasticity of helical nanotubes based on coiled-coil assemblies.Structure (London, England : 1993) · 2015Article
- Ambiguities in helical reconstruction.eLife · 2014Article
- DNA strand exchange and RecA homologs in meiosis.Cold Spring Harbor perspectives in biology · 2014Review
- Sufficient amounts of functional HOP2/MND1 complex promote interhomolog DNA repair but are dispensable for intersister DNA repair during meiosis in Arabidopsis.The Plant cell · 2013Article
- Article
- Are ParM filaments polar or bipolar?Journal of molecular biology · 2012Article
- Filaments from Ignicoccus hospitalis show diversity of packing in proteins containing N-terminal type IV pilin helices.Journal of molecular biology · 2012Article
- The recombinases DMC1 and RAD51 are functionally and spatially separated during meiosis in Arabidopsis.The Plant cell · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Proteins in the RecA/Rad51/RadA family form nucleoprotein filaments on DNA that catalyze a strand exchange reaction as part of homologous genetic recombination. Because of the centrality of this system to many aspects of DNA repair, the generation of genetic diversity, and cancer when this system fails or is not properly regulated, these filaments have been the object of many biochemical and biophysical studies. A recent paper has argued that the human Dmc1 protein, a meiotic homolog of bacterial RecA and human Rad51, forms filaments on single-stranded DNA with approximately 9 subunits per turn in contrast to the filaments formed on double-stranded DNA with approximately 6.4 subunits per turn and that the stoichiometry of DNA binding is different between these two filaments. We show using scanning transmission electron microscopy that the Dmc1 filament formed on single-stranded DNA has a mass per unit length expected from approximately 6.5 subunits per turn. More generally, we show how ambiguities in helical symmetry determination can generate incorrect solutions and why one sometimes must use other techniques, such as biochemistry, metal shadowing, or scanning transmission electron microscopy, to resolve these ambiguities. While three-dimensional reconstruction of helical filaments from EM images is a powerful tool, the intrinsic ambiguities that may be present with limited resolution are not sufficiently appreciated.
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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.