ArticleNature communications2022
Redβ
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 20 citations in OpenAlex.
- Mechanism of single-strand annealing from native mass spectrometry and cryo-EM structures of RAD52 homolog Mgm101.Nucleic acids research · 2026Article
- Enhancement of single-stranded template annealing activity by Rad52 during repair of CRISPR-induced dsDNA breaks.Nucleic acids research · 2026Article
- Compact bacterial recombination complexes drive efficient kilobase-scale knock-in in mammalian cells.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
- Monomers and short oligomers of human RAD52 promote single-strand annealing.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis for cooperative ssDNA binding by bacteriophage protein filament P12.Nucleic acids research · 2025Article
- Phage parasites targeting phage homologous recombinases provide antiviral immunity.Nature communications · 2025Article
- A structural phylogenetic tree of Rad52 and its annealase superfamily.Computational and structural biotechnology journal · 2025Article
- Novel Nuclease MbovP701 with a Yqaj Domain Is Interrelated with the Growth ofMicroorganisms · 2024Article
- Half a century after their discovery: Structural insights into exonuclease and annealase proteins catalyzing recombineering.Engineering microbiology · 2024Review
- Single-Stranded DNA-Binding Proteins Mediate DSB Repair and Effectively Improve CRISPR/Cas9 Genome Editing inMicroorganisms · 2023Article
- The cryo-EM structure of full-length RAD52 protein contains an undecameric ring.FEBS open bio · 2023Article
- The Rad52 SSAP superfamily and new insight into homologous recombination.Communications biology · 2023Article
- Structure of a RecT/Redβ family recombinase in complex with a duplex intermediate of DNA annealing.Nature communications · 2022Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Redβ protein of the bacteriophage λ red recombination system is a model annealase which catalyzes single-strand annealing homologous DNA recombination. Here we present the structure of a helical oligomeric annealing intermediate of Redβ, consisting of N-terminal residues 1-177 bound to two complementary 27mer oligonucleotides, determined via cryogenic electron microscopy (cryo-EM) to a final resolution of 3.3 Å. The structure reveals a continuous binding groove which positions and stabilizes complementary DNA strands in a planar orientation to facilitate base pairing via a network of hydrogen bonding. Definition of the inter-subunit interface provides a structural basis for the propensity of Redβ to oligomerize into functionally significant long helical filaments, a trait shared by most annealases. Our cryo-EM structure and molecular dynamics simulations suggest that residues 133-138 form a flexible loop which modulates access to the binding groove. More than half a century after its discovery, this combination of structural and computational observations has allowed us to propose molecular mechanisms for the actions of the model annealase Redβ, a defining member of the Redβ/RecT protein family.
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