ArticleNucleic acids research2019
Crystal structure of the Redβ C-terminal domain in complex with λ Exonuclease reveals an unexpected homology with λ Orf and an interaction with Escherichia coli single stranded DNA binding protein.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 18 citations in OpenAlex.
- ETfinder: harnessing conserved C-terminal tails of single-stranded DNA-binding proteins for mining and engineering RecET systems in non-model microbial chassis.Nucleic acids research · 2026Article
- 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
- Efficient high-precision transgene knock-in by Recombinases (Redα/β)-enhanced DNA integration-CRISPR-Cas9 (RED-CRISPR).Nature communications · 2025Article
- 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 recombineering-based platform for high-throughput genomic editing inApplied and environmental microbiology · 2025Article
- A diverse single-stranded DNA-annealing protein library enables efficient genome editing across bacterial phyla.Proceedings of the National Academy of Sciences of the United States of America · 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
- Proof of ssDNA degraded from dsDNA for ET recombination.Biochemistry and biophysics reports · 2024Article
- Half a century after their discovery: Structural insights into exonuclease and annealase proteins catalyzing recombineering.Engineering microbiology · 2024Review
- The emerging role of recombineering in microbiology.Engineering microbiology · 2023Review
- 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
- RedβNature communications · 2022Article
- ReScribe: An Unrestrained Tool Combining Multiplex Recombineering and Minimal-PAM ScCas9 for Genome RecodingACS synthetic biology · 2021Article
- Mutational Analysis of Redβ Single Strand Annealing Protein: Roles of the 14 Lysine Residues in DNA Binding and Recombination In Vivo.International journal of molecular sciences · 2021Article
- Identification of phage recombinase function unit in genus Corynebacterium.Applied microbiology and biotechnology · 2021Article
- Oligomeric complexes formed by Redβ single strand annealing protein in its different DNA bound states.Nucleic acids research · 2021Article
- Characterizing the portability of phage-encoded homologous recombination proteins.Nature chemical biology · 2021Article
- Recombineering and MAGE.Nature reviews. Methods primers · 2021Article
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9 authors at 2 institutions in 1 country.
Funding
Abstract
Bacteriophage λ encodes a DNA recombination system that includes a 5'-3' exonuclease (λ Exo) and a single strand annealing protein (Redβ). The two proteins form a complex that is thought to mediate loading of Redβ directly onto the single-stranded 3'-overhang generated by λ Exo. Here, we present a 2.3 Å crystal structure of the λ Exo trimer bound to three copies of the Redβ C-terminal domain (CTD). Mutation of residues at the hydrophobic core of the interface disrupts complex formation in vitro and impairs recombination in vivo. The Redβ CTD forms a three-helix bundle with unexpected structural homology to phage λ Orf, a protein that binds to E. coli single-stranded DNA binding protein (SSB) to function as a recombination mediator. Based on this relationship, we found that Redβ binds to full-length SSB, and to a peptide corresponding to its nine C-terminal residues, in an interaction that requires the CTD. These results suggest a dual role of the CTD, first in binding to λ Exo to facilitate loading of Redβ directly onto the initial single-stranded DNA (ssDNA) at a 3'-overhang, and second in binding to SSB to facilitate annealing of the overhang to SSB-coated ssDNA at the replication fork.
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