ArticleNucleic acids research2018
Recombination directionality factor gp3 binds ϕC31 integrase via the zinc domain, potentially affecting the trajectory of the coiled-coil motif.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- In vitro properties of large serine integrase hybrids derived from ϕC31 and TG1 integrases.Nucleic acids research · 2026Article
- Identification of cognate recombination directionality factors for large serine recombinases by virtual pulldown.Nucleic acids research · 2025Article
- Large serine integrases utilise scavenged phage proteins as directionality cofactors.Nucleic acids research · 2025Article
- Structural basis of directionality control in large serine integrases.bioRxiv : the preprint server for biology · 2025Article
- There and turn back again: the application of phage serine integrases in eukaryotic systems.Frontiers in bioengineering and biotechnology · 2025Review
- Variable orthogonality of serine integrase interactions within the ϕC31 family.Scientific reports · 2024Article
- Variable orthogonality of RDF - large serine integrase interactions within the ϕC31 family.bioRxiv : the preprint server for biology · 2024Article
- Article
- The influence of coiled-coil motif of serine recombinase toward the directionality regulation.Biophysical journal · 2023Article
- Systematic discovery of recombinases for efficient integration of large DNA sequences into the human genome.Nature biotechnology · 2023Article
- A Bacterial Two-Hybrid System for In Vivo Assays of Protein-Protein Interactions and Drug Discovery.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Control of the Serine Integrase Reaction: Roles of the Coiled-Coil and Helix E Regions in DNA Site Synapsis and Recombination.Journal of bacteriology · 2021Article
- A bipartite thermodynamic-kinetic contribution by an activating mutation to RDF-independent excision by a phage serine integrase.Nucleic acids research · 2020Article
- Identification of the First Gene Transfer Agent (GTA) Small Terminase inJournal of virology · 2019Article
- Single-Molecule Tethered Particle Motion: Stepwise Analyses of Site-Specific DNA Recombination.Micromachines · 2018Review
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Authors and funding
6 authors at 3 institutions in 1 country.
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Abstract
To establish a prophage state, the genomic DNA of temperate bacteriophages normally becomes integrated into the genome of their host bacterium by integrase-mediated, site-specific DNA recombination. Serine integrases catalyse a single crossover between an attachment site in the host (attB) and a phage attachment site (attP) on the circularized phage genome to generate the integrated prophage DNA flanked by recombinant attachment sites, attL and attR. Exiting the prophage state and entry into the lytic growth cycle requires an additional phage-encoded protein, the recombination directionality factor or RDF, to mediate recombination between attL and attR and excision of the phage genome. The RDF is known to bind integrase and switch its activity from integration (attP x attB) to excision (attL x attR) but its precise mechanism is unclear. Here, we identify amino acid residues in the RDF, gp3, encoded by the Streptomyces phage ϕC31 and within the ϕC31 integrase itself that affect the gp3:Int interaction. We show that residue substitutions in integrase that reduce gp3 binding adversely affect both excision and integration reactions. The mutant integrase phenotypes are consistent with a model in which the RDF binds to a hinge region at the base of the coiled-coil motif in ϕC31 integrase.
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