ArticleNucleic acids research2017
Control of serine integrase recombination directionality by fusion with the directionality factor.
Article in Nucleic acids research, 2017. 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, 34 citations in OpenAlex.
- In vitro properties of large serine integrase hybrids derived from ϕC31 and TG1 integrases.Nucleic acids research · 2026Article
- Programmable cell differentiation in budding yeast uncouples reproductive and metabolic tasks.bioRxiv : the preprint server for biology · 2025Article
- 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
- 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
- A bipartite thermodynamic-kinetic contribution by an activating mutation to RDF-independent excision by a phage serine integrase.Nucleic acids research · 2020Article
- A memory switch for plant synthetic biology based on the phage ϕC31 integration system.Nucleic acids research · 2020Article
- Article
- Control of ϕC31 integrase-mediated site-specific recombination by protein trans-splicing.Nucleic acids research · 2019Article
- A single-input binary counting module based on serine integrase site-specific recombination.Nucleic acids research · 2019Article
- Diverse target gene modifications in Plasmodium falciparum using Bxb1 integrase and an intronic attB.Parasites & vectors · 2018Review
- Mathematical model of a serine integrase-controlled toggle switch with a single input.Journal of the Royal Society, Interface · 2018Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Bacteriophage serine integrases are extensively used in biotechnology and synthetic biology for assembly and rearrangement of DNA sequences. Serine integrases promote recombination between two different DNA sites, attP and attB, to form recombinant attL and attR sites. The 'reverse' reaction requires another phage-encoded protein called the recombination directionality factor (RDF) in addition to integrase; RDF activates attL × attR recombination and inhibits attP × attB recombination. We show here that serine integrases can be fused to their cognate RDFs to create single proteins that catalyse efficient attL × attR recombination in vivo and in vitro, whereas attP × attB recombination efficiency is reduced. We provide evidence that activation of attL × attR recombination involves intra-subunit contacts between the integrase and RDF moieties of the fusion protein. Minor changes in the length and sequence of the integrase-RDF linker peptide did not affect fusion protein recombination activity. The efficiency and single-protein convenience of integrase-RDF fusion proteins make them potentially very advantageous for biotechnology/synthetic biology applications. Here, we demonstrate efficient gene cassette replacement in a synthetic metabolic pathway gene array as a proof of principle.
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