ArticleBiology open2014
Serine integrase chimeras with activity in E. coli and HeLa cells.
Article in Biology open, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Programmable enzymes for targeted gene insertion.Nature reviews. Genetics · 2026Review
- In vitro properties of large serine integrase hybrids derived from ϕC31 and TG1 integrases.Nucleic acids research · 2026Article
- S-SELeCT: a human-evolved serine integrase system for efficient large-cargo genome integration.Nucleic acids research · 2026Article
- There and turn back again: the application of phage serine integrases in eukaryotic systems.Frontiers in bioengineering and biotechnology · 2025Review
- Systematic discovery of recombinases for efficient integration of large DNA sequences into the human genome.Nature biotechnology · 2023Article
- Diverse target gene modifications in Plasmodium falciparum using Bxb1 integrase and an intronic attB.Parasites & vectors · 2018Review
- A novel family of tyrosine integrases encoded by the temperate pleolipovirus SNJ2.Nucleic acids research · 2018Article
- Control of serine integrase recombination directionality by fusion with the directionality factor.Nucleic acids research · 2017Article
- Mechanism of bacterial gene rearrangement: SprA-catalyzed precise DNA recombination and its directionality control by SprB ensure the gene rearrangement and stable expression of spsM during sporulation in Bacillus subtilis.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In recent years, application of serine integrases for genomic engineering has increased in popularity. The factor-independence and unidirectionality of these large serine recombinases makes them well suited for reactions such as site-directed vector integration and cassette exchange in a wide variety of organisms. In order to generate information that might be useful for altering the specificity of serine integrases and to improve their efficiency, we tested a hybridization strategy that has been successful with several small serine recombinases. We created chimeras derived from three characterized members of the serine integrase family, phiC31, phiBT1, and TG1 integrases, by joining their amino- and carboxy-terminal portions. We found that several phiBT1-phiC31 (BC) and phiC31-TG1 (CT) hybrid integrases are active in E. coli. BC chimeras function on native att-sites and on att-sites that are hybrids between those of the two donor enzymes, while CT chimeras only act on the latter att-sites. A BC hybrid, BC{-1}, was also active in human HeLa cells. Our work is the first to demonstrate chimeric serine integrase activity. This analysis sheds light on integrase structure and function, and establishes a potentially tractable means to probe the specificity of the thousands of putative large serine recombinases that have been revealed by bioinformatics studies.
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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.