Evidence map›Paper›PMID 31667500›Full record

ArticleNucleic acids research2019

Control of ϕC31 integrase-mediated site-specific recombination by protein trans-splicing.

Femi J Olorunniji, Makeba Lawson-Williams, Arlene L McPherson, Jane E Paget, W Marshall Stark, Susan J Rosser

Open access · goldAbstract read
In one paragraph

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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.5field-weighted citation impact, top 35% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural basis of directionality control in large serine integrases.bioRxiv : the preprint server for biology · 2025
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. A Genetic Circuit Design for Targeted Viral RNA Degradation.Bioengineering (Basel, Switzerland) · 2023
    Article
  10. Review
  11. Article
  12. Article
  13. Engineering the Erythromycin-Producing StrainFrontiers in microbiology · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Femi J OlorunnijiSchool of Pharmacy and Biomolecular Sciences, Faculty of Science, Liverpool John Moores University, James Parsons Building, Byrom Street, Liverpool L3 3AF, UK.
Makeba Lawson-WilliamsSchool of Pharmacy and Biomolecular Sciences, Faculty of Science, Liverpool John Moores University, James Parsons Building, Byrom Street, Liverpool L3 3AF, UK.
Arlene L McPhersonInstitute of Molecular, Cell and Systems Biology, University of Glasgow, Bower Building, Glasgow G12 8QQ, UK.
Jane E PagetUK Centre for Mammalian Synthetic Biology at the Institute of Quantitative Biology, Biochemistry, and Biotechnology, SynthSys, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3JD, UK.
W Marshall StarkInstitute of Molecular, Cell and Systems Biology, University of Glasgow, Bower Building, Glasgow G12 8QQ, UK.
Susan J RosserUK Centre for Mammalian Synthetic Biology at the Institute of Quantitative Biology, Biochemistry, and Biotechnology, SynthSys, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3JD, UK.
Liverpool John Moores University · GBUniversity of Edinburgh · GBUniversity of Glasgow · GB

Funding

Biotechnology and Biological Sciences Research Council BB/003356/1Biotechnology and Biological Sciences Research Council BB/M018040/1Biotechnology and Biological Sciences Research Council BB/M018229/1Medical Research Council MC_PC_16077
6 · The paper itself

Abstract

Serine integrases are emerging as core tools in synthetic biology and have applications in biotechnology and genome engineering. We have designed a split-intein serine integrase-based system with potential for regulation of site-specific recombination events at the protein level in vivo. The ϕC31 integrase was split into two extein domains, and intein sequences (Npu DnaEN and Ssp DnaEC) were attached to the two termini to be fused. Expression of these two components followed by post-translational protein trans-splicing in Escherichia coli generated a fully functional ϕC31 integrase. We showed that protein splicing is necessary for recombination activity; deletion of intein domains or mutation of key intein residues inactivated recombination. We used an invertible promoter reporter system to demonstrate a potential application of the split intein-regulated site-specific recombination system in building reversible genetic switches. We used the same split inteins to control the reconstitution of a split Integrase-Recombination Directionality Factor fusion (Integrase-RDF) that efficiently catalysed the reverse attR x attL recombination. This demonstrates the potential for split-intein regulation of the forward and reverse reactions using the integrase and the integrase-RDF fusion, respectively. The split-intein integrase is a potentially versatile, regulatable component for building synthetic genetic circuits and devices.

Indexed as

Recombination, GeneticAmino Acid SequenceCloning, MolecularEscherichia coliExteinsIntegrasesInteinsOrganisms, Genetically ModifiedProtein EngineeringProtein SplicingSerineSubstrate SpecificityTrans-SplicingIntegrasesSerine

Identifiers

PMID31667500
PMCPMC6868429
OpenAlexW2988717646

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.