Evidence map›Paper›PMID 27387286›Full record

ArticleNucleic acids research2016

The mechanism of ϕC31 integrase directionality: experimental analysis and computational modelling.

Alexandra Pokhilko, Jia Zhao, Oliver Ebenhöh, Margaret C M Smith, W Marshall Stark, Sean D Colloms

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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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 2 countries.

Alexandra PokhilkoInstitute of Molecular, Cell and Systems Biology, Bower Building, University of Glasgow, Glasgow G12 8QQ, Scotland, UK.
Jia ZhaoInstitute of Molecular, Cell and Systems Biology, Bower Building, University of Glasgow, Glasgow G12 8QQ, Scotland, UK.
Oliver EbenhöhCluster of Excellence on Plant Sciences (CEPLAS), Heinrich-Heine-University, Universitätsstraße 1, D-40225 Düsseldorf, Germany Institute for Complex Systems and Mathematical Biology, University of Aberdeen, AB24 3UE, UK.
Margaret C M SmithDepartment of Biology, University of York, Wentworth Way, York YO10 5DD, UK.
W Marshall StarkInstitute of Molecular, Cell and Systems Biology, Bower Building, University of Glasgow, Glasgow G12 8QQ, Scotland, UK Marshall.Stark@glasgow.ac.uk.
Sean D CollomsInstitute of Molecular, Cell and Systems Biology, Bower Building, University of Glasgow, Glasgow G12 8QQ, Scotland, UK Sean.Colloms@glasgow.ac.uk.
University of Glasgow · GBCluster of Excellence on Plant Sciences · DEUniversity of York · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K003356/1
6 · The paper itself

Abstract

Serine integrases, DNA site-specific recombinases used by bacteriophages for integration and excision of their DNA to and from their host genomes, are increasingly being used as tools for programmed rearrangements of DNA molecules for biotechnology and synthetic biology. A useful feature of serine integrases is the simple regulation and unidirectionality of their reactions. Recombination between the phage attP and host attB sites is promoted by the serine integrase alone, giving recombinant attL and attR sites, whereas the 'reverse' reaction (between attL and attR) requires an additional protein, the recombination directionality factor (RDF). Here, we present new experimental data on the kinetics and regulation of recombination reactions mediated by ϕC31 integrase and its RDF, and use these data as the basis for a mathematical model of the reactions. The model accounts for the unidirectionality of the attP × attB and attL × attR reactions by hypothesizing the formation of structurally distinct, kinetically stable integrase-DNA product complexes, dependent on the presence or absence of RDF. The model accounts for all the available experimental data, and predicts how mutations of the proteins or alterations of reaction conditions might increase the conversion efficiency of recombination.

Indexed as

Computer SimulationRecombination, GeneticAttachment Sites, MicrobiologicalBiological AssayBiological FactorsDNAEnzyme StabilityIntegrasesKineticsModels, BiologicalPlasmidsThermodynamicsViral ProteinsBiological FactorsDNAIntegrasesViral Proteins

Identifiers

PMID27387286
PMCPMC5009753
OpenAlexW2466157466

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.