ArticleNucleic acids research2008
A motif in the C-terminal domain of phiC31 integrase controls the directionality of recombination.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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.
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.
Who cites it
42 citing papers in PubMed, 68 citations in OpenAlex.
- 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
- A new-engineered integrative tool to target the terminal compartment of the Streptomyces chromosome.Applied microbiology and biotechnology · 2026Article
- Site-specific DNA insertion into the human genome with engineered recombinases.Nature biotechnology · 2025Article
- Mitigating genetic instability caused by the excision activity of theApplied and environmental microbiology · 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
- The influence of coiled-coil motif of serine recombinase toward the directionality regulation.Biophysical journal · 2023Article
- 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
- Integrating vectors for genetic studies in the rare Actinomycete Amycolatopsis marina.BMC biotechnology · 2019Article
- Serine Integrase attP Binding and Specificity.Journal of molecular biology · 2018Article
- Diverse target gene modifications in Plasmodium falciparum using Bxb1 integrase and an intronic attB.Parasites & vectors · 2018Review
- Single-Molecule Tethered Particle Motion: Stepwise Analyses of Site-Specific DNA Recombination.Micromachines · 2018Review
- Recombination directionality factor gp3 binds ϕC31 integrase via the zinc domain, potentially affecting the trajectory of the coiled-coil motif.Nucleic acids research · 2018Article
- Using a phiC31 "Disintegrase" to make new attP sites in the Drosophila genome at locations showing chromosomal position effects.PloS one · 2018Article
- Control of serine integrase recombination directionality by fusion with the directionality factor.Nucleic acids research · 2017Article
- Coiled-coil interactions mediate serine integrase directionality.Nucleic acids research · 2017Article
- Control of Recombination Directionality by the Listeria Phage A118 Protein Gp44 and the Coiled-Coil Motif of Its Serine Integrase.Journal of bacteriology · 2017Article
- Genome Integration and Excision by a New Streptomyces Bacteriophage, ϕJoe.Applied and environmental microbiology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Bacteriophage C31 encodes an integrase, which acts on the phage and host attachment sites, attP and attB, to form an integrated prophage flanked by attL and attR. In the absence of accessory factors, C31 integrase cannot catalyse attL x attR recombination to excise the prophage. To understand the mechanism of directionality, mutant integrases were characterized that were active in excision. A hyperactive integrase, Int E449K, gained the ability to catalyse attL x attR, attL x attL and attR x attR recombination whilst retaining the ability to recombine attP x attB. A catalytically defective derivative of this mutant, Int S12A, E449K, could form stable complexes with attP/attB, attL/attR, attL/attL and attR/attR under conditions where Int S12A only complexed with attP/attB. Further analysis of the Int E449K-attL/attR synaptic events revealed a preference for one of the two predicted synapse structures with different orientations of the attL/attR sites. Several amino acid substitutions conferring hyperactivity, including E449K, were localized to one face of a predicted coiled-coil motif in the C-terminal domain. This work shows that a motif in the C-terminal domain of C31 integrase controls the formation of the synaptic interface in both integration and excision, possibly through a direct role in protein-protein interactions.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.