ArticleNucleic acids research2017
Coiled-coil interactions mediate serine integrase directionality.
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 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Computational prediction resolves thousands of homooligomeric phage protein structures.bioRxiv : the preprint server for biology · 2026Article
- Directed evolution on compact landing pads yields highly efficient recombinases for large DNA integration.Nucleic acids research · 2026Article
- Site-specific DNA insertion into the human genome with engineered recombinases.Nature biotechnology · 2025Article
- Identification of cognate recombination directionality factors for large serine recombinases by virtual pulldown.Nucleic acids research · 2025Article
- Structural basis of directionality control in large serine integrases.bioRxiv : the preprint server for biology · 2025Article
- There and turn back again: the application of phage serine integrases in eukaryotic systems.Frontiers in bioengineering and biotechnology · 2025Review
- Versatile allelic replacement and self-excising integrative vectors for plasmid genome mutation and complementation.Microbiology spectrum · 2024Article
- Article
- The influence of coiled-coil motif of serine recombinase toward the directionality regulation.Biophysical journal · 2023Article
- A coiled-coil-based design strategy for the thermostabilization of G-protein-coupled receptors.Scientific reports · 2023Article
- A phage weaponizes a satellite recombinase to subvert viral restriction.Nucleic acids research · 2022Article
- 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
- Allosteric HIV Integrase Inhibitors Promote Formation of Inactive Branched Polymers via Homomeric Carboxy-Terminal Domain Interactions.Structure (London, England : 1993) · 2021Article
- A bipartite thermodynamic-kinetic contribution by an activating mutation to RDF-independent excision by a phage serine integrase.Nucleic acids research · 2020Article
- The ea22 gene of lambdoid phages: preserved prolysogenic function despite of high sequence diversity.Virus genes · 2020Article
- Serine Integrase attP Binding and Specificity.Journal of molecular biology · 2018Article
- 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
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Serine integrases are bacteriophage enzymes that carry out site-specific integration and excision of their viral genomes. The integration reaction is highly directional; recombination between the phage attachment site attP and the host attachment site attB to form the hybrid sites attL and attR is essentially irreversible. In a recent model, extended coiled-coil (CC) domains in the integrase subunits are proposed to interact in a way that favors the attPxattB reaction but inhibits the attLxattR reaction. Here, we show for the Listeria innocua integrase (LI Int) system that the CC domain promotes self-interaction in isolated Int and when Int is bound to attachment sites. Three independent crystal structures of the CC domain reveal the molecular nature of the CC dimer interface. Alanine substitutions of key residues in the interface support the functional significance of the structural model and indicate that the same interaction is responsible for promoting integration and for inhibiting excision. An updated model of a LI Int•attL complex that incorporates the high resolution CC dimer structure provides insights that help to explain the unusual CC dimer structure and potential sources of stability in Int•attL and Int•attR complexes. Together, the data provide a molecular basis for understanding serine integrase directionality.
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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.