ArticleNucleic acids research2013
Attachment site recognition and regulation of directionality by the serine integrases.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 96 citations in OpenAlex.
- In vitro properties of large serine integrase hybrids derived from ϕC31 and TG1 integrases.Nucleic acids research · 2026Article
- Retargeted serine integrases for one-step, precise integration of large DNA sequences in human cells.Nature biotechnology · 2026Article
- Fourth-generation gene editors: Integration-based genome engineering.Molecular therapy. Advances · 2026Review
- S-SELeCT: a human-evolved serine integrase system for efficient large-cargo genome integration.Nucleic acids research · 2026Article
- Directed evolution on compact landing pads yields highly efficient recombinases for large DNA integration.Nucleic acids research · 2026Article
- Plasmid2MC: efficient cell-free generation of high-purity minicircle DNA for genome editing in mammalian cells.Communications biology · 2025Article
- Site-specific DNA insertion into the human genome with engineered recombinases.Nature biotechnology · 2025Article
- Advances in large-scale DNA engineering with the CRISPR system.Experimental & molecular medicine · 2025Review
- Identification of cognate recombination directionality factors for large serine recombinases by virtual pulldown.Nucleic acids research · 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
- Efficient site-specific integration of large genes in mammalian cells via continuously evolved recombinases and prime editing.Nature biomedical engineering · 2025Article
- There and turn back again: the application of phage serine integrases in eukaryotic systems.Frontiers in bioengineering and biotechnology · 2025Review
- Variable orthogonality of serine integrase interactions within the ϕC31 family.Scientific reports · 2024Article
- Directed evolution of hyperactive integrases for site specific insertion of transgenes.Nucleic acids research · 2024Article
- Directed evolution of hyperactive integrases for site specific insertion of transgenes.bioRxiv : the preprint server for biology · 2024Article
- Variable orthogonality of RDF - large serine integrase interactions within the ϕC31 family.bioRxiv : the preprint server for biology · 2024Article
- All-in-one IQ toggle switches with high versatilities for fine-tuning of transgene expression in mammalian cells and tissues.Molecular therapy. Methods & clinical development · 2024Article
- An efflux pump in genomic island GI-M202a mediates the transfer of polymyxin B resistance in Pandoraea pnomenusa M202.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- The influence of coiled-coil motif of serine recombinase toward the directionality regulation.Biophysical journal · 2023Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Serine integrases catalyze the integration of bacteriophage DNA into a host genome by site-specific recombination between 'attachment sites' in the phage (attP) and the host (attB). The reaction is highly directional; the reverse excision reaction between the product attL and attR sites does not occur in the absence of a phage-encoded factor, nor does recombination occur between other pairings of attachment sites. A mechanistic understanding of how these enzymes achieve site-selectivity and directionality has been limited by a lack of structural models. Here, we report the structure of the C-terminal domains of a serine integrase bound to an attP DNA half-site. The structure leads directly to models for understanding how the integrase-bound attP and attB sites differ, why these enzymes preferentially form attP × attB synaptic complexes to initiate recombination, and how attL × attR recombination is prevented. In these models, different domain organizations on attP vs. attB half-sites allow attachment-site specific interactions to form between integrase subunits via an unusual protruding coiled-coil motif. These interactions are used to preferentially synapse integrase-bound attP and attB and inhibit synapsis of integrase-bound attL and attR. The results provide a structural framework for understanding, testing and engineering serine integrase function.
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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.