ArticleMobile DNA2011
Effect of attC structure on cassette excision by integron integrases.
Article in Mobile DNA, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- Trade-off between canonical and unusual recombination sites promotes diversity and stability of gene cassette arrays of mobile integrons.Scientific reports · 2026Article
- Bacterial natural transformation drives cassette shuffling and simplifies recombination in chromosomal integrons.Nucleic acids research · 2025Article
- The recombination efficiency of the bacterial integron depends on the mechanical stability of the synaptic complex.Science advances · 2024Article
- Novel Mobile Integrons and Strain-Specific Integrase Genes withinMicroorganisms · 2022Article
- Integron Functionality and Genome Innovation: An Update on the Subtle and Smart Strategy of Integrase and Gene Cassette Expression Regulation.Microorganisms · 2022Review
- Predicting the taxonomic and environmental sources of integron gene cassettes using structural and sequence homology of attC sites.Communications biology · 2021Article
- Integron and its role in antimicrobial resistance: A literature review on some bacterial pathogens.Iranian journal of basic medical sciences · 2021Review
- A comprehensive survey of integron-associated genes present in metagenomes.BMC genomics · 2020Article
- Functional Analysis of theAntibiotics (Basel, Switzerland) · 2020Article
- Structure-specific DNA recombination sites: Design, validation, and machine learning-based refinement.Science advances · 2020Article
- New Determinants of Aminoglycoside Resistance and Their Association with the Class 1 Integron Gene Cassettes inInternational journal of molecular sciences · 2020Article
- Integrase-Mediated Recombination of theAntimicrobial agents and chemotherapy · 2018Article
- Class 1 integrons are low-cost structures in Escherichia coli.The ISME journal · 2017Article
- Efficiency of integron cassette insertion in correct orientation is ensured by the interplay of the three unpaired features of attC recombination sites.Nucleic acids research · 2016Article
- Diversity of Class 1 Integron Gene Cassette Rearrangements Selected under Antibiotic Pressure.Journal of bacteriology · 2015Article
- Quantitative and qualitative impact of hospital effluent on dissemination of the integron pool.The ISME journal · 2014Article
- Integrase-mediated recombination of the veb1 gene cassette encoding an extended-spectrum β-lactamase.PloS one · 2012Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIntegrons are genetic elements able to integrate and disseminate genes as cassettes by a site-specific recombination mechanism. These elements contain a gene coding for an integrase that carries out recombination by interacting with two different target sites; the attI site in cis with the integrase and the palindromic attC site of a gene cassette. Integron integrases (IntIs) bind specifically to the bottom strand of attC sites. The extrahelical bases resulting from folding of attC bottom strands are important for the recognition by integrases. These enzymes are directly involved in the accumulation and formation of new cassette arrangements in the variable region of integrons. Thus, it is important to better understand interactions between IntIs and their substrates.
resultsWe compared the ability of five IntIs to carry out excision of several cassettes flanked by different attC sites. The results showed that for most cassettes, IntI1 was the most active integrase. However, IntI2*179E and SonIntIA could easily excise cassettes containing the attCdfrA1 site located upstream, whereas IntI1 and IntI3 had only a weak excision activity for these cassettes. Analysis of the secondary structure adopted by the bottom strand of attCdfrA1 has shown that the identity of the extrahelical bases and the distance between them (A-N7-8-C) differ from those of attCs contained in the cassettes most easily excisable by IntI1 (T-N6-G). We used the attCdfrA1 site upstream of the sat2 gene cassette as a template and varied the identity and spacing between the extrahelical bases in order to determine how these modifications influence the ability of IntI1, IntI2*179E, IntI3 and SonIntIA to excise cassettes. Our results show that IntI1 is more efficient in cassette excision using T-N6-G or T-N6-C attCs while IntI3 recognizes only a limited range of attCs. IntI2*179E and SonIntIA are more tolerant of changes to the identity and spacing of extrahelical bases.
conclusionsThis study provides new insights into the factors that influence the efficiency of cassette excision by integron integrases. It also suggests that IntI2 and SonIntIA have an evolutionary path that is different from IntI1 and IntI3, in their ability to recognize and excise cassettes.
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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.