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Full-length integrase genes in class 2 integrons are rare but can catalyze gene cassette movement. Specific variants show higher integration and excision efficiency, with limited impact from amino acid polymorphisms.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Genetics

Background:

  • Integrons are key in spreading antimicrobial resistance genes.
  • Class 2 integrons typically possess a truncated integrase (IntI2*) due to an internal stop codon.
  • Natural full-length integrase genes (intI2) in class 2 integrons are infrequently reported.

Purpose of the Study:

  • To analyze natural full-length intI2 sequences from the INTEGRALL database.
  • To evaluate the gene cassette integration and excision activities of different full-length IntI2 variants.
  • To investigate the impact of amino acid polymorphisms on IntI2 function.

Main Methods:

  • Retrieved 236 intI2 sequences from the INTEGRALL database.
  • Identified seven natural full-length intI2 genes, categorized into five types based on amino acid sequences.
  • Utilized quantitative real-time PCR to assess integration and excision efficiencies catalyzed by IntI2 variants in Escherichia coli.
  • Predicted secondary structures of IntI2 proteins using online software.

Main Results:

  • All five identified full-length IntI2 variants could catalyze sat2 gene cassette integration and specific excision events.
  • IntI2 variant A176 demonstrated the highest integration and excision frequency, approximately double that of IntI2 S175_A176.
  • Amino acid polymorphisms were located away from predicted functional sites, suggesting limited influence on catalytic activity.

Conclusions:

  • Natural full-length class 2 integrases are functional and capable of catalyzing gene cassette recombination.
  • Specific IntI2 variants exhibit varying catalytic efficiencies, with IntI2 A176 being the most active.
  • Observed amino acid variations in full-length IntI2s have a minimal effect on their enzymatic activity.