Abstract
A new aminoglycoside resistance gene (aphA1-IAB) confers high-level resistance to neomycin. The sequence of aphA1-IAB is closely related to aphA1 found in the transposons TN4352, TN903 and Tn602. For example, aphA1-IAB differs from aphA1-903 at five nucleotides that result in four amino acid replacements. The enzyme encoded by aphA1-IAB has a significantly higher turnover number with neomycin, kanamycin and G418 as substrates than does the aphA1-903 enzyme. A parsimonious phylogenetic tree suggests that aphA1-IAB evolved from an ancestral form that is closely related or identical to the aphA1 found in Tn903. The excess of replacement substitutions over silent substitutions in aphA1-IAB, as well as its convergence toward aphA3 from Staphylococcus aureus, is indicative of selective evolution. Our hypothesis to explain these results is that aphA1-IAB evolved under the selective pressure of neomycin use in relatively recent times.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2039-2046 |
| Number of pages | 8 |
| Journal | Molecular Microbiology |
| Volume | 5 |
| Issue number | 8 |
| State | Published - Aug 1991 |
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ASJC Scopus subject areas
- Molecular Biology
- Microbiology
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Evolved neomycin phosphotransferase from an isolate of Klebsiella pneumoniae. / Lee, K. Y.; Hopkins, J. D.; Syvanen, Michael.
In: Molecular Microbiology, Vol. 5, No. 8, 08.1991, p. 2039-2046.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Evolved neomycin phosphotransferase from an isolate of Klebsiella pneumoniae
AU - Lee, K. Y.
AU - Hopkins, J. D.
AU - Syvanen, Michael
PY - 1991/8
Y1 - 1991/8
N2 - A new aminoglycoside resistance gene (aphA1-IAB) confers high-level resistance to neomycin. The sequence of aphA1-IAB is closely related to aphA1 found in the transposons TN4352, TN903 and Tn602. For example, aphA1-IAB differs from aphA1-903 at five nucleotides that result in four amino acid replacements. The enzyme encoded by aphA1-IAB has a significantly higher turnover number with neomycin, kanamycin and G418 as substrates than does the aphA1-903 enzyme. A parsimonious phylogenetic tree suggests that aphA1-IAB evolved from an ancestral form that is closely related or identical to the aphA1 found in Tn903. The excess of replacement substitutions over silent substitutions in aphA1-IAB, as well as its convergence toward aphA3 from Staphylococcus aureus, is indicative of selective evolution. Our hypothesis to explain these results is that aphA1-IAB evolved under the selective pressure of neomycin use in relatively recent times.
AB - A new aminoglycoside resistance gene (aphA1-IAB) confers high-level resistance to neomycin. The sequence of aphA1-IAB is closely related to aphA1 found in the transposons TN4352, TN903 and Tn602. For example, aphA1-IAB differs from aphA1-903 at five nucleotides that result in four amino acid replacements. The enzyme encoded by aphA1-IAB has a significantly higher turnover number with neomycin, kanamycin and G418 as substrates than does the aphA1-903 enzyme. A parsimonious phylogenetic tree suggests that aphA1-IAB evolved from an ancestral form that is closely related or identical to the aphA1 found in Tn903. The excess of replacement substitutions over silent substitutions in aphA1-IAB, as well as its convergence toward aphA3 from Staphylococcus aureus, is indicative of selective evolution. Our hypothesis to explain these results is that aphA1-IAB evolved under the selective pressure of neomycin use in relatively recent times.
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M3 - Article
C2 - 1662755
AN - SCOPUS:0025864241
VL - 5
SP - 2039
EP - 2046
JO - Molecular Microbiology
JF - Molecular Microbiology
SN - 0950-382X
IS - 8
ER -