Mutations in aarE, the ubiA Homolog of Providencia stuartii, Result in High-Level Aminoglycoside Resistance and Reduced Expression of the Chromosomal Aminoglycoside 2′-N-Acetyltransferase |
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| Authors: | Michael R. Paradise Gregory Cook Robert K. Poole Philip N. Rather |
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| Affiliation: | Department of Medicine and Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine,1. and Research Service, Veterans Affairs Medical Center,3. Cleveland, Ohio 44106, and Microbial Physiology Research Group, King’s College London, London W8 & AH, United Kingdom2. |
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| Abstract: | The aarE1 allele was identified on the basis of the resulting phenotype of increased aminoglycoside resistance. The aarE1 mutation also resulted in a small-colony phenotype and decreased levels of aac(2′)-Ia mRNA. The deduced AarE gene product displayed 61% amino acid identity to the Escherichia coli UbiA protein, an octaprenyltransferase required for the second step of ubiquinone biosynthesis. Complementation experiments in both Providencia stuartii and E. coli demonstrated that aarE and ubiA are functionally equivalent. |
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