Characterization of aarA, a pleiotrophic negative regulator of the 2'-N-acetyltransferase in Providencia stuartii.
We have utilized transposon mutagenesis to obtain insertional mutations in Providencia stuartii that activate the chromosomal aac(2')-la gene. Two closely linked mini-Tn5Cm insertions were obtained in a locus designated aarA, and a single insertion was obtained in a separate locus, aarC. Nucleotide sequence analysis, complementation studies, and localization of the sites of mini-Tn5Cm insertion have allowed the identification of the aarA coding region. The deduced AarA protein had a molecular mass of 31,086 kDa and displayed characteristics of an integral membrane protein. A strain deleted for the aarA gene by allelic exchange showed at least a fourfold increase in the accumulation of aac(2')-la mRNA and an eightfold increase in aminoglycoside resistance. Mutations in aarA were pleiotrophic and also resulted in loss of pigmentation and a deficiency in cell separation during division.
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Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, Ohio.
Orosz
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D000123:Acetyltransferases / Q000235:genetics*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D001483:Base Sequence; D003001:Cloning, Molecular; D004251:DNA Transposable Elements; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D005798:Genes, Bacterial; D005809:Genes, Regulator; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D011532:Providencia / Q000235:genetics*; D012097:Repressor Proteins / Q000235:genetics*; D017384:Sequence Deletion
D001426:Bacterial Proteins; D004251:DNA Transposable Elements; D012097:Repressor Proteins; C088713:aarA protein, Providencia stuartii; D000123:Acetyltransferases; C019681:aminoglycoside acetyltransferase