Severity of the streptomycin resistance and streptomycin dependence phenotypes of ribosomal protein S12 of Thermus thermophilus depends on the identity of highly conserved amino acid residues.
The structural basis for the streptomycin dependence phenotype of ribosomal protein S12 mutants is poorly understood. Here we describe the application of site-directed mutagenesis and gene replacement of Thermus thermophilus rpsL to assess the importance of side chain identity and tertiary interactions as phenotypic determinants of drug-dependent mutants.
Carr
Jennifer F
JF
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02912, USA.
Gregory
Steven T
ST
Dahlberg
Albert E
AE
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D024881:Drug Resistance, Bacterial; D016297:Mutagenesis, Site-Directed; D010641:Phenotype; D017434:Protein Structure, Tertiary; D012269:Ribosomal Proteins / Q000737:chemistry / Q000235:genetics*; D016963:Thermus thermophilus / Q000187:drug effects* / Q000235:genetics*
D012269:Ribosomal Proteins; C034212:ribosomal protein S12