title: 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.
abstract: 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.
authors.affiliation: Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02912, USA.
authors.forename: Jennifer F
authors.initials: JF
authors.lastname: Carr
authors.forename: Steven T
authors.initials: ST
authors.lastname: Gregory
authors.forename: Albert E
authors.initials: AE
authors.lastname: Dahlberg
mesh_terms: 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*
chemical_list: D012269:Ribosomal Proteins; C034212:ribosomal protein S12