Effects of streptomycin resistance mutations on posttranslational modification of ribosomal protein S12.
Ribosomal protein S12 contains a highly conserved aspartic acid residue that is posttranslationally beta-methylthiolated. Using mass spectrometry, we have determined the modification states of several S12 mutants of Thermus thermophilus and conclude that beta-methylthiolation is not a determinant of the streptomycin phenotype.
Carr
Jennifer F
JF
Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, RI 02912, USA.
Hamburg
Daisy-Malloy
DM
Gregory
Steven T
ST
Limbach
Patrick A
PA
Dahlberg
Albert E
AE
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001224:Aspartic Acid / Q000378:metabolism; D001412:Bacillus subtilis / Q000737:chemistry / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D024881:Drug Resistance, Bacterial; D008969:Molecular Sequence Data; D009154:Mutation; D011499:Protein Processing, Post-Translational; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013307:Streptomycin / Q000494:pharmacology*; D016963:Thermus thermophilus / Q000737:chemistry* / Q000187:drug effects*
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C034212:ribosomal protein S12; D001224:Aspartic Acid; D013307:Streptomycin