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Effects of streptomycin resistance mutations on posttranslational modification of ribosomal protein S12
Jennifer F Carr1, Daisy-Malloy Hamburg, Steven T Gregory
1Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, RI 02912, USA.
Abstract:
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.
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