Effects of streptomycin resistance mutations on posttranslational modification of ribosomal protein S12

Abstract

Ribosomal protein S12 contains a highly conserved aspartic acid residue that is posttranslationally β-methylthiolated. Using mass spectrometry, we have determined the modification states of several S12 mutants of Thermus thermophilus and conclude that β-methylthiolation is not a determinant of the streptomycin phenotype. Copyright © 2006, American Society for Microbiology. All Rights Reserved.