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.
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Carr, J. F., Hamburg, D. M., Gregory, S. T., Limbach, P. A., & Dahlberg, A. E. (2006). Effects of streptomycin resistance mutations on posttranslational modification of ribosomal protein S12. Journal of Bacteriology, 188(5), 2020–2023. https://doi.org/10.1128/JB.188.5.2020-2023.2006
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