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Journal of Bacteriology, March 2006, p. 2020-2023, Vol. 188, No. 5
0021-9193/06/$08.00+0     doi:10.1128/JB.188.5.2020-2023.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Effects of Streptomycin Resistance Mutations on Posttranslational Modification of Ribosomal Protein S12

Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02912,¹ Rieveschl Laboratories for Mass Spectrometry, Department of Chemistry, University of Cincinnati, Cincinnati, Ohio 45221²

Received 14 November 2005/ Accepted 12 December 2005

Ribosomal protein S12 contains a highly conserved aspartic acid residue that is posttranslationally ß-methylthiolated. Using mass spectrometry, we have determined the modification states of several S12 mutants of Thermus thermophilus and conclude that ß-methylthiolation is not a determinant of the streptomycin phenotype.

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