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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 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.

SUBMITTER: Carr JF 

PROVIDER: S-EPMC1426572 | biostudies-literature | 2006 Mar

REPOSITORIES: biostudies-literature

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

Carr Jennifer F JF   Hamburg Daisy-Malloy DM   Gregory Steven T ST   Limbach Patrick A PA   Dahlberg Albert E AE  

Journal of bacteriology 20060301 5


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. ...[more]

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