Effects of streptomycin resistance mutations on posttranslational modification of ribosomal protein S12
Effects of streptomycin resistance mutations on posttranslational modification of ribosomal protein S12
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DOI：
10.1128/jb.188.5.2020-2023.2006
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发表时间：
2006-03-01
影响因子：
3.2
通讯作者：
Dahlberg, AE
中科院分区：
文献类型：
--
作者：
Carr, JF;Hamburg, DM;Dahlberg, AE
核糖体蛋白S12含有一个高度保守的天冬氨酸残基，它在翻译后是β-甲基硫醇化的。用质谱仪测定了嗜热菌S12突变体的修饰状态，得出结论：β-甲硫基化不是链霉素表型的决定因素。
Ribosomal protein S12 contains a highly conserved aspartic acid residue that is posttranslationally beta-methyl-thiolated. 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.