Summary
120 phenotypic revertants of a temperature-sensitive alanyl-tRNA synthetase (alaS) mutant of Escherichia coli were isolated and screened for the ribosomal suppressor phenotype reported recently. About 20% of the mutants showed altered ribosomal sedimentation patterns which indicated a defect in ribosome assembly. The mutants were analysed by two-dimensional polyacrylamide gel electrophoresis and immunological methods for changes in ribosomal proteins.
Alterations of ribosomal proteins could be identified in three mutants. One of them (0–1) had an alteration in protein S5. The mutated protein was immunologically different not only from wild type S5 but also from the altered S5 of spectinomycin resistant mutants and from the altered S5 of mutants suppressing streptomycin dependence. Two other mutants (39-1 and 64-2) had an altered S20 protein. In one of them (64-2) protein S20 was present in a reduced amount compared to the amount of S20 in wild type ribosomes.
For the mutant (0–1) with the altered protein S5 a clear correlation could be demonstrated between the presence of the altered ribosomal protein and the suppression of temperature-sensitive growth of the alaS mutant.
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Communicated by E. Bautz
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Wittmann, H.G., Stöffler, G., Piepersberg, W. et al. Altered S5 and S20 ribosomal proteins in revertants of an alanyl-tRNA synthetase mutant of Escherichia coli . Molec. Gen. Genet. 134, 225–236 (1974). https://doi.org/10.1007/BF00267717
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DOI: https://doi.org/10.1007/BF00267717