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- W2243859980 abstract "Thinking concerning mutants of the prokaryotic ribosome (which are overwhelmingly mutants altered in the protein component of this organelle) has gone through several stages. Until about 10 years ago, when identification of the altered component in a ribosomal mutant was possible then it turned out that the alternation was in one of a small subset of the 52 or so proteins. Thus, Escherichia coli mutations conferring resistance to the antibiotic spectinomycin, relieving dependence on the antibiotic streptomycin for growth, and suppressing temperature-sensitive tRNA synthetase lesions may all be the result of mutations in the gene for ribosomal protein S5 (Piepersberg et al., 1975). Mutants altered in proteins S4 and S12 were also readily obtained. Inability to obtain mutants with alterations in most other ribosomal proteins (r-proteins) was assumed to be the consequence of such alterations being lethal to the cell: An organelle consisting of about 60 different components might be thrown irreversibly out of kilter from the pleiotropic effects of change in even a single component." @default.
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- W2243859980 date "1986-01-01" @default.
- W2243859980 modified "2023-09-23" @default.
- W2243859980 title "Mutant Studies on the Prokaryotic Ribosome" @default.
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- W2243859980 doi "https://doi.org/10.1007/978-1-4612-4884-2_43" @default.
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