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Synthesis and stability of individual ribosomal proteins in the presence of rifampicin

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Summary

The effects of rifampicin on the differential synthesis rate and stability of individual ribosomal proteins (r-proteins) was examined. The differential synthesis rate of the average r-protein was observed to increase following rifampicin, suggesting that r-proteins are organized into transcriptional units which are longer than the average genetic units being transcribed under these conditions of growth. From the changes in the differential synthesis rates after rifampicin an order of r-protein cistrons with respect to decreasing proximity to their respective promoters can be suggested; this order however is subject to certain assumptions which are discussed.

Following the termination of a short period of [3H] leucine labeling in the presence of rifampicin, the amount of radioactivity associated with many individual r-proteins was observed to gradually disappear. This observation suggests that some r-proteins synthesized in the presence of rifampcin are unstable; the onset of this instability of 30S and 50S r-proteins was correlated with the termination of the production of 16S and 23S rRNA.

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Communicated by H. Ozeki

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Dennis, P.P. Synthesis and stability of individual ribosomal proteins in the presence of rifampicin. Molec. gen. Genet. 134, 39–47 (1974). https://doi.org/10.1007/BF00332811

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