Several thousand mutagenized clones of Escherichia coli were screened for methyl group incorporation into protein in crude extracts, in order to isolate mutants lacking the full complement of methyl groups in ribosomal proteins. One mutant isolated by this method and designated prm-1 incorporated 6-
Methylation of ribosomal proteins during ribosome assembly in Escherichia coli
โ Scribed by Chang, F. N.
- Publisher
- Springer
- Year
- 1981
- Tongue
- English
- Weight
- 433 KB
- Volume
- 183
- Category
- Article
- ISSN
- 0026-8925
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๐ SIMILAR VOLUMES
The ribosomes of an Escherichia coli mutant, designated prm-2, can be methylated in vitro by an enzymatic fraction from wild-type. This enzyme is inactive on the ribosomes from another mutant, prm-1, is reported previously to be methyl group-deficient in protein L11. In vitro methylation of prm-2 ri
Two genes governing ribosomal protein methylation have been located on the map of Escherichia coli by conjugation and transduction crosses between wild-type and prm (protein methylation) mutants. The Prm phenotype of recombinants was determined by an in vitro assay of methylgroups incorporation into
The exchange of ribosomal proteins among ribosomes of E. coli has been measured, using a density label technique. As expected most of the proteins do not exchange appreciably. However a substantial fraction of each of proteins S1, S2, S21, L7/L12, L9, L10, L11, L26 and L33 is found to exchange, but