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Methylation of ribosomal proteins during ribosome assembly in Escherichia coli

โœ 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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Genetics of ribosomal protein methylatio
โœ Colson, Charles ;Smith, Hamilton O. ๐Ÿ“‚ Article ๐Ÿ“… 1977 ๐Ÿ› Springer ๐ŸŒ English โš– 689 KB

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-

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โœ Lhoest, Jacques ;Colson, Charles ๐Ÿ“‚ Article ๐Ÿ“… 1977 ๐Ÿ› Springer ๐ŸŒ English โš– 493 KB

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

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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

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โœ Robertson, W. R. ;Dowsett, S. J. ;Hardy, S. J. S. ๐Ÿ“‚ Article ๐Ÿ“… 1977 ๐Ÿ› Springer ๐ŸŒ English โš– 932 KB

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