Literature DB >> 111927

Methylation of basic proteins in ribosomes from wild-type and thiostrepton-resistant strains of Bacillus megaterium and their electrophoretic analysis.

M Cannon, E Cundliffe.   

Abstract

Ribosomes, radioactively labelled in vivo with both [1-14C]methionine and [methyl-3H]methionine, have been isolated from both wild-type and thiostrepton-resistant strains of Bacillus megaterium and their constituent proteins separated by two-dimensional gel electrophoresis. Ribosomes from the wild-type strain possess one basic protein that is extensively methylated. In contrast no such protein can be detected in ribosomes from the thiostrepton-resistant strain.

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Year:  1979        PMID: 111927     DOI: 10.1111/j.1432-1033.1979.tb13142.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Methylation of ribosomal proteins in bacteria: evidence of conserved modification of the eubacterial 50S subunit.

Authors:  A M Amaro; C A Jerez
Journal:  J Bacteriol       Date:  1984-04       Impact factor: 3.490

2.  Methylation of ribosomal proteins in Bacillus subtilis.

Authors:  E Mardones; A M Amaro; C A Jerez
Journal:  J Bacteriol       Date:  1980-04       Impact factor: 3.490

3.  Functional homology between E. coli ribosomal protein L11 and B. megaterium protein BM-L11.

Authors:  M J Stark; E Cundliffe; J Dijk; G Stöffler
Journal:  Mol Gen Genet       Date:  1980
  3 in total

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