title: The phenotypic suppression of a mutation in the gene rplX for ribosomal protein L24 by mutations affecting the lon gene product for protease LA in Escherichia coli K12.
abstract: A suppressor mutation of a temperature-sensitive mutant of ribosomal protein L24 (rplX19) was mapped close to the lon gene by genetic analysis and was shown to affect protease LA. The degradation and the synthesis rates of individual ribosomal proteins were determined. Proteins L24, L14, L15 and L27 were found to be degraded faster in the original rplX19 mutant than in the rplX19 mutant containing the suppressor mutation. Other ribosomal proteins were either weakly or not at all degraded in both mutants. Temperature-sensitive growth was also suppressed by the overproduction of mutant protein L24 from a plasmid. Our results suggest that (1) either free ribosomal proteins or proteins bound to abortive assembly precursors are highly susceptible to the lon gene product and (2) the mutationally altered protein L24 can still function at the nonpermissive growth temperature of the mutant, if it is present in sufficient amounts.
authors.affiliation: Max-Planck-Institut für Molekulare Genetik, Abt. Wittmann, Berlin, Dahlem.
authors.forename: K
authors.initials: K
authors.lastname: Nishi
authors.forename: J
authors.initials: J
authors.lastname: Schnier
mesh_terms: D049069:ATP-Dependent Proteases; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D029968:Escherichia coli Proteins; D005796:Genes; D005798:Genes, Bacterial; D006360:Heat-Shock Proteins; D007700:Kinetics; D009154:Mutation; D010641:Phenotype; D010957:Plasmids; D049070:Protease La; D012269:Ribosomal Proteins / Q000235:genetics* / Q000378:metabolism; D012697:Serine Endopeptidases / Q000235:genetics*; D013489:Suppression, Genetic
chemical_list: D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D012269:Ribosomal Proteins; C036298:ribosomal protein L24; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La