title: Streptomyces relC mutants with an altered ribosomal protein ST-L11 and genetic analysis of a Streptomyces griseus relC mutant.
abstract: Several relaxed (rel) mutants have been obtained from Streptomyces species by selecting colonies resistant to thiopeptin, an analogue of thiostrepton. Using two-dimensional gel electrophoresis, I compared the ribosomal proteins from rel and rel+ pairs of S. antibioticus, S. lavendulae, S. griseoflavus, and S. griseus. It was found that all of the Streptomyces rel mutants thus examined had an altered or missing ribosomal protein, designated tentatively ST-L11. These rel mutants therefore could be classified as relC mutants and were highly sensitive to erythromycin or high temperature. A relC mutant of S. griseus was defective in streptomycin production, but phenotypic reversion of this defect to normal productivity was found at high incidence among progeny of the relC mutant. This phenotypic reversion did not accompany a reappearance of ribosomal protein ST-L11, and furthermore the ability of accumulating ppGpp still remained at a low level, thus suggesting existence of a mutation (named sup) which suppresses the streptomycin deficiency phenotype exhibited by the relC mutant. Genetic analysis revealed that there is a correlation between the rel mutation and the inability to produce streptomycin or aerial mycelia. The sup mutation was found to lie at a chromosomal locus distinct from that of the relC mutation. It was therefore concluded that the dependence of streptomycin production on the normal function of the relC gene could be entirely bypassed by a mutation at the suppressor locus (sup). The suppressing effect of the sup mutation on the relC mutation was blocked when the afs mutation (defective in A-factor synthesis) was introduced into a relC sup double mutant. It is proposed that the sup gene or its product can be direct or indirect target for ppGpp.
authors.affiliation: Exploratory Research Laboratories, Fujisawa Pharmaceutical Co., Ltd., Ibaraki, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Ochi
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D003433:Crosses, Genetic; D004352:Drug Resistance, Microbial / Q000235:genetics; D015180:Electrophoresis, Gel, Two-Dimensional; D004917:Erythromycin / Q000494:pharmacology; D005838:Genotype; D007700:Kinetics; D008561:Membrane Fusion; D009154:Mutation; D010455:Peptides / Q000494:pharmacology; D011523:Protoplasts / Q000502:physiology; D011995:Recombination, Genetic; D012269:Ribosomal Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D013302:Streptomyces / Q000187:drug effects / Q000235:genetics*; D013305:Streptomyces griseus / Q000235:genetics*; D014158:Transcription, Genetic
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; D012269:Ribosomal Proteins; C022076:thiopeptin; D004917:Erythromycin