Isolation and characterization of lon mutants in Salmonella typhimurium.
In this paper we report the isolation and characterization of lon mutants in Salmonella typhimurium. The mutants were isolated by using positive selection by chlorpromazine resistance. The physiological and biochemical properties of the lon mutants in S. typhimurium are very similar to those of Escherichia coli lon mutants. Mutants altered at this locus contain little or no activity of the ATP-dependent protease La and show a number of pleiotropic phenotypes, including increased production of capsular polysaccharides, increased sensitivity to UV light and other DNA-damaging agents, and a decreased ability to degrade abnormal proteins.
D049069:ATP-Dependent Proteases; D004251:DNA Transposable Elements; D010450:Endopeptidases / Q000032:analysis / Q000235:genetics*; D029968:Escherichia coli Proteins; D005816:Genetic Complementation Test; D006360:Heat-Shock Proteins; D009154:Mutation; D049070:Protease La; D011691:Puromycin / Q000378:metabolism; D012486:Salmonella typhimurium / Q000201:enzymology* / Q000235:genetics / Q000528:radiation effects; D012697:Serine Endopeptidases; D014466:Ultraviolet Rays
D004251:DNA Transposable Elements; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D011691:Puromycin; D010450:Endopeptidases; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La