Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1986 Jan;165(1):193–197. doi: 10.1128/jb.165.1.193-197.1986

Isolation and characterization of lon mutants in Salmonella typhimurium.

D Downs, L Waxman, A L Goldberg, J Roth
PMCID: PMC214388  PMID: 3001022

Abstract

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.

Full text

PDF
194

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Apte B. N., Rhodes H., Zipser D. Mutation blocking the specific degradation of reinitiation polypeptides in E. coli. Nature. 1975 Sep 25;257(5524):329–331. doi: 10.1038/257329a0. [DOI] [PubMed] [Google Scholar]
  2. Bachmann B. J., Low K. B. Linkage map of Escherichia coli K-12, edition 6. Microbiol Rev. 1980 Mar;44(1):1–56. doi: 10.1128/mr.44.1.1-56.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bukhari A. I., Zipser D. Mutants of Escherichia coli with a defect in the degradation of nonsense fragments. Nat New Biol. 1973 Jun 20;243(129):238–241. doi: 10.1038/newbio243238a0. [DOI] [PubMed] [Google Scholar]
  4. Chan R. K., Botstein D., Watanabe T., Ogata Y. Specialized transduction of tetracycline resistance by phage P22 in Salmonella typhimurium. II. Properties of a high-frequency-transducing lysate. Virology. 1972 Dec;50(3):883–898. doi: 10.1016/0042-6822(72)90442-4. [DOI] [PubMed] [Google Scholar]
  5. Charette M. F., Henderson G. W., Markovitz A. ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4728–4732. doi: 10.1073/pnas.78.8.4728. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cheung W. Y. Calmodulin plays a pivotal role in cellular regulation. Science. 1980 Jan 4;207(4426):19–27. doi: 10.1126/science.6243188. [DOI] [PubMed] [Google Scholar]
  7. Chung C. H., Goldberg A. L. The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4931–4935. doi: 10.1073/pnas.78.8.4931. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Chung C. H., Waxman L., Goldberg A. L. Studies of the protein encoded by the lon mutation, capR9, in Escherichia coli. A labile form of the ATP-dependent protease La that inhibits the wild type protease. J Biol Chem. 1983 Jan 10;258(1):215–221. [PubMed] [Google Scholar]
  9. George J., Castellazzi M., Buttin G. Prophage induction and cell division in E. coli. III. Mutations sfiA and sfiB restore division in tif and lon strains and permit the expression of mutator properties of tif. Mol Gen Genet. 1975 Oct 22;140(4):309–332. [PubMed] [Google Scholar]
  10. Goldberg A. L. Degradation of abnormal proteins in Escherichia coli (protein breakdown-protein structure-mistranslation-amino acid analogs-puromycin). Proc Natl Acad Sci U S A. 1972 Feb;69(2):422–426. doi: 10.1073/pnas.69.2.422. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Goldberg A. L., Waxman L. The role of ATP hydrolysis in the breakdown of proteins and peptides by protease La from Escherichia coli. J Biol Chem. 1985 Oct 5;260(22):12029–12034. [PubMed] [Google Scholar]
  12. Gottesman S., Gottesman M., Shaw J. E., Pearson M. L. Protein degradation in E. coli: the lon mutation and bacteriophage lambda N and cII protein stability. Cell. 1981 Apr;24(1):225–233. doi: 10.1016/0092-8674(81)90518-3. [DOI] [PubMed] [Google Scholar]
  13. Gottesman S., Zipser D. Deg phenotype of Escherichia coli lon mutants. J Bacteriol. 1978 Feb;133(2):844–851. doi: 10.1128/jb.133.2.844-851.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Grossman A. D., Burgess R. R., Walter W., Gross C. A. Mutations in the Ion gene of E. coli K12 phenotypically suppress a mutation in the sigma subunit of RNA polymerase. Cell. 1983 Jan;32(1):151–159. doi: 10.1016/0092-8674(83)90505-6. [DOI] [PubMed] [Google Scholar]
  15. HOWARD-FLANDERS P., SIMSON E., THERIOT L. A LOCUS THAT CONTROLS FILAMENT FORMATION AND SENSITIVITY TO RADIATION IN ESCHERICHIA COLI K-12. Genetics. 1964 Feb;49:237–246. doi: 10.1093/genetics/49.2.237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Huisman O., D'Ari R., George J. Further characterization of sfiA and sfiB mutations in Escherichia coli. J Bacteriol. 1980 Oct;144(1):185–191. doi: 10.1128/jb.144.1.185-191.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Kaibuchi K., Sano K., Hoshijima M., Takai Y., Nishizuka Y. Phosphatidylinositol turnover in platelet activation; calcium mobilization and protein phosphorylation. Cell Calcium. 1982 Oct;3(4-5):323–335. doi: 10.1016/0143-4160(82)90020-3. [DOI] [PubMed] [Google Scholar]
  18. Kleckner N., Roth J., Botstein D. Genetic engineering in vivo using translocatable drug-resistance elements. New methods in bacterial genetics. J Mol Biol. 1977 Oct 15;116(1):125–159. doi: 10.1016/0022-2836(77)90123-1. [DOI] [PubMed] [Google Scholar]
  19. Kowit J. D., Goldberg A. L. Intermediate steps in the degradation of a specific abnormal protein in Escherichia coli. J Biol Chem. 1977 Dec 10;252(23):8350–8357. [PubMed] [Google Scholar]
  20. Larimore F. S., Waxman L., Goldberg A. L. Studies of the ATP-dependent proteolytic enzyme, protease La, from Escherichia coli. J Biol Chem. 1982 Apr 25;257(8):4187–4195. [PubMed] [Google Scholar]
  21. Mizusawa S., Gottesman S. Protein degradation in Escherichia coli: the lon gene controls the stability of sulA protein. Proc Natl Acad Sci U S A. 1983 Jan;80(2):358–362. doi: 10.1073/pnas.80.2.358. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Molnár J., Holland I. B., Mándi Y. Selection of ion mutants in Escherichia coli by treatment with phenothiazines. Genet Res. 1977 Aug;30(1):13–20. doi: 10.1017/s0016672300017420. [DOI] [PubMed] [Google Scholar]
  23. Radke K. L., Siegel E. C. Mutation preventing capsular polysaccharide synthesis in Escherichia coli K-12 and its effect on bacteriophage resistance. J Bacteriol. 1971 May;106(2):432–437. doi: 10.1128/jb.106.2.432-437.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Ratzkin B., Roth J. Cluster of genes controlling proline degradation in Salmonella typhimurium. J Bacteriol. 1978 Feb;133(2):744–754. doi: 10.1128/jb.133.2.744-754.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Sanderson K. E., Roth J. R. Linkage map of Salmonella typhimurium, Edition VI. Microbiol Rev. 1983 Sep;47(3):410–453. doi: 10.1128/mr.47.3.410-453.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Trisler P., Gottesman S. lon transcriptional regulation of genes necessary for capsular polysaccharide synthesis in Escherichia coli K-12. J Bacteriol. 1984 Oct;160(1):184–191. doi: 10.1128/jb.160.1.184-191.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  28. WULFF D. L. THE ROLE OF THYMINE DIMER IN THE PHOTO-INACTIVATION OF THE BACTERIOPHAGE T4V1. J Mol Biol. 1963 Oct;7:431–441. doi: 10.1016/s0022-2836(63)80035-2. [DOI] [PubMed] [Google Scholar]
  29. Waxman L., Goldberg A. L. Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion. Proc Natl Acad Sci U S A. 1982 Aug;79(16):4883–4887. doi: 10.1073/pnas.79.16.4883. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Waxman L., Goldberg A. L. Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction. J Biol Chem. 1985 Oct 5;260(22):12022–12028. [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES