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. 1984 Jul;159(1):283–287. doi: 10.1128/jb.159.1.283-287.1984

lon gene product of Escherichia coli is a heat-shock protein.

T A Phillips, R A VanBogelen, F C Neidhardt
PMCID: PMC215626  PMID: 6330035

Abstract

The product of the pleiotropic gene lon is a protein with protease activity and has been tentatively identified as protein H94.0 on the reference two-dimensional gel of Escherichia coli proteins. Purified Lon protease migrated with the prominent cellular protein H94.0 in E. coli K-12 strains. Peptide map patterns of Lon protease and H94.0 were identical. A mutant form of the protease had altered mobility during gel electrophoresis. An E. coli B/r strain that is known to be defective in Lon function contained no detectable H94.0 protein under normal growth conditions. Upon a shift to 42 degrees C, however, the Lon protease was induced to high levels in K-12 strains and a small amount of protein became detectable at the H94.0 location in strain B/r. Heat induction of Lon protease was dependent on the normal allele of the regulatory gene, htpR, establishing lon as a member of the high-temperature-production regulon of E. coli.

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Selected References

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  1. ADLER H. I., HARDIGREE A. A. ANALYSIS OF A GENE CONTROLLING CELL DIVISION AND SENSITIVITY TO RADIATION IN ESCHERICHIA COLI. J Bacteriol. 1964 Mar;87:720–726. doi: 10.1128/jb.87.3.720-726.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bachmann B. J. Linkage map of Escherichia coli K-12, edition 7. Microbiol Rev. 1983 Jun;47(2):180–230. doi: 10.1128/mr.47.2.180-230.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bloch P. L., Phillips T. A., Neidhardt F. C. Protein identifications of O'Farrell two-dimensional gels: locations of 81 Escherichia coli proteins. J Bacteriol. 1980 Mar;141(3):1409–1420. doi: 10.1128/jb.141.3.1409-1420.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blumenthal R. M., Reeh S., Pedersen S. Regulation of transcription factor rho and the alpha subunit of RNA polymerase in Escherichia coli B/r. Proc Natl Acad Sci U S A. 1976 Jul;73(7):2285–2288. doi: 10.1073/pnas.73.7.2285. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Buchanan C. E., Hua S. S., Avni H., Markovitz A. Transcriptional control of the calactose operon by the capR (lon) and capT genes. J Bacteriol. 1973 May;114(2):891–893. doi: 10.1128/jb.114.2.891-893.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  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. Cleveland D. W., Fischer S. G., Kirschner M. W., Laemmli U. K. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem. 1977 Feb 10;252(3):1102–1106. [PubMed] [Google Scholar]
  9. Donch J., Chung Y. S., Greenberg J. Locus for radiation resistance in Escherichia coli strain B-r. Genetics. 1969 Feb;61(2):363–370. doi: 10.1093/genetics/61.2.363. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Donch J., Greenberg J. Ultraviolet sensitivity gene of Escherichia coli B. J Bacteriol. 1968 May;95(5):1555–1559. doi: 10.1128/jb.95.5.1555-1559.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. Georgopoulos C., Tilly K., Drahos D., Hendrix R. The B66.0 protein of Escherichia coli is the product of the dnaK+ gene. J Bacteriol. 1982 Mar;149(3):1175–1177. doi: 10.1128/jb.149.3.1175-1177.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. 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]
  14. 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]
  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. Hightower L. E. Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides. J Cell Physiol. 1980 Mar;102(3):407–427. doi: 10.1002/jcp.1041020315. [DOI] [PubMed] [Google Scholar]
  17. Hua S. S., Markovitz A. Multiple regulator gene control of the galactose operon in Escherichia coli K-12. J Bacteriol. 1972 Jun;110(3):1089–1099. doi: 10.1128/jb.110.3.1089-1099.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Huisman O., D'Ari R. An inducible DNA replication-cell division coupling mechanism in E. coli. Nature. 1981 Apr 30;290(5809):797–799. doi: 10.1038/290797a0. [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. Krueger J. H., Walker G. C. groEL and dnaK genes of Escherichia coli are induced by UV irradiation and nalidixic acid in an htpR+-dependent fashion. Proc Natl Acad Sci U S A. 1984 Mar;81(5):1499–1503. doi: 10.1073/pnas.81.5.1499. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. 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]
  22. Lemaux P. G., Herendeen S. L., Bloch P. L., Neidhardt F. C. Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts. Cell. 1978 Mar;13(3):427–434. doi: 10.1016/0092-8674(78)90317-3. [DOI] [PubMed] [Google Scholar]
  23. MARKOVITZ A. REGULATORY MECHANISMS FOR SYNTHESIS OF CAPSULAR POLYSACCHARIDE IN MUCOID MUTANTS OF ESCHERICHIA COLI K12. Proc Natl Acad Sci U S A. 1964 Feb;51:239–246. doi: 10.1073/pnas.51.2.239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Mackie G., Wilson D. B. Regulation of the gal operon of Escherichia coli by the capR gene. J Biol Chem. 1972 May 25;247(10):2973–2978. [PubMed] [Google Scholar]
  25. 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]
  26. Neidhardt F. C., Bloch P. L., Pedersen S., Reeh S. Chemical measurement of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli. J Bacteriol. 1977 Jan;129(1):378–387. doi: 10.1128/jb.129.1.378-387.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Neidhardt F. C., Bloch P. L., Smith D. F. Culture medium for enterobacteria. J Bacteriol. 1974 Sep;119(3):736–747. doi: 10.1128/jb.119.3.736-747.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Neidhardt F. C., Phillips T. A., VanBogelen R. A., Smith M. W., Georgalis Y., Subramanian A. R. Identity of the B56.5 protein, the A-protein, and the groE gene product of Escherichia coli. J Bacteriol. 1981 Jan;145(1):513–520. doi: 10.1128/jb.145.1.513-520.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Neidhardt F. C., VanBogelen R. A. Positive regulatory gene for temperature-controlled proteins in Escherichia coli. Biochem Biophys Res Commun. 1981 May 29;100(2):894–900. doi: 10.1016/s0006-291x(81)80257-4. [DOI] [PubMed] [Google Scholar]
  30. Neidhardt F. C., Vaughn V., Phillips T. A., Bloch P. L. Gene-protein index of Escherichia coli K-12. Microbiol Rev. 1983 Jun;47(2):231–284. doi: 10.1128/mr.47.2.231-284.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  32. Phillips T. A., Bloch P. L., Neidhardt F. C. Protein identifications on O'Farrell two-dimensional gels: locations of 55 additional Escherichia coli proteins. J Bacteriol. 1980 Dec;144(3):1024–1033. doi: 10.1128/jb.144.3.1024-1033.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Saito H., Uchida H. Organization and expression of the dnaJ and dnaK genes of Escherichia coli K12. Mol Gen Genet. 1978 Aug 4;164(1):1–8. doi: 10.1007/BF00267592. [DOI] [PubMed] [Google Scholar]
  34. Schoemaker J. M., Henderson G. W., Markovitz A. Escherichia coli polypeptide controlled by the lon (capR) ATP hydrolysis-dependent protease and possibly involved in cell division. J Bacteriol. 1982 Nov;152(2):919–923. doi: 10.1128/jb.152.2.919-923.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Schoemaker J. M., Markovitz A. Identification of the gene lon (capR) product as a 94-kilodalton polypeptide by cloning and deletion analysis. J Bacteriol. 1981 Jul;147(1):46–56. doi: 10.1128/jb.147.1.46-56.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Shineberg B., Zipser D. The ion gene and degradation of beta-galactosidase nonsense fragments. J Bacteriol. 1973 Dec;116(3):1469–1471. doi: 10.1128/jb.116.3.1469-1471.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Takano T. Bacterial mutants defective in plasmid formation: requirement for the lon + allele. Proc Natl Acad Sci U S A. 1971 Jul;68(7):1469–1473. doi: 10.1073/pnas.68.7.1469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Tilly K., VanBogelen R. A., Georgopoulos C., Neidhardt F. C. Identification of the heat-inducible protein C15.4 as the groES gene product in Escherichia coli. J Bacteriol. 1983 Jun;154(3):1505–1507. doi: 10.1128/jb.154.3.1505-1507.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. VanBogelen R. A., Vaughn V., Neidhardt F. C. Gene for heat-inducible lysyl-tRNA synthetase (lysU) maps near cadA in Escherichia coli. J Bacteriol. 1983 Feb;153(2):1066–1068. doi: 10.1128/jb.153.2.1066-1068.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Walker J. R., Ussery C. L., Allen J. S. Bacterial cell division regulation: lysogenization of conditional cell division lon - mutants of Escherichia coli by bacteriophage. J Bacteriol. 1973 Mar;113(3):1326–1332. doi: 10.1128/jb.113.3.1326-1332.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Wanner B. L., Kodaira R., Neidhardt F. C. Physiological regulation of a decontrolled lac operon. J Bacteriol. 1977 Apr;130(1):212–222. doi: 10.1128/jb.130.1.212-222.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Yamamori T., Yura T. Genetic control of heat-shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K-12. Proc Natl Acad Sci U S A. 1982 Feb;79(3):860–864. doi: 10.1073/pnas.79.3.860. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Yochem J., Uchida H., Sunshine M., Saito H., Georgopoulos C. P., Feiss M. Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication. Mol Gen Genet. 1978 Aug 4;164(1):9–14. doi: 10.1007/BF00267593. [DOI] [PubMed] [Google Scholar]
  44. Zehnbauer B. A., Foley E. C., Henderson G. W., Markovitz A. Identification and purification of the Lon+ (capR+) gene product, a DNA-binding protein. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2043–2047. doi: 10.1073/pnas.78.4.2043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Zehnbauer B. A., Markovitz A. Cloning of gene lon (capR) of Escherichia coli K-12 and identification of polypeptides specified by the cloned deoxyribonucleic acid fragment. J Bacteriol. 1980 Aug;143(2):852–863. doi: 10.1128/jb.143.2.852-863.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]

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