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. 1986 Oct;168(1):213–220. doi: 10.1128/jb.168.1.213-220.1986

Participation of the dnaK and dnaJ gene products in phosphorylation of glutaminyl-tRNA synthetase and threonyl-tRNA synthetase of Escherichia coli K-12.

M Wada, K Sekine, H Itikawa
PMCID: PMC213440  PMID: 3531168

Abstract

The heat shock proteins DnaK and DnaJ of Escherichia coli participate in phosphorylation of both glutaminyl-tRNA synthetase and threonyl-tRNA synthetase. When cellular proteins extracted from the dnaK7(Ts) and dnaJ259(Ts) mutant cells labeled with 32Pi at 42 degrees C were analyzed by two-dimensional gel electrophoresis, no phosphorylation of these proteins was observed when they were compared with those from wild-type cells.

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Selected References

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

  1. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  2. Clarke L., Carbon J. A colony bank containing synthetic Col El hybrid plasmids representative of the entire E. coli genome. Cell. 1976 Sep;9(1):91–99. doi: 10.1016/0092-8674(76)90055-6. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Enami M., Ishihama A. Protein phosphorylation in Escherichia coli and purification of a protein kinase. J Biol Chem. 1984 Jan 10;259(1):526–533. [PubMed] [Google Scholar]
  5. Gallant J. A. Stringent control in E. coli. Annu Rev Genet. 1979;13:393–415. doi: 10.1146/annurev.ge.13.120179.002141. [DOI] [PubMed] [Google Scholar]
  6. Garnak M., Reeves H. C. Phosphorylation of Isocitrate dehydrogenase of Escherichia coli. Science. 1979 Mar 16;203(4385):1111–1112. doi: 10.1126/science.34215. [DOI] [PubMed] [Google Scholar]
  7. Gerken S. C., Arfin S. M. Threonyl-tRNA synthetase from Chinese hamster ovary cells is phosphorylated on serine. J Biol Chem. 1984 Sep 25;259(18):11160–11161. [PubMed] [Google Scholar]
  8. Itikawa H., Ryu J. Isolation and characterization of a temperature-sensitive dnaK mutant of Escherichia coli B. J Bacteriol. 1979 May;138(2):339–344. doi: 10.1128/jb.138.2.339-344.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Iwakura Y., Ito K., Ishihama A. Biosynthesis of RNA polymerase in Escherichia coli. I. Control of RNA polymerase content at various growth rates. Mol Gen Genet. 1974;133(1):1–23. doi: 10.1007/BF00268673. [DOI] [PubMed] [Google Scholar]
  10. Krebs E. G., Beavo J. A. Phosphorylation-dephosphorylation of enzymes. Annu Rev Biochem. 1979;48:923–959. doi: 10.1146/annurev.bi.48.070179.004423. [DOI] [PubMed] [Google Scholar]
  11. LaPorte D. C., Koshland D. E., Jr A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle. Nature. 1982 Dec 2;300(5891):458–460. doi: 10.1038/300458a0. [DOI] [PubMed] [Google Scholar]
  12. LaPorte D. C., Thorsness P. E., Koshland D. E., Jr Compensatory phosphorylation of isocitrate dehydrogenase. A mechanism for adaptation to the intracellular environment. J Biol Chem. 1985 Sep 5;260(19):10563–10568. [PubMed] [Google Scholar]
  13. Li H. C., Brown G. G. Orthophosphate and histone dependent polyphosphate kinase from E. coli. Biochem Biophys Res Commun. 1973 Aug 6;53(3):875–881. doi: 10.1016/0006-291x(73)90174-5. [DOI] [PubMed] [Google Scholar]
  14. Manai M., Cozzone A. J. Analysis of the protein-kinase activity of Escherichia coli cells. Biochem Biophys Res Commun. 1979 Dec 14;91(3):819–826. doi: 10.1016/0006-291x(79)91953-3. [DOI] [PubMed] [Google Scholar]
  15. Neidhardt F. C. Roles of amino acid activating enzymes in cellular physiology. Bacteriol Rev. 1966 Dec;30(4):701–719. doi: 10.1128/br.30.4.701-719.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Neidhardt F. C., VanBogelen R. A., Vaughn V. The genetics and regulation of heat-shock proteins. Annu Rev Genet. 1984;18:295–329. doi: 10.1146/annurev.ge.18.120184.001455. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. 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]
  19. Pastan I., Adhya S. Cyclic adenosine 5'-monophosphate in Escherichia coli. Bacteriol Rev. 1976 Sep;40(3):527–551. doi: 10.1128/br.40.3.527-551.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Rahmsdorf H. J., Herrlich P., Pai S. H., Schweiger M., Wittmann H. G. Ribosomes after infection with bacteriophage T4 and T7. Mol Gen Genet. 1973 Dec 31;127(3):259–271. doi: 10.1007/BF00333766. [DOI] [PubMed] [Google Scholar]
  21. Roozen K. J., Fenwick R. G., Jr, Curtiss R., 3rd Synthesis of ribonucleic acid and protein in plasmid-containing minicells of Escherichia coli K-12. J Bacteriol. 1971 Jul;107(1):21–33. doi: 10.1128/jb.107.1.21-33.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Saito H., Uchida H. Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12. J Mol Biol. 1977 Jun 15;113(1):1–25. doi: 10.1016/0022-2836(77)90038-9. [DOI] [PubMed] [Google Scholar]
  23. Springer M., Plumbridge J. A., Butler J. S., Graffe M., Dondon J., Mayaux J. F., Fayat G., Lestienne P., Blanquet S., Grunberg-Manago M. Autogenous control of Escherichia coli threonyl-tRNA synthetase expression in vivo. J Mol Biol. 1985 Sep 5;185(1):93–104. doi: 10.1016/0022-2836(85)90185-8. [DOI] [PubMed] [Google Scholar]
  24. Wada M., Itikawa H. Participation of Escherichia coli K-12 groE gene products in the synthesis of cellular DNA and RNA. J Bacteriol. 1984 Feb;157(2):694–696. doi: 10.1128/jb.157.2.694-696.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Walsh K., Koshland D. E., Jr Branch point control by the phosphorylation state of isocitrate dehydrogenase. A quantitative examination of fluxes during a regulatory transition. J Biol Chem. 1985 Jul 15;260(14):8430–8437. [PubMed] [Google Scholar]
  26. Yamao F., Inokuchi H., Cheung A., Ozeki H., Söll D. Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene. J Biol Chem. 1982 Oct 10;257(19):11639–11643. [PubMed] [Google Scholar]
  27. Zylicz M., Georgopoulos C. Purification and properties of the Escherichia coli dnaK replication protein. J Biol Chem. 1984 Jul 25;259(14):8820–8825. [PubMed] [Google Scholar]
  28. Zylicz M., LeBowitz J. H., McMacken R., Georgopoulos C. The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system. Proc Natl Acad Sci U S A. 1983 Nov;80(21):6431–6435. doi: 10.1073/pnas.80.21.6431. [DOI] [PMC free article] [PubMed] [Google Scholar]

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