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. 1987 Mar;169(3):1102–1106. doi: 10.1128/jb.169.3.1102-1106.1987

Genetic suppression of a temperature-sensitive groES mutation by an altered subunit of RNA polymerase of Escherichia coli K-12.

M Wada, H Fujita, H Itikawa
PMCID: PMC211906  PMID: 3546264

Abstract

Temperature-resistant suppressor mutants were isolated from Escherichia coli mutant strain groES131(Ts). Phage P1-mediated transduction and a two-dimensional gel electrophoretic analysis of cellular proteins indicated that these suppressor mutants carry an additional mutation in either the groEL gene or the rpoA gene.

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Selected References

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  1. 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]
  2. Bagdasarian M. M., Izakowska M., Bagdasarian M. Suppression of the DnaA phenotype by mutations in the rpoB cistron of ribonucleic acid polymerase in Salmonella typhimurium and Escherichia coli. J Bacteriol. 1977 May;130(2):577–582. doi: 10.1128/jb.130.2.577-582.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bochner B. R., Ames B. N. Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography. J Biol Chem. 1982 Aug 25;257(16):9759–9769. [PubMed] [Google Scholar]
  4. 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]
  5. Chandrasekhar G. N., Tilly K., Woolford C., Hendrix R., Georgopoulos C. Purification and properties of the groES morphogenetic protein of Escherichia coli. J Biol Chem. 1986 Sep 15;261(26):12414–12419. [PubMed] [Google Scholar]
  6. 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]
  7. Fayet O., Louarn J. M., Georgopoulos C. Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes. Mol Gen Genet. 1986 Mar;202(3):435–445. doi: 10.1007/BF00333274. [DOI] [PubMed] [Google Scholar]
  8. Friedman D. I., Olson E. R., Georgopoulos C., Tilly K., Herskowitz I., Banuett F. Interactions of bacteriophage and host macromolecules in the growth of bacteriophage lambda. Microbiol Rev. 1984 Dec;48(4):299–325. doi: 10.1128/mr.48.4.299-325.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Georgopoulos C. P., Hendrix R. W., Casjens S. R., Kaiser A. D. Host participation in bacteriophage lambda head assembly. J Mol Biol. 1973 May 5;76(1):45–60. doi: 10.1016/0022-2836(73)90080-6. [DOI] [PubMed] [Google Scholar]
  10. Ishihama A., Ikeuchi T., Yura T. A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia coli. I. Copurification and separation. J Biochem. 1976 May;79(5):917–925. doi: 10.1093/oxfordjournals.jbchem.a131159. [DOI] [PubMed] [Google Scholar]
  11. Itikawa H., Fujita H., Wada M. High temperature induction of a stringent response in the dnaK(Ts) and dnaJ(Ts) mutants of Escherichia coli. J Biochem. 1986 Jun;99(6):1719–1724. doi: 10.1093/oxfordjournals.jbchem.a135648. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Jenkins A. J., March J. B., Oliver I. R., Masters M. A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene. Mol Gen Genet. 1986 Mar;202(3):446–454. doi: 10.1007/BF00333275. [DOI] [PubMed] [Google Scholar]
  14. LENNOX E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology. 1955 Jul;1(2):190–206. doi: 10.1016/0042-6822(55)90016-7. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. Sunshine M., Feiss M., Stuart J., Yochem J. A new host gene (groPC) necessary for lambda DNA replication. Mol Gen Genet. 1977 Feb 28;151(1):27–34. doi: 10.1007/BF00446909. [DOI] [PubMed] [Google Scholar]
  20. Takano T., Kakefuda T. Involvement of a bacterial factor in morphogenesis of bacteriophage capsid. Nat New Biol. 1972 Sep 13;239(89):34–37. doi: 10.1038/newbio239034a0. [DOI] [PubMed] [Google Scholar]
  21. Tilly K., Georgopoulos C. Evidence that the two Escherichia coli groE morphogenetic gene products interact in vivo. J Bacteriol. 1982 Mar;149(3):1082–1088. doi: 10.1128/jb.149.3.1082-1088.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Tilly K., Murialdo H., Georgopoulos C. Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1629–1633. doi: 10.1073/pnas.78.3.1629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Wada M., Sekine K., Itikawa H. Participation of the dnaK and dnaJ gene products in phosphorylation of glutaminyl-tRNA synthetase and threonyl-tRNA synthetase of Escherichia coli K-12. J Bacteriol. 1986 Oct;168(1):213–220. doi: 10.1128/jb.168.1.213-220.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Walker G. C. Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli. Microbiol Rev. 1984 Mar;48(1):60–93. doi: 10.1128/mr.48.1.60-93.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Yamamori T., Ito K., Nakamura Y., Yura T. Transient regulation of protein synthesis in Escherichia coli upon shift-up of growth temperature. J Bacteriol. 1978 Jun;134(3):1133–1140. doi: 10.1128/jb.134.3.1133-1140.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Zweig M., Cummings D. J. Cleavage of head and tail proteins during bacteriophage T5 assembly: selective host involvement in the cleavage of a tail protein. J Mol Biol. 1973 Nov 5;80(3):505–518. doi: 10.1016/0022-2836(73)90418-x. [DOI] [PubMed] [Google Scholar]
  28. van der Ende A., Baker T. A., Ogawa T., Kornberg A. Initiation of enzymatic replication at the origin of the Escherichia coli chromosome: primase as the sole priming enzyme. Proc Natl Acad Sci U S A. 1985 Jun;82(12):3954–3958. doi: 10.1073/pnas.82.12.3954. [DOI] [PMC free article] [PubMed] [Google Scholar]

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