Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1987 Aug;84(15):5177–5181. doi: 10.1073/pnas.84.15.5177

Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli.

J C Bardwell, E A Craig
PMCID: PMC298817  PMID: 3299380

Abstract

We have isolated a gene from Escherichia coli homologous to the gene encoding the Mr 83,000 Drosophila heat shock protein (hsp83). In E. coli the protein homologous to hsp83 is a heat shock protein called C62.5. The predicted amino acid sequence of C62.5 is 41% and 42% identical to the Drosophila and human hsp83 proteins, respectively. Selected regions of the protein have conservation as high as 90%. The gene encoding C62.5 (named htpG) is located between the dnaZ and adk genes at 11.1 minutes on the E. coli chromosome. The htpG gene appears to be a newly identified locus. The isolation of an E. coli homologue of hsp83 illustrates the remarkable conservation of heat shock proteins in evolution and will facilitate genetic and biochemical experiments aimed at determining the function of hsp83.

Full text

PDF
5181

Images in this article

Selected References

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

  1. Bardwell J. C., Craig E. A. Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc Natl Acad Sci U S A. 1984 Feb;81(3):848–852. doi: 10.1073/pnas.81.3.848. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blackman R. K., Meselson M. Interspecific nucleotide sequence comparisons used to identify regulatory and structural features of the Drosophila hsp82 gene. J Mol Biol. 1986 Apr 20;188(4):499–515. doi: 10.1016/s0022-2836(86)80001-8. [DOI] [PubMed] [Google Scholar]
  3. Brugge J., Yonemoto W., Darrow D. Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex. Mol Cell Biol. 1983 Jan;3(1):9–19. doi: 10.1128/mcb.3.1.9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brune M., Schumann R., Wittinghofer F. Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia coli. Nucleic Acids Res. 1985 Oct 11;13(19):7139–7151. doi: 10.1093/nar/13.19.7139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Burns D. M., Beacham I. R. Nucleotide sequence and transcriptional analysis of the E. coli ushA gene, encoding periplasmic UDP-sugar hydrolase (5'-nucleotidase): regulation of the ushA gene, and the signal sequence of its encoded protein product. Nucleic Acids Res. 1986 May 27;14(10):4325–4342. doi: 10.1093/nar/14.10.4325. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cowing D. W., Bardwell J. C., Craig E. A., Woolford C., Hendrix R. W., Gross C. A. Consensus sequence for Escherichia coli heat shock gene promoters. Proc Natl Acad Sci U S A. 1985 May;82(9):2679–2683. doi: 10.1073/pnas.82.9.2679. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Craig E. A. The heat shock response. CRC Crit Rev Biochem. 1985;18(3):239–280. doi: 10.3109/10409238509085135. [DOI] [PubMed] [Google Scholar]
  8. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Doolittle R. F., Feng D. F., Johnson M. S., McClure M. A. Relationships of human protein sequences to those of other organisms. Cold Spring Harb Symp Quant Biol. 1986;51(Pt 1):447–455. doi: 10.1101/sqb.1986.051.01.054. [DOI] [PubMed] [Google Scholar]
  10. Farrelly F. W., Finkelstein D. B. Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae. J Biol Chem. 1984 May 10;259(9):5745–5751. [PubMed] [Google Scholar]
  11. Hershey H. V., Taylor M. W. Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes. Gene. 1986;43(3):287–293. doi: 10.1016/0378-1119(86)90218-0. [DOI] [PubMed] [Google Scholar]
  12. Hori H., Osawa S. Evolutionary change in 5S RNA secondary structure and a phylogenic tree of 54 5S RNA species. Proc Natl Acad Sci U S A. 1979 Jan;76(1):381–385. doi: 10.1073/pnas.76.1.381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hunt C., Morimoto R. I. Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6455–6459. doi: 10.1073/pnas.82.19.6455. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hübscher U., Kornberg A. The delta subunit of Escherichia coli DNA polymerase III holoenzyme is the dnaX gene product. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6284–6288. doi: 10.1073/pnas.76.12.6284. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kodaira M., Biswas S. B., Kornberg A. The dnaX gene encodes the DNA polymerase III holoenzyme tau subunit, precursor of the gamma subunit, the dnaZ gene product. Mol Gen Genet. 1983;192(1-2):80–86. doi: 10.1007/BF00327650. [DOI] [PubMed] [Google Scholar]
  16. Koyasu S., Nishida E., Kadowaki T., Matsuzaki F., Iida K., Harada F., Kasuga M., Sakai H., Yahara I. Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8054–8058. doi: 10.1073/pnas.83.21.8054. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Lai B. T., Chin N. W., Stanek A. E., Keh W., Lanks K. W. Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies. Mol Cell Biol. 1984 Dec;4(12):2802–2810. doi: 10.1128/mcb.4.12.2802. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lanks K. W., Kasambalides E. J. Purification and characterization of a major component from the cytoplasmic matrix of cultured murine L cells. Biochim Biophys Acta. 1979 May 23;578(1):1–12. doi: 10.1016/0005-2795(79)90106-5. [DOI] [PubMed] [Google Scholar]
  19. Lindquist S. The heat-shock response. Annu Rev Biochem. 1986;55:1151–1191. doi: 10.1146/annurev.bi.55.070186.005443. [DOI] [PubMed] [Google Scholar]
  20. Lloyd R. G., Buckman C. Identification and genetic analysis of sbcC mutations in commonly used recBC sbcB strains of Escherichia coli K-12. J Bacteriol. 1985 Nov;164(2):836–844. doi: 10.1128/jb.164.2.836-844.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Nagata S., Nagashima K., Tsunetsugu-Yokota Y., Fujimura K., Miyazaki M., Kaziro Y. Polypeptide chain elongation factor 1 alpha (EF-1 alpha) from yeast: nucleotide sequence of one of the two genes for EF-1 alpha from Saccharomyces cerevisiae. EMBO J. 1984 Aug;3(8):1825–1830. doi: 10.1002/j.1460-2075.1984.tb02053.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Nagata S., Tsunetsugu-Yokota Y., Naito A., Kaziro Y. Molecular cloning and sequence determination of the nuclear gene coding for mitochondrial elongation factor Tu of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1983 Oct;80(20):6192–6196. doi: 10.1073/pnas.80.20.6192. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Neidhardt F. C., VanBogelen R. A., Lau E. T. Molecular cloning and expression of a gene that controls the high-temperature regulon of Escherichia coli. J Bacteriol. 1983 Feb;153(2):597–603. doi: 10.1128/jb.153.2.597-603.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. 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]
  25. 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]
  26. 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]
  27. Sanchez E. R., Toft D. O., Schlesinger M. J., Pratt W. B. Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J Biol Chem. 1985 Oct 15;260(23):12398–12401. [PubMed] [Google Scholar]
  28. Schuh S., Yonemoto W., Brugge J., Bauer V. J., Riehl R. M., Sullivan W. P., Toft D. O. A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src. J Biol Chem. 1985 Nov 15;260(26):14292–14296. [PubMed] [Google Scholar]
  29. Vieira J., Messing J. The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene. 1982 Oct;19(3):259–268. doi: 10.1016/0378-1119(82)90015-4. [DOI] [PubMed] [Google Scholar]
  30. Winans S. C., Elledge S. J., Krueger J. H., Walker G. C. Site-directed insertion and deletion mutagenesis with cloned fragments in Escherichia coli. J Bacteriol. 1985 Mar;161(3):1219–1221. doi: 10.1128/jb.161.3.1219-1221.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Yin K. C., Blinkowa A., Walker J. R. Nucleotide sequence of the Escherichia coli replication gene dnaZX. Nucleic Acids Res. 1986 Aug 26;14(16):6541–6549. doi: 10.1093/nar/14.16.6541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Zurawski G., Clegg M. T. The barley chloroplast DNA atpBE, trnM2, and trnV1 loci. Nucleic Acids Res. 1984 Mar 12;12(5):2549–2559. doi: 10.1093/nar/12.5.2549. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES