Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1992 Aug;99(4):1362–1369. doi: 10.1104/pp.99.4.1362

Association of 70-Kilodalton Heat-Shock Cognate Proteins with Acclimation to Cold 1

Lisa G Neven 1,2,3, Dale W Haskell 1,2,3, Charles L Guy 1,2,3, Nancy Denslow 1,2,3, Paul A Klein 1,2,3, Linda G Green 1,2,3, Allison Silverman 1,2,3
PMCID: PMC1080633  PMID: 16669045

Abstract

Exposure of young spinach seedlings (Spinacia oleracea L. cv Bloomsdale) to 5°C leads to an increase in the synthesis of several 79-kilodalton proteins that are present in leaf tissue grown at 20°C. Protein sequence analyses and immunological cross-reactivity indicate that this group of proteins belongs to the 70-kilodalton heat-shock family. Steady-state transcript levels and protein synthesis are increased two- to threefold within 1 day, but immunoblot analyses suggest that the steady-state concentration of this protein group in leaf tissue only gradually accumulates at low temperature. It is proposed that the increased synthesis of several members of the 70-kilodalton heat-shock family could result from an influence of low temperature on protein folding and/or assembly processes.

Full text

PDF
1369

Images in this article

1364Figure 1
on p.1364
1365Figure 2
on p.1365
1366Figure 3
on p.1366
1366Figure 4
on p.1366
1367Figure 6
on p.1367

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. Beckmann R. P., Mizzen L. E., Welch W. J. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science. 1990 May 18;248(4957):850–854. doi: 10.1126/science.2188360. [DOI] [PubMed] [Google Scholar]
  3. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  4. Chirico W. J., Waters M. G., Blobel G. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature. 1988 Apr 28;332(6167):805–810. doi: 10.1038/332805a0. [DOI] [PubMed] [Google Scholar]
  5. Deshaies R. J., Koch B. D., Werner-Washburne M., Craig E. A., Schekman R. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature. 1988 Apr 28;332(6167):800–805. doi: 10.1038/332800a0. [DOI] [PubMed] [Google Scholar]
  6. Fontes E. B., Shank B. B., Wrobel R. L., Moose S. P., OBrian G. R., Wurtzel E. T., Boston R. S. Characterization of an immunoglobulin binding protein homolog in the maize floury-2 endosperm mutant. Plant Cell. 1991 May;3(5):483–496. doi: 10.1105/tpc.3.5.483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gaitanaris G. A., Papavassiliou A. G., Rubock P., Silverstein S. J., Gottesman M. E. Renaturation of denatured lambda repressor requires heat shock proteins. Cell. 1990 Jun 15;61(6):1013–1020. doi: 10.1016/0092-8674(90)90066-n. [DOI] [PubMed] [Google Scholar]
  8. Guy C. L., Haskell D. Detection of polypeptides associated with the cold acclimation process in spinach. Electrophoresis. 1988 Nov;9(11):787–796. doi: 10.1002/elps.1150091115. [DOI] [PubMed] [Google Scholar]
  9. Guy C. L., Haskell D. Induction of freezing tolerance in spinach is associated with the synthesis of cold acclimation induced proteins. Plant Physiol. 1987 Jul;84(3):872–878. doi: 10.1104/pp.84.3.872. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Guy C. L., Niemi K. J., Brambl R. Altered gene expression during cold acclimation of spinach. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3673–3677. doi: 10.1073/pnas.82.11.3673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hardy S. J., Randall L. L. A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB. Science. 1991 Jan 25;251(4992):439–443. doi: 10.1126/science.1989077. [DOI] [PubMed] [Google Scholar]
  12. Hemmingsen S. M., Woolford C., van der Vies S. M., Tilly K., Dennis D. T., Georgopoulos C. P., Hendrix R. W., Ellis R. J. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature. 1988 May 26;333(6171):330–334. doi: 10.1038/333330a0. [DOI] [PubMed] [Google Scholar]
  13. Ingolia T. D., Craig E. A. Drosophila gene related to the major heat shock-induced gene is transcribed at normal temperatures and not induced by heat shock. Proc Natl Acad Sci U S A. 1982 Jan;79(2):525–529. doi: 10.1073/pnas.79.2.525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Ingolia T. D., Craig E. A., McCarthy B. J. Sequence of three copies of the gene for the major Drosophila heat shock induced protein and their flanking regions. Cell. 1980 Oct;21(3):669–679. doi: 10.1016/0092-8674(80)90430-4. [DOI] [PubMed] [Google Scholar]
  15. Ingolia T. D., Slater M. R., Craig E. A. Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila. Mol Cell Biol. 1982 Nov;2(11):1388–1398. doi: 10.1128/mcb.2.11.1388. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mahboub S., Richard C., Delacourte A., Han K. K. Applications of chemical cleavage procedures to the peptide mapping of neurofilament triplet protein bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal Biochem. 1986 Apr;154(1):171–182. doi: 10.1016/0003-2697(86)90511-7. [DOI] [PubMed] [Google Scholar]
  17. Munro S., Pelham H. R. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell. 1986 Jul 18;46(2):291–300. doi: 10.1016/0092-8674(86)90746-4. [DOI] [PubMed] [Google Scholar]
  18. Neumann D., Nover L., Parthier B., Rieger R., Scharf K. D., Wollgiehn R., zur Nieden U. Heat shock and other stress response systems of plants. Results Probl Cell Differ. 1989;16:1–155. [PubMed] [Google Scholar]
  19. Normington K., Kohno K., Kozutsumi Y., Gething M. J., Sambrook J. S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell. 1989 Jun 30;57(7):1223–1236. doi: 10.1016/0092-8674(89)90059-7. [DOI] [PubMed] [Google Scholar]
  20. Rochester D. E., Winer J. A., Shah D. M. The structure and expression of maize genes encoding the major heat shock protein, hsp70. EMBO J. 1986 Mar;5(3):451–458. doi: 10.1002/j.1460-2075.1986.tb04233.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Rose M. D., Misra L. M., Vogel J. P. KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell. 1989 Jun 30;57(7):1211–1221. doi: 10.1016/0092-8674(89)90058-5. [DOI] [PubMed] [Google Scholar]
  22. Schaap A. P., Akhavan H., Romano L. J. Chemiluminescent substrates for alkaline phosphatase: application to ultrasensitive enzyme-linked immunoassays and DNA probes. Clin Chem. 1989 Sep;35(9):1863–1864. [PubMed] [Google Scholar]
  23. Slater M. R., Craig E. A. The SSB1 heat shock cognate gene of the yeast Saccharomyces cerevisiae. Nucleic Acids Res. 1989 Jun 26;17(12):4891–4891. doi: 10.1093/nar/17.12.4891. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Velazquez J. M., Sonoda S., Bugaisky G., Lindquist S. Is the major Drosophila heat shock protein present in cells that have not been heat shocked? J Cell Biol. 1983 Jan;96(1):286–290. doi: 10.1083/jcb.96.1.286. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Weiser C. J. Cold Resistance and Injury in Woody Plants: Knowledge of hardy plant adaptations to freezing stress may help us to reduce winter damage. Science. 1970 Sep 25;169(3952):1269–1278. doi: 10.1126/science.169.3952.1269. [DOI] [PubMed] [Google Scholar]
  26. Wu C. H., Caspar T., Browse J., Lindquist S., Somerville C. Characterization of an HSP70 Cognate Gene Family in Arabidopsis. Plant Physiol. 1988 Nov;88(3):731–740. doi: 10.1104/pp.88.3.731. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES