Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1989 Oct;91(2):552–558. doi: 10.1104/pp.91.2.552

The Heat Shock Response of Carrot 1

Protein Variations between Cultured Cell Lines

Cheol Ho Hwang 1, J Lynn Zimmerman 1
PMCID: PMC1062036  PMID: 16667068

Abstract

We have defined several parameters surrounding the heat shock response of cultured cells of carrot (Daucus carota L.) and have found that these cells exhibit a typical “higher plant” heat shock response. In particular, the resolution of the heat shock proteins (hsps) by two-dimensional polyacrylamide gel electrophoresis (PAGE) has revealed a pattern of proteins very similar to the hsps from soybean; specifically, the low molecular weight class is composed of approximately 15 to 20 different polypeptides which likely represent different members of a small gene family. In addition, we have compared the (2-D) PAGE profiles of hsps isolated from several different cultured cell lines currently maintained in our laboratory and have found notable differences in the low molecular weight hsps between cell lines. Some of the differences appear to be quantitative, while others may be qualitative. Each of the cell lines was derived from a different seedling of the same seed stock of the same cultivar; thus, genetic differences should be minimized. In addition, two of the cell lines, which show clear differences, were initially derived from a single parental line, and thus arose from a single genetic stock. Possible explanations for the cell line differences observed here are either partial aneuploidy or modified gene regulation resulting from molecular changes during the time in culture (i.e. somaclonal variation). These observations serve to highlight the potential for variation that exists in cells in culture even for such a highly conserved response and gene set as the heat shock genes.

Full text

PDF
552

Images in this article

553Figure 1
on p.553
554Figure 2
on p.554
555Figure 3
on p.555

Selected References

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

  1. Burke J. J., Hatfield J. L., Klein R. R., Mullet J. E. Accumulation of heat shock proteins in field-grown cotton. Plant Physiol. 1985 Jun;78(2):394–398. doi: 10.1104/pp.78.2.394. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cooper P., Ho T. H. Heat shock proteins in maize. Plant Physiol. 1983 Feb;71(2):215–222. doi: 10.1104/pp.71.2.215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ireland R. C., Berger E. M. Synthesis of low molecular weight heat shock peptides stimulated by ecdysterone in a cultured Drosophila cell line. Proc Natl Acad Sci U S A. 1982 Feb;79(3):855–859. doi: 10.1073/pnas.79.3.855. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Kanabus J., Pikaard C. S., Cherry J. H. Heat Shock Proteins in Tobacco Cell Suspension during Growth Cycle. Plant Physiol. 1984 Jul;75(3):639–644. doi: 10.1104/pp.75.3.639. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Key J. L., Lin C. Y., Chen Y. M. Heat shock proteins of higher plants. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3526–3530. doi: 10.1073/pnas.78.6.3526. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  7. Lin C. Y., Roberts J. K., Key J. L. Acquisition of Thermotolerance in Soybean Seedlings : Synthesis and Accumulation of Heat Shock Proteins and their Cellular Localization. Plant Physiol. 1984 Jan;74(1):152–160. doi: 10.1104/pp.74.1.152. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Mansfield M. A., Key J. L. Synthesis of the low molecular weight heat shock proteins in plants. Plant Physiol. 1987 Aug;84(4):1007–1017. doi: 10.1104/pp.84.4.1007. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Nagao R. T., Czarnecka E., Gurley W. B., Schöffl F., Key J. L. Genes for low-molecular-weight heat shock proteins of soybeans: sequence analysis of a multigene family. Mol Cell Biol. 1985 Dec;5(12):3417–3428. doi: 10.1128/mcb.5.12.3417. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. Schneider R., Gander I., Müller U., Mertz R., Winnacker E. L. A sensitive and rapid gel retention assay for nuclear factor I and other DNA-binding proteins in crude nuclear extracts. Nucleic Acids Res. 1986 Feb 11;14(3):1303–1317. doi: 10.1093/nar/14.3.1303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Schöffl F., Key J. L. An analysis of mRNAs for a group of heat shock proteins of soybean using cloned cDNAs. J Mol Appl Genet. 1982;1(4):301–314. [PubMed] [Google Scholar]
  13. Sirotkin K., Davidson N. Developmentally regulated transcription from Drosophila melanogaster chromosomal site 67B. Dev Biol. 1982 Jan;89(1):196–210. doi: 10.1016/0012-1606(82)90307-4. [DOI] [PubMed] [Google Scholar]
  14. Zimmerman J. L., Petri W., Meselson M. Accumulation of a specific subset of D. melanogaster heat shock mRNAs in normal development without heat shock. Cell. 1983 Apr;32(4):1161–1170. doi: 10.1016/0092-8674(83)90299-4. [DOI] [PubMed] [Google Scholar]

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

RESOURCES