Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1990 Dec;94(4):1689–1695. doi: 10.1104/pp.94.4.1689

Sequence and Expression of a HSP83 from Arabidopsis thaliana1

Timothy W Conner 1,2, Peter R LaFayette 1, Ronald T Nagao 1, Joe L Key 1
PMCID: PMC1077439  PMID: 16667903

Abstract

A full-length cDNA encoding a heat shock protein (hsp) belonging to the 83 to 90 kilodalton hsp family of Arabidopsis thaliana has been isolated and sequenced. Truncated cDNA clones were isolated by nucleic acid hybridization to a truncated soybean HSP83 cDNA probe and a fragment generated from a Drosophila HSP83 gene. A single strand DNA vector/primer based extension procedure was employed to obtain the full-length cDNA. The level of transcripts homologous to this cDNA (AtHS83) is low in 2-week-old Arabidopsis plants but is rapidly enhanced by elevated temperatures. DNA sequence comparison between this cDNA and hsp83-90 sequences from human, yeast and Drosophila reveal amino acid identities of 63 to 69%, typical identities for interspecies comparisons between hsp83 to 90 kilodalton proteins. Genomic DNA blot analysis performed with probes derived from AtHS83 indicate the presence of a HSP83 gene family estimated to be comprised of at least three genes.

Full text

PDF
1692

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. Ancient heat shock gene is dispensable. J Bacteriol. 1988 Jul;170(7):2977–2983. doi: 10.1128/jb.170.7.2977-2983.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bardwell J. C., Craig E. A. Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5177–5181. doi: 10.1073/pnas.84.15.5177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. Borkovich K. A., Farrelly F. W., Finkelstein D. B., Taulien J., Lindquist S. hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol. 1989 Sep;9(9):3919–3930. doi: 10.1128/mcb.9.9.3919. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chirala S. S., Kasturi R., Pazirandeh M., Stolow D. T., Huang W. Y., Wakil S. J. A novel cDNA extension procedure. Isolation of chicken fatty acid synthase cDNA clones. J Biol Chem. 1989 Mar 5;264(7):3750–3757. [PubMed] [Google Scholar]
  6. Dale R. M., McClure B. A., Houchins J. P. A rapid single-stranded cloning strategy for producing a sequential series of overlapping clones for use in DNA sequencing: application to sequencing the corn mitochondrial 18 S rDNA. Plasmid. 1985 Jan;13(1):31–40. doi: 10.1016/0147-619x(85)90053-8. [DOI] [PubMed] [Google Scholar]
  7. Dragon E. A., Sias S. R., Kato E. A., Gabe J. D. The genome of Trypanosoma cruzi contains a constitutively expressed, tandemly arranged multicopy gene homologous to a major heat shock protein. Mol Cell Biol. 1987 Mar;7(3):1271–1275. doi: 10.1128/mcb.7.3.1271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
  10. Gamborg O. L., Miller R. A., Ojima K. Nutrient requirements of suspension cultures of soybean root cells. Exp Cell Res. 1968 Apr;50(1):151–158. doi: 10.1016/0014-4827(68)90403-5. [DOI] [PubMed] [Google Scholar]
  11. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  12. Hickey E., Brandon S. E., Smale G., Lloyd D., Weber L. A. Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein. Mol Cell Biol. 1989 Jun;9(6):2615–2626. doi: 10.1128/mcb.9.6.2615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Holmgren R., Corces V., Morimoto R., Blackman R., Meselson M. Sequence homologies in the 5' regions of four Drosophila heat-shock genes. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3775–3778. doi: 10.1073/pnas.78.6.3775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kimpel J. A., Key J. L. Presence of Heat Shock mRNAs in Field Crown Soybeans. Plant Physiol. 1985 Nov;79(3):672–678. doi: 10.1104/pp.79.3.672. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lindquist S., Craig E. A. The heat-shock proteins. Annu Rev Genet. 1988;22:631–677. doi: 10.1146/annurev.ge.22.120188.003215. [DOI] [PubMed] [Google Scholar]
  16. Lütcke H. A., Chow K. C., Mickel F. S., Moss K. A., Kern H. F., Scheele G. A. Selection of AUG initiation codons differs in plants and animals. EMBO J. 1987 Jan;6(1):43–48. doi: 10.1002/j.1460-2075.1987.tb04716.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Moore S. K., Kozak C., Robinson E. A., Ullrich S. J., Appella E. Cloning and nucleotide sequence of the murine hsp84 cDNA and chromosome assignment of related sequences. Gene. 1987;56(1):29–40. doi: 10.1016/0378-1119(87)90155-7. [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. 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]
  20. Rebbe N. F., Ware J., Bertina R. M., Modrich P., Stafford D. W. Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family. Gene. 1987;53(2-3):235–245. doi: 10.1016/0378-1119(87)90012-6. [DOI] [PubMed] [Google Scholar]
  21. Rose D. W., Wettenhall R. E., Kudlicki W., Kramer G., Hardesty B. The 90-kilodalton peptide of the heme-regulated eIF-2 alpha kinase has sequence similarity with the 90-kilodalton heat shock protein. Biochemistry. 1987 Oct 20;26(21):6583–6587. doi: 10.1021/bi00395a003. [DOI] [PubMed] [Google Scholar]
  22. Schlesinger M. J. Heat shock proteins: the search for functions. J Cell Biol. 1986 Aug;103(2):321–325. doi: 10.1083/jcb.103.2.321. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Vieira J., Messing J. Production of single-stranded plasmid DNA. Methods Enzymol. 1987;153:3–11. doi: 10.1016/0076-6879(87)53044-0. [DOI] [PubMed] [Google Scholar]
  24. 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