Skip to main content
Log in

Isolation of a cDNA encoding a 70 kDa heat-shock cognate protein expressed in vegetative tissues ofArabidopsis thaliana

  • Short Communication
  • Published:
Plant Molecular Biology Aims and scope Submit manuscript


A cDNA encoding a 70 kDa heat shock ‘cognate’ protein (hsc70) was isolated fromArabidopsis thaliana by using a rat hsc70 cDNA as probe. Sequence analysis demonstrated the conservation of functional domains and important amino acid residues among hsc70s in plants and animals. The expression of this gene was stress-inducible, and was found at a substantial level during normal growth in root, stem, leaf and flower tissues, but not in siliques. Multiple copies of this gene exist in theArabidopsis genome.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Subscribe and save

Springer+ Basic
EUR 32.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or Ebook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.


  1. Chappell TG, Konforti BB, Schmid SL, Rothman JE: The ATPase core of a clathrin uncoating protein. J Biol Chem 262: 746–751 (1987).

    Google Scholar 

  2. Chirico WJ, Waters MG, Blobel G: 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 332: 805–810 (1988).

    Google Scholar 

  3. Deshaies RJ, Koch BD, Werner-Washburne M, Craig EA, Schekman R: A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332: 800–805 (1988).

    Google Scholar 

  4. Duck N, McCormick S, Winter J: Heat shock protein hsp70 cognate gene expression in vegetative and reproductive organs ofLycopersicon esculentum. Proc Natl Acad Sci USA 86: 3674–3678 (1989).

    Google Scholar 

  5. Flaherty KM, DeLuca-Flaherty C, McKay DB: Three dimensional structure of the ATPase fragment of a 70K heat shock cognate protein. Nature 346: 623–628 (1990).

    Google Scholar 

  6. Gaut JR, Hendershot LM: Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain. J Biol Chem 268: 7248–7255 (1993).

    Google Scholar 

  7. Gething M-J, Sambrook J: Protein folding in the cell. Nature 355: 33–45 (1992).

    Google Scholar 

  8. Huang S-p, Tsai M-Y, Tzou Y-M, Wu W-g, Wang C: Aspartyl residue 10 is essential for ATPase activity of rat hsc70. J Biol Chem 268: 2063–2068 (1993).

    Google Scholar 

  9. Jepson I, Bray J, Jenkins G, Schuch W, Edwards K: A rapid procedure for the construction of PCR cDNA libraries from small amounts of plant tissue. Plant Mol Biol Rep 9: 131–138 (1991).

    Google Scholar 

  10. Miernyk JA, Duck NB, Shatters RGJr, Folk WR: The 70-kilodalton heat shock cognate can act as a molecular chaperone during the membrane translocation of a plant secretory protein precursor. Plant Cell 4: 821–829 (1992).

    Google Scholar 

  11. Murakami H, Pain D, Blobel G: 70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria. J Cell Biol 107: 2051–2057 (1988).

    Google Scholar 

  12. Reiter RS, Williams JGK, Feldmann KA, Rafalski A, Tingey SV, Scolnik PO: Global and local genome mapping inArabidopsis thaliana by using recombinant inbred lines and random amplified polymorphic DNAs. Proc Natl Acad Sci USA 89: 1477–1481 (1992).

    Google Scholar 

  13. Shi Y, Thomas JO: The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Mol Cell Biol 12: 2186–2192 (1992).

    Google Scholar 

  14. Terlecky SR, Chiang H-L, Olson TS, Dice JF: Protein and peptide binding and stimulation ofin vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein. J Biol Chem 267: 9202–9209 (1992).

    Google Scholar 

  15. Tsai M-Y, Wang C: Uncoupling of peptide-stimulated ATPase and clathrin-uncoating activity in deletion mutant of hsc70. J Biol Chem 269: 5958–5962 (1994).

    Google Scholar 

  16. Vierling E: The role of heat shock proteins in plants. Annu Rev Plant Physiol Plant Mol Biol 42: 579–620 (1991).

    Google Scholar 

  17. Waegemann K, Paulsen H, Soll J: Translocation of proteins into isolated chloroplasts requires cytosolic factors to obtain import competence. FEBS Lett 261: 89–92 (1990).

    Google Scholar 

  18. Wang C, Lin B-L: The disappearance of an hsc70 species in mung bean seed during germination: purification and characterization of the protein. Plant Mol Biol 21: 317–329 (1993).

    Google Scholar 

  19. Wang T-F, Chang T-h, Wang C: Identification of the peptide binding domain of hsc70: 18-kDa fragment located immediately after ATPase domain is sufficient for high affinity binding. J Biol Chem 268: 26049–26051 (1993).

    Google Scholar 

  20. Wu CH, Caspar T, Browse J, Lindquist S, Somerville C: Characterization of an HSP70 cognate gene family inArabidopsis. Plant Physiol 88: 731–740 (1988).

    Google Scholar 

Download references

Author information

Authors and Affiliations


Rights and permissions

Reprints and permissions

About this article

Cite this article

Wu, SH., Wang, C., Chen, J. et al. Isolation of a cDNA encoding a 70 kDa heat-shock cognate protein expressed in vegetative tissues ofArabidopsis thaliana . Plant Mol Biol 25, 577–583 (1994).

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI:

Key words