Skip to main content
Log in

Cloning and characterization of a cDNA encoding an antimicrobial chitin-binding protein from amaranth,Amaranthus caudatus

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

Abstract

A cDNA clone encoding an antimicrobial chitin-binding protein from amaranth (Amaranthus caudatus L.) was isolated using a cDNA library constructed from near-mature seed poly(A)+ mRNA. The deduced amino acid sequence of the cDNA clone encodes a predicted polypeptide of 86 amino acids. This polypeptide has three distinct domains: an amino-terminal putative signal peptide (25 amino acids), a domain corresponding to the mature protein (30 amino acids), and a carboxyl-terminal propeptide (31 amino acids) containing a putative N-glycosylation site. The encoded protein differs from all known members of the family of chitin-binding proteins. Transcripts of the expected size (650 bp) are present in developing seeds but not in roots, leaves or stressed leaves.

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

Access this article

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

Instant access to the full article PDF.

References

  1. Bednarek SY, Raikhel NV: The barley lectin carboxylterminal propeptide is a vacuolar protein sorting determinant in plants. Plant Cell 3: 1195–1206 (1992).

    Google Scholar 

  2. Broekaert W, Lee H-I, Kush A, Chua N-H, Raikhel N: Wound-induced accumulation of mRNA containing hevein sequence in laticifers of rubber tree (Hevea brasiliensis). Proc Natl Acad Sci USA 87: 7633–7637 (1990).

    Google Scholar 

  3. Broekaert WF, Mariën W, Terras FRG, De Bolle MFC, Proost P, Van Damme J, Dillen L, Claeys M, Rees SB, Vanderleyden J, Cammue BPA: Antimicrobial peptides fromAmaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins. Biochemistry 31: 4308–4314 (1992).

    Google Scholar 

  4. Broglie KE, Gaynor JJ, Broglie RM: Molecular cloning of the genes encoding an endochitinase fromPhaseolus vulgaris. Proc Natl Acad Sci USA 83: 6820–6824 (1986).

    Google Scholar 

  5. Chrispeels MJ, Raikhel NV: Short peptide domains target proteins to plant vacuoles. Cell 68: 613–616 (1992).

    Google Scholar 

  6. de Vries S, Hoge H, Bisseling T: Isolation of total and polysomal RNA from plant tissues. In: Gelvin SB, Schilperoort RA, Verma DPS (eds). Plant Molecular Biology Manual, pp. B6/1-B6/13 Kluwer Academic Publishers, Dordrecht (1988).

    Google Scholar 

  7. Faye L, Johnson D, Sturm A, Chrispeels MJ: Structure, biosynthesis, and function of asparagine-linked glycans on plant glycoproteins. Physiol Plant 75: 309–314 (1989).

    Google Scholar 

  8. Linthorst HJM: Pathogenesis-related proteins of plants. Crit Rev Plant Sci 10: 123–150 (1991).

    Google Scholar 

  9. Linthorst HJM, Danhash N, Brederode FT, van Kan JAL, de Wit PJGM, Bol JF: Tobacco and tomato PR proteins homologous towin and pro-hevein lack the ‘hevein’ domain. Mol Plant-Microbe Interact 4: 586–592 (1991).

    Google Scholar 

  10. Logemann J, Schell J, Willmitzer L: Improved method for the isolation of RNA from plant tissues. Anal Biochem 163: 16–20 (1987).

    Google Scholar 

  11. Raikhel NV, Broekaert WF: Chitin-binding proteins: their biology and possible function. In: Verma DPS (ed) Control of Plant Gene Expression, pp. 407–423. CRC Press (1993).

  12. Saedler H, Nevers P: Transposition in plants: a molecular mode. EMBO J 4: 585–590 (1985).

    Google Scholar 

  13. Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1989).

    Google Scholar 

  14. Shinshi H, Mohnen D, Meins F: Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc Natl Acad Sci USA 84: 89–93 (1987).

    Google Scholar 

  15. Shinshi H, Wenzler H, Neuhaus J-M, Felix G, Hofsteenge J, Meins FJr: Evidence for N- and C-terminal processing of a plant defense-related enzyme: primary structure of tobacco prepro-β-1,3-glucanase. Proc Natl Acad Sci USA 85: 5541–5545 (1988).

    Google Scholar 

  16. Shinshi H, Neuhaus J-M, Ryals J, Meins FJr: Structure of tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain. Plant Mol Biol 14: 357–368 (1990).

    Google Scholar 

  17. Von Heijne G: Transcending the impenetrable: how proteins come to terms with membranes. Biochim Biophys Acta 974: 307–333 (1988).

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

De Bolle, M.F.C., David, K.M.M., Rees, S.B. et al. Cloning and characterization of a cDNA encoding an antimicrobial chitin-binding protein from amaranth,Amaranthus caudatus . Plant Mol Biol 22, 1187–1190 (1993). https://doi.org/10.1007/BF00028991

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00028991

Key words

Navigation