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.
References
Bednarek SY, Raikhel NV: The barley lectin carboxylterminal propeptide is a vacuolar protein sorting determinant in plants. Plant Cell 3: 1195–1206 (1992).
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).
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).
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).
Chrispeels MJ, Raikhel NV: Short peptide domains target proteins to plant vacuoles. Cell 68: 613–616 (1992).
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).
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).
Linthorst HJM: Pathogenesis-related proteins of plants. Crit Rev Plant Sci 10: 123–150 (1991).
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).
Logemann J, Schell J, Willmitzer L: Improved method for the isolation of RNA from plant tissues. Anal Biochem 163: 16–20 (1987).
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).
Saedler H, Nevers P: Transposition in plants: a molecular mode. EMBO J 4: 585–590 (1985).
Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1989).
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).
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).
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).
Von Heijne G: Transcending the impenetrable: how proteins come to terms with membranes. Biochim Biophys Acta 974: 307–333 (1988).
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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
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DOI: https://doi.org/10.1007/BF00028991