Cloning and functional characterization of a class III chitinase gene from grapevine: Inhibition of fungal growth by recombinant VvChiF III

Abstract


S.A. Salami *, A. Ebadi , M.R. Naghavi and I.B. Dry

To characterize the structure and function of chitinase genes, a class III chitinase gene (VvChiF III) was isolated from Vitis vinifera cv. Flame seedless. The VvChiF III open reading frame comprised 894 nucleotides with no introns and encoded a protein of 297 amino acids. The amino acid sequence encoded by VvChiF III showed a high identity to that of a class III chitinase isolated from V. vinifera cv. Koshu and to other acidic chitinase. Analysis of the VvChiF III amino acid sequence showed that this gene corresponds to the Glyco-hydro-18 super family that consisting of a signal peptide with the length of 25 amino acids. Purified VvChiF III showed chitinase activity toward the soluble substrate, glycolchitin and antifungal activity against Botrytis cinerea.

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