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