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