Abstract
A gene (Chl) encoding a novel type of chitinase was isolated from Beta vulgaris. The Ch1 protein consists of an N-terminal hydrophobic prepeptide of 25 amino acids followed by a hevein-like domain of 22 amino acid residues, an unusually long proline-rich domain of 131 amino acid residues with 90 prolines, and finally a catalytic domain of 261 amino acid residues. Proteins with similar proline-rich domains are present in some other plants. The Chl gene shows a transient expression in response to fungal infection.
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Berglund, L., Brunstedt, J., Nielsen, K.K. et al. A proline-rich chitinase from Beta vulgaris . Plant Mol Biol 27, 211–216 (1995). https://doi.org/10.1007/BF00019193
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DOI: https://doi.org/10.1007/BF00019193