Abstract
A gene (Chi) encoding a novel type of chitinase was isolated from Beta vulgaris. The Chi 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.
Original language | English |
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Journal | Plant Molecular Biology |
Volume | 27 |
Issue number | 1 |
Pages (from-to) | 211-216 |
ISSN | 0167-4412 |
DOIs | |
Publication status | Published - 1995 |
Externally published | Yes |