Berglund L, Brunstedt J, Nielsen K K, Chen Z, Mikkelsen J D, Marcker K A
Department of Molecular Biology, University of Aarhus, Denmark.
Plant Mol Biol. 1995 Jan;27(1):211-6. doi: 10.1007/BF00019193.
A gene (Ch1) 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 Ch1 gene shows a transient expression in response to fungal infection.
从甜菜中分离出一个编码新型几丁质酶的基因（Ch1）。Ch1蛋白由一个25个氨基酸的N端疏水前肽、一个22个氨基酸残基的类橡胶素结构域、一个异常长的富含131个氨基酸残基且含90个脯氨酸的富含脯氨酸结构域以及最后一个261个氨基酸残基的催化结构域组成。其他一些植物中也存在具有类似富含脯氨酸结构域的蛋白质。Ch1基因在真菌感染时表现出瞬时表达。
