Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340.
Proc Natl Acad Sci U S A. 1989 Mar;86(5):1539-42. doi: 10.1073/pnas.86.5.1539.
A polygalacturonide purified from a tomato leaf pectic polysaccharide that induces the systemic synthesis of proteinase inhibitors in tomato plants enhances the phosphorylation of specific proteins in plasma membrane fractions isolated from tomato and potato leaves. In tomato plasma membranes, two proteins of 34 and 29 kDa show enhanced phosphorylation in response to the polyuronide. In potato plasma membranes, only a protein of 34 kDa exhibited enhanced phosphorylation due to the polyuronide. A noncarbohydrate class of proteinase inhibitor inducing factor, recently identified by workers in this laboratory, resulted in the in vitro hyperphosphorylation of a family of proteins of approximately 27 kDa. The phosphorylation of specific polypeptides in leaves in response to the same factors that induce the expression of proteinase inhibitor genes suggests that protein kinases may play an important role in the mechanism of signal transduction leading to defense gene expression.
从番茄叶果胶多糖中纯化出的一种多聚半乳糖醛酸，能诱导番茄植株体内蛋白酶抑制剂的系统合成，它能增强从番茄和土豆叶片中分离出的质膜级分中特定蛋白质的磷酸化。在番茄质膜中，有两种 34 和 29 kDa 的蛋白质对多聚半乳糖醛酸的反应增强了磷酸化作用。在土豆质膜中，只有一种 34 kDa 的蛋白质由于多聚半乳糖醛酸而表现出增强的磷酸化作用。本实验室的研究人员最近发现的一种非碳水化合物类蛋白酶抑制剂诱导因子，导致大约 27 kDa 的一组蛋白质在体外的过度磷酸化。在叶片中，对相同诱导蛋白酶抑制剂基因表达的因子的反应中，特定多肽的磷酸化表明蛋白激酶可能在导致防御基因表达的信号转导机制中起重要作用。
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