ECP 诱导蛋白半胱氨酸残基的功能分析真菌番茄病原体——暗绿棒孢。
Functional analysis of cysteine residues of ECP elicitor proteins of the fungal tomato pathogen Cladosporium fulvum.
机构信息
Laboratory of Phytopathology, Wageningen University, Binnenhaven 5, 6709 PD Wageningen, the Netherlands.
出版信息
Mol Plant Pathol. 2002 Mar 1;3(2):91-5. doi: 10.1046/j.1464-6722.2001.00095.x.
summary A striking feature of all elicitor proteins of Cladosporium fulvum that are specifically recognized by tomato is that they contain an even number of cysteine residues. These cysteine residues are thought to be involved in disulphide bridges. In this study, a mutational analysis of the cysteine residues of ECP1, ECP2 and ECP5 was performed, to examine their role in stability and hypersensitive response-inducing activity of the proteins. We show that not all cysteine residues of the ECPs are critical for the hypersensitive response-inducing activity of the proteins, and we propose that the role of cysteine residues in the ECPs is more complex than anticipated.
摘要
被番茄特异性识别的所有棒孢叶点霉激发子蛋白的一个显著特征是它们都含有偶数个半胱氨酸残基。这些半胱氨酸残基被认为参与二硫键的形成。在这项研究中，对 ECP1、ECP2 和 ECP5 中的半胱氨酸残基进行了突变分析，以研究它们在这些蛋白的稳定性和诱导过敏反应活性中的作用。结果表明，不是所有 ECP 中的半胱氨酸残基对于蛋白的诱导过敏反应活性都是关键的，我们提出 ECP 中的半胱氨酸残基的作用比预期的更复杂。
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