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四种拟南芥小檗碱桥酶样蛋白是特定的氧化酶,可使激发子活性寡聚半乳糖醛酸失活。

Four Arabidopsis berberine bridge enzyme-like proteins are specific oxidases that inactivate the elicitor-active oligogalacturonides.

机构信息

Department of Biology and Biotechnology 'Charles Darwin', Sapienza University of Rome, Piazzale Aldo Moro 5, 00185, Rome, Italy.

Department MESVA, University of L'Aquila, L'Aquila, Italy.

出版信息

Plant J. 2018 Apr;94(2):260-273. doi: 10.1111/tpj.13852. Epub 2018 Mar 15.

DOI:10.1111/tpj.13852
PMID:29396998
Abstract

Recognition of endogenous molecules acting as 'damage-associated molecular patterns' (DAMPs) is a key feature of immunity in both animals and plants. Oligogalacturonides (OGs), i.e. fragments derived from the hydrolysis of homogalacturonan, a major component of pectin are a well known class of DAMPs that activate immunity and protect plants against several microbes. However, hyper-accumulation of OGs severely affects growth, eventually leading to cell death and clearly pointing to OGs as players in the growth-defence trade-off. Here we report a mechanism that may control the homeostasis of OGs avoiding their deleterious hyper-accumulation. By combining affinity chromatography on acrylamide-trapped OGs and other procedures, an Arabidopsis thaliana enzyme that specifically oxidizes OGs was purified and identified. The enzyme was named OG OXIDASE 1 (OGOX1) and shown to be encoded by the gene At4g20830. As a typical flavo-protein, OGOX1 is a sulphite-sensitive H O -producing enzyme that displays maximal activity on OGs with a degree of polymerization >4. OGOX1 belongs to a large gene family of mainly apoplastic putative FAD-binding proteins [Berberine Bridge Enzyme-like (BBE-like); 27 members], whose biochemical and biological function is largely unexplored. We have found that at least four BBE-like enzymes in Arabidopsis are OG oxidases (OGOX1-4). Oxidized OGs display a reduced capability of activating the immune responses and are less hydrolysable by fungal polygalacturonases. Plants overexpressing OGOX1 are more resistant to Botrytis cinerea, pointing to a crucial role of OGOX enzymes in plant immunity.

摘要

内源性分子识别作为“损伤相关分子模式”(DAMPs)是动物和植物免疫的一个关键特征。寡半乳糖醛酸(OGs),即源自果胶主要成分同质半乳糖醛酸水解的片段,是激活免疫并保护植物免受几种微生物侵害的一类众所周知的 DAMPs。然而,OGs 的过度积累严重影响生长,最终导致细胞死亡,并清楚地表明 OGs 是生长与防御权衡中的参与者。在这里,我们报告了一种可能控制 OGs 内稳态的机制,避免其有害的过度积累。通过在丙烯酰胺捕获的 OGs 上进行亲和层析和其他程序的组合,我们纯化并鉴定了一种特异性氧化 OGs 的拟南芥酶。该酶被命名为 OG 氧化酶 1(OGOX1),并被证明由 At4g20830 基因编码。作为一种典型的黄素蛋白,OGOX1 是一种亚硫酸盐敏感的 H2O 产生酶,对聚合度>4 的 OGs 显示最大活性。OGOX1 属于一个大型基因家族,主要是质外体假定的 FAD 结合蛋白[小檗碱桥接酶样(BBE-like); 27 个成员],其生化和生物学功能在很大程度上尚未探索。我们发现拟南芥中至少有四个 BBE-like 酶是 OG 氧化酶(OGOX1-4)。氧化的 OGs 显示出降低激活免疫反应的能力,并且更难被真菌多聚半乳糖醛酸酶水解。过表达 OGOX1 的植物对 Botrytis cinerea 的抗性更强,这表明 OGOX 酶在植物免疫中起着至关重要的作用。

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