The thioredoxin MoTrx2 protein mediates reactive oxygen species (ROS) balance and controls pathogenicity as a target of the transcription factor MoAP1 in Magnaporthe oryzae
The thioredoxin MoTrx2 protein mediates reactive oxygen species (ROS) balance and controls pathogenicity as a target of the transcription factor MoAP1 in Magnaporthe oryzae
复制标题
硫氧还蛋白 MoTrx2 蛋白作为稻瘟病菌转录因子 MoAP1 的靶标介导活性氧 (ROS) 平衡并控制致病性
DOI：
10.1111/mpp.12484
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发表时间：
2017-12-01
影响因子：
4.9
通讯作者：
Zhang, Zhengguang
中科院分区：
文献类型：
--
作者：
Wang, Jingzhen;Yin, Ziyi;Zhang, Zhengguang
我们以前已经表明，转录因子MoAP 1管理的氧化反应，是重要的致病性稻瘟病菌。为了探索潜在的机制，我们已经确定了硫氧还蛋白MoTrx 2作为M中MoAP 1的靶标。米。硫氧还蛋白是高度保守的12-kDa氧化还原酶，含有二硫醇-二硫化物活性位点，并作为抗自由基的抗氧化剂，如活性氧（ROS）。在酵母和真菌中，硫氧还蛋白对于氧化应激耐受性和生长是重要的。为了研究MoTrx 2的功能，我们产生了Delta Motrx 2突变体，这些突变体表现出各种缺陷，包括亚硫酸盐同化、无性和性分化、感染性菌丝生长和致病性。我们发现Delta Motrx 2突变体在宿主细胞入侵过程中清除ROS和主动抑制水稻防御反应方面存在缺陷。我们还发现，Delta Motrx 2突变体显示较高的细胞内活性氧水平在孢子萌发，但较低的过氧化物酶和漆酶活性，这有助于在毒力的衰减。鉴于MoTrx 2在胁迫反应和致病性中的功能与MoAP 1重叠，我们的研究结果进一步表明MoTrx 2是一个关键的硫氧还蛋白蛋白，其功能受到MoAP 1的转录调控。米。
We have shown previously that the transcription factor MoAP1 governs the oxidative response and is important for pathogenicity in the rice blast fungus Magnaporthe oryzae. To explore the underlying mechanism, we have identified thioredoxin MoTrx2 as a target of MoAP1 in M. oryzae. Thioredoxins are highly conserved 12-kDa oxidoreductase enzymes containing a dithiol-disulfide active site, and function as antioxidants against free radicals, such as reactive oxygen species (ROS). In yeast and fungi, thioredoxins are important for oxidative stress tolerance and growth. To study the functions of MoTrx2, we generated Delta Motrx2 mutants that exhibit various defects, including sulfite assimilation, asexual and sexual differentiation, infectious hyphal growth and pathogenicity. We found that Delta Motrx2 mutants possess a defect in the scavenging of ROS during host cell invasion and in the active suppression of the rice defence response. We also found that Delta Motrx2 mutants display higher intracellular ROS levels during conidial germination, but lower peroxidase and laccase activities, which contribute to the attenuation in virulence. Given that the function of MoTrx2 overlaps that of MoAP1 in the stress response and pathogenicity, our findings further indicate that MoTrx2 is a key thioredoxin protein whose function is subjected to transcriptional regulation by MoAP1 in M. oryzae.