Phytoplasma-induced Changes in the Acetylome and Succinylome of Paulownia tomentosa Provide Evidence for Involvement of Acetylated Proteins in Witches' Broom Disease
Phytoplasma-induced Changes in the Acetylome and Succinylome of Paulownia tomentosa Provide Evidence for Involvement of Acetylated Proteins in Witches' Broom Disease
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DOI：
10.1074/mcp.ra118.001104
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发表时间：
2019-06-01
影响因子：
7
通讯作者：
Gu, Zhibin
中科院分区：
文献类型：
--
作者：
Cao, Yabing;Fan, Guoqiang;Gu, Zhibin
赖氨酸乙酰化和琥珀酰化是蛋白质的翻译后修饰，已被证明在植物对病原体感染的反应中发挥作用。植原体感染可直接改变落叶植物泡桐的多种代谢过程，并导致泡桐丛枝病（PaWB），这是全球范围内泡桐死亡的主要原因。然而，在植原体感染过程中赖氨酸乙酰化和琥珀酰化的程度和功能还有待探讨。在这里，我们研究了植原体感染毛泡桐幼苗蛋白质组，乙酰基组和琥珀酰组的变化，采用定量质谱。我们总共鉴定了8963个蛋白质，2893个乙酰化蛋白质（5558个乙酰化位点）和1271个琥珀酰化蛋白质（1970个琥珀酰化位点），其中425个（533个位点）同时乙酰化和琥珀酰化。比较分析显示，276个蛋白质，546乙酰化蛋白质（741乙酰化位点）和5琥珀酰化蛋白质（5琥珀酰化位点）在响应植原体感染的调节，表明乙酰化可能比琥珀酰化在PaWB中更重要。酶促分析表明，乙酰化的特定网站在原叶绿素还原酶和RuBisCO，叶绿素和淀粉生物合成的关键酶，分别修改植原体感染的幼苗的活动。在这些结果的基础上，我们提出了一个模型来阐明反应的分子机制PaWB和乙酰化对蛋白质功能的影响的功能研究提供了一个资源。
Lysine acetylation and succinylation are post-translational modifications of proteins that have been shown to play roles in plants response to pathogen infection. Phytoplasma infection can directly alter multiple metabolic processes in the deciduous plant Paulownia and lead to Paulownia witches' broom (PaWB) disease, the major cause of Paulownia mortality worldwide. However, the extent and function of lysine aceylation and succinylation during phytoplasma infection have yet to be explored. Here, we investigated the changes in the proteome, acetylome, and succinylome of phytoplasma-infected Paulownia tomentosa seedlings using quantitative mass spectrometry. In total, we identified 8963 proteins, 2893 acetylated proteins (5558 acetylation sites), and 1271 succinylated proteins (1970 succinylation sites), with 425 (533 sites) simultaneously acetylated and succinylated. Comparative analysis revealed that 276 proteins, 546 acetylated proteins (741 acetylation sites) and 5 succinylated proteins (5 succinylation sites) were regulated in response to phytoplasma infection, suggesting that acetylation may be more important than succinylation in PaWB. Enzymatic assays showed that acetylation of specific sites in protochlorophyllide reductase and RuBisCO, key enzymes in chlorophyll and starch biosynthesis, respectively, modifies their activity in phytoplasma-infected seedlings. On the basis of these results, we propose a model to elucidate the molecular mechanism of responses to PaWB and offer a resource for functional studies on the effects of acetylation on protein function.