Histone H2B Monoubiquitination Is Involved in Regulating the Dynamics of Microtubules during the Defense Response to Verticillium dahliae Toxins in Arabidopsis1[OPEN]
Histone H2B Monoubiquitination Is Involved in Regulating the Dynamics of Microtubules during the Defense Response to Verticillium dahliae Toxins in Arabidopsis1[OPEN]
复制标题
组蛋白 H2B 单泛素化参与拟南芥黄萎病毒素防御反应过程中微管动态的调节 (1[OPEN])
DOI：
10.1104/pp.113.234567
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发表时间：
2014-04-01
期刊：
影响因子：
7.4
通讯作者：
Li, Ying-Zhang
中科院分区：
文献类型：
--
作者：
Hu, Min;Pei, Bao-Lei;Li, Ying-Zhang
组蛋白H2B单泛素化（H2Bub）被认为是一种调控机制，控制植物的一系列细胞过程，但H2Bub参与生物胁迫反应的分子机制在很大程度上是未知的。在这项研究中，我们使用野生型和H2Bub功能丧失突变的拟南芥（拟南芥），以阐明其机制参与调节植物的防御反应大丽轮枝菌（Vd）毒素。我们表明，皮质微管（MTs）的解聚是不同的野生型和突变体的反应Vd毒素。组蛋白MONOUBIQUITINATION1和组蛋白MONOUBIQUITINATION2突变的功能丧失等位基因表现出较弱的MT解聚，蛋白酪氨酸磷酸化在MT动力学的调节中起关键作用。此外，H2Bub是蛋白酪氨酸磷酸酶基因表达的正调节剂。这些研究结果提供了直接的证据H2Bub作为一个重要的修改与调节作用，在防御Vd毒素，并表明，H2Bub参与调节的动态MTs，可能通过蛋白酪氨酸磷酸酶介导的信号通路。
Histone H2B monoubiquitination (H2Bub) is being recognized as a regulatory mechanism that controls a range of cellular processes in plants, but the molecular mechanisms of H2Bub that are involved in responses to biotic stress are largely unknown. In this study, we used wild-type and H2Bub loss-of-function mutations of Arabidopsis (Arabidopsis thaliana) to elucidate which of its mechanisms are involved in the regulation of the plant's defense response to Verticillium dahliae (Vd) toxins. We demonstrate that the depolymerization of the cortical microtubules (MTs) was different in the wild type and the mutants in the response to Vd toxins. The loss-of-function alleles of HISTONE MONOUBIQUITINATION1 and HISTONE MONOUBIQUITINATION2 mutations present a weaker depolymerization of theMTs, and protein tyrosine phosphorylation plays a critical role in the regulation of the dynamics of MTs. Moreover, H2Bub is a positive regulator of the gene expression of protein tyrosine phosphatases. These findings provide direct evidence for H2Bub as an important modification with regulatory roles in the defense against Vd toxins and demonstrate that H2Bub is involved in modulating the dynamics of MTs, likely through the protein tyrosine phosphatase-mediated signaling pathway.