A Lipid-Anchored NAC Transcription Factor Is Translocated into the Nucleus and Activates Glyoxalase I Expression during Drought Stress
A Lipid-Anchored NAC Transcription Factor Is Translocated into the Nucleus and Activates Glyoxalase I Expression during Drought Stress
复制标题
脂质锚定的 NAC 转录因子在干旱胁迫期间转位至细胞核并激活乙二醛酶 I 表达
DOI：
10.1105/tpc.17.00044
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发表时间：
2017-07-01
期刊：
影响因子：
11.6
通讯作者：
Wang, Tao
中科院分区：
文献类型：
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作者：
Duan, Mei;Zhang, Rongxue;Wang, Tao
植物特异性NAC （NAM、ATAF1/2和CUC2）转录因子在植物对干旱胁迫的响应中起着至关重要的作用。在这里，我们报道了一种在苜蓿中脂锚定的NACsa TF。MfNACsa是植物抗干旱胁迫的重要调控因子，导致参与氧化还原和脂质转运及定位的基因表达差异。MfNACsa在非应激条件下与膜相关，更具体地说，它通过s -棕榈酰化作用于质膜。然而，Cys(26)- ser突变或s -棕榈酰化抑制会导致MfNACsa保留在内质网/高尔基体中。干旱胁迫下，MfNACsa通过硫酯酶MtAPT1介导的去s棕榈酰化转运至细胞核，APT1的共表达导致MfNACsa的核易位，而APT1催化位点的突变导致MfNACsa与MfNACsa共定位，MfNACsa的膜保留。具体来说，细胞核MfNACsa在干旱胁迫下结合glyoxalase I （MtGlyl）启动子，通过维持谷胱甘肽库处于还原状态而产生耐旱性，这一过程依赖于APT1-NACsa调控模块。我们的研究结果揭示了s -棕榈酰化NAC在应激反应中核易位的新机制。
The plant-specific NAC (NAM, ATAF1/2, and CUC2) transcription factors (TFs) play a vital role in the response to drought stress. Here, we report a lipid-anchored NACsa TF in Medicago falcata. MfNACsa is an essential regulator of plant tolerance to drought stress, resulting in the differential expression of genes involved in oxidation reduction and lipid transport and localization. MfNACsa is associated with membranes under unstressed conditions and, more specifically, is targeted to the plasma membrane through S-palmitoylation. However, a Cys(26)-to-Ser mutation or inhibition of S-palmitoylation results in MfNACsa retention in the endoplasmic reticulum/Golgi. Under drought stress, MfNACsa translocates to the nucleus through de-S-palmitoylation mediated by the thioesterase MtAPT1, as coexpression of APT1 results in the nuclear translocation of MfNACsa, whereas mutation of the catalytic site of APT1 results in colocalization with MfNACsa and membrane retention of MfNACsa. Specifically, the nuclear MfNACsa binds the glyoxalase I (MtGlyl) promoter under drought stress, resulting in drought tolerance by maintaining the glutathione pool in a reduced state, and the process is dependent on the APT1-NACsa regulatory module. Our findings reveal a novel mechanism for the nuclear translocation of an S-palmitoylated NAC in response to stress.