Two homologous protein S-acyltransferases, PAT13 and PAT14, cooperatively regulate leaf senescence in Arabidopsis
Two homologous protein S-acyltransferases, PAT13 and PAT14, cooperatively regulate leaf senescence in Arabidopsis
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两种同源蛋白 S-酰基转移酶 PAT13 和 PAT14 协同调节拟南芥叶片衰老。
DOI：
10.1093/jxb/erv347
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发表时间：
2015-10-01
影响因子：
6.9
通讯作者：
Yang, Chengwei
中科院分区：
文献类型：
--
作者：
Lai, Jianbin;Yu, Boya;Yang, Chengwei
蛋白质半胱氨酸残基上的脂质修饰，称为S-棕榈酰化或S-酰化，调节蛋白质的亚细胞定位和功能。S-酰化由一组具有保守的Asp-His-His-Cys（DHHC）基序的蛋白质酰基转移酶（PAT）催化。在酵母和哺乳动物细胞中，S-酰化的分子功能已被详细研究，但其在植物细胞中的作用仍不清楚。本文报道了两种同源蛋白酰基转移酶--PAT 13和PAT 14--的表达在拟南芥的老叶中适度增加。PAT 13和PAT 14的双突变体表现出严重的叶片早衰表型。在双突变体中，该表型被PAT 13或PAT 14过表达补充，证实了PAT 13和PAT 14在该过程中的作用。此外，活性氧（ROS）和细胞死亡的水平显着诱导双突变体。为了研究PAT 13和PAT 14的分子功能，利用生物信息学方法预测了它们潜在的S-酰化底物。亚细胞定位和S-酰化的候选底物一氧化氮相关1（NOA 1），这也发挥了作用，在叶片衰老控制，部分破坏的原生质体的双突变体。NOA 1的S-酰化损伤影响其亚细胞定位及其在叶片衰老调控中的功能。因此，蛋白质S-酰基转移酶PAT 13和PAT 14可能通过NOA 1的S-酰基化参与叶片衰老的调控，为研究S-酰基化在叶片衰老调控中的作用机制提供了新的视角。
Lipid modification on the cysteine residues of proteins, known as S-palmitoylation or S-acylation, regulates the subcellular localization and the function of proteins. S-acylation is catalysed by a group of protein acyltransferases (PATs) with a conserved Asp-His-His-Cys (DHHC) motif. The molecular function of S-acylation has been studied in details in yeast and mammalian cells, but its role in plant cells remains unclear. Here it is reported that the expression of two homologous protein acyltransferases- PAT13 and PAT14 -was moderately increased in the older leaves of Arabidopsis. The double mutant of PAT13 and PAT14 displayed a severely early leaf senescence phenotype. The phenotype was complemented by PAT13 or PAT14 overexpression in the double mutant, confirming the roles of PAT13 and PAT14 in this process. Furthermore, the levels of reactive oxygen species (ROS) and cell death were dramatically induced in the double mutant. To investigate the molecular functions of PAT13 and PAT14, their potential S-acylation substrates were predicted by bioinformatics methods. The subcellular localization and S-acylation of a candidate substrate NITRIC OXIDE ASSOCIATED 1 (NOA1), which also plays a role in leaf senescence control, were partially disrupted in the protoplasts of the double mutant. Impairment of S-acylation on NOA1 affected its subcellular localization and its function in leaf senescence regulation. Conclusively, protein S-acyltransferases PAT13 and PAT14 are involved in leaf senescence control- possibly via NOA1 S-acylation-, providing a new sight into the regulation mechanism of S-acylation in leaf senescence.