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Calcium-dependent protein kinase CPK31 interacts with arsenic transporter AtNIP1;1 and regulates arsenite uptake in Arabidopsis thaliana

机译:钙依赖性蛋白激酶CPK31与砷转运蛋白AtNIP1; 1相互作用并调节拟南芥中砷的吸收

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摘要

Although arsenite [As(III)] is non-essential and toxic for plants, it is effectively absorbed through various transporters into the roots. Here we identified a calcium-dependent protein kinase (CPK31) response for As(III) tolerance in Arabidopsis. We identified CPK31 as an interacting protein of a nodulin 26-like intrinsic protein (NIP1;1), an aquaporin involved in As(III) uptake. Similarly to the nip1;1 mutants, the loss-of-function mutants of CPK31 improved the tolerance against As(III) but not As(V), and accumulated less As(III) in roots than that of the wild-type plants. The promoter-β-glucuronidase and quantitative Real-Time PCR analysis revealed that CPK31 displayed overlapping expression profiles with NIP1;1 in the roots, suggesting that they might function together in roots. Indeed, the cpk31 nip1;1 double mutants exhibited stronger As(III) tolerance than cpk31 mutants, but similar to nip1;1 mutants, supporting the idea that CPK31 might serve as an upstream regulator of NIP1;1. Furthermore, transient CPK31 overexpression induced by dexamethasone caused the decrease in As(III) tolerance of transgenic Arabidopsis lines. These findings reveal that CPK31 is a key factor in As(III) response in plants.
机译:尽管亚砷酸盐[As(III)]对植物不是必需和有毒的,但它可以通过各种转运蛋白有效地吸收到根中。在这里,我们确定了拟南芥中As(III)耐受性的钙依赖性蛋白激酶(CPK31)反应。我们确定CPK31为结节蛋白26样内在蛋白(NIP1; 1),参与As(III)吸收的水通道蛋白的相互作用蛋白。与nip1; 1突变体相似,CPK31功能丧失的突变体提高了对As(III)的耐受性,但对As(V)的耐受性却没有提高,并且根部的As(III)积累量少于野生型植物。启动子-β-葡糖醛酸糖苷酶和实时荧光定量PCR分析表明,CPK31在根中显示与NIP1; 1重叠的表达谱,表明它们可能在根中一起起作用。确实,cpk31 nip1; 1双重突变体显示出比cpk31突变体更强的As(III)耐受性,但与nip1; 1突变体相似,支持了CPK31可以充当NIP1; 1的上游调节子的观点。此外,地塞米松诱导的瞬时CPK31过表达引起转基因拟南芥品系的As(III)耐受性降低。这些发现表明,CPK31是植物中As(III)反应的关键因素。

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