Arabidopsis MKS1 is involved in basal immunity and requires an intact N-terminal domain for proper function.

Arabidopsis MKS1 is involved in basal immunity and requires an intact N-terminal domain for proper function.
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DOI:
10.1371/journal.pone.0014364
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发表时间:
2010-12-28
期刊:
影响因子:
3.7
通讯作者:
Petersen M
Petersen M
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Petersen K;Qiu JL;Lütje J;Fiil BK;Hansen S;Mundy J;Petersen M

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在动物和植物中的天然免疫信号传导途径由丝裂原活化蛋白激酶(MAPK)级联调节。MAP激酶4(MPK 4)通过核底物MKS 1在先天免疫受体下游发挥作用,以调节WRKY 33转录因子的活性,WRKY 33转录因子进而控制抗微生物植物抗毒素的产生。我们调查的作用MKS 1在基础电阻和重要性,其N-和C-末端结构域MKS 1功能。我们使用的信息,mks 1的功能丧失部分抑制mpk 4的功能丧失表型,以及转基因表达的功能MKS 1在mpk 4/mks 1双突变体恢复mpk 4侏儒表型。用突变型MKS 1构建体转化mks 1/mpk 4表明,在推定的MAP激酶对接结构域MKS 1-L32 A或不能与WRKY 33相互作用的截短型MKS 1中的单个氨基酸取代在将双突变体恢复为mpk 4表型方面是缺陷的。这些结果证明了MKS 1中与MPK 4和WRKY 33相互作用的功能需求。此外,核定位的MKS 1被证明依赖于一个完整的N-末端结构域。此外,功能丧失的mks 1突变体表现出增加的敏感性菌株的假单胞菌和透明operonospora arabidopsidis,表明MKS 1在基础防御反应中发挥作用。总之,我们的研究结果表明,MKS 1的功能和亚细胞位置需要一个完整的N-末端重要的MPK 4和WRKY 33的相互作用。
Innate immune signaling pathways in animals and plants are regulated by mitogen-activated protein kinase (MAPK) cascades. MAP kinase 4 (MPK4) functions downstream of innate immune receptors via a nuclear substrate MKS1 to regulate the activity of the WRKY33 transcription factor, which in turn controls the production of anti-microbial phytoalexins. We investigate the role of MKS1 in basal resistance and the importance of its N- and C-terminal domains for MKS1 function. We used the information that mks1 loss-of-function partially suppresses the mpk4 loss-of-function phenotype, and that transgenic expression of functional MKS1 in mpk4/mks1 double mutants reverted the mpk4 dwarf phenotype. Transformation of mks1/mpk4 with mutant versions of MKS1 constructs showed that a single amino acid substitution in a putative MAP kinase docking domain, MKS1-L32A, or a truncated MKS1 version unable to interact with WRKY33, were deficient in reverting the double mutant to the mpk4 phenotype. These results demonstrate functional requirement in MKS1 for the interaction with MPK4 and WRKY33. In addition, nuclear localization of MKS1 was shown to depend on an intact N-terminal domain. Furthermore, loss-of-function mks1 mutants exhibited increased susceptibility to strains of Pseudomonas syringae and Hyaloperonospora arabidopsidis, indicating that MKS1 plays a role in basal defense responses. Taken together, our results indicate that MKS1 function and subcellular location requires an intact N-terminus important for both MPK4 and WRKY33 interactions.
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