Identification and characterization of ABA receptors in Oryza sativa.

Identification and characterization of ABA receptors in Oryza sativa.
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DOI:
10.1371/journal.pone.0095246
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发表时间:
2014
期刊:
影响因子:
3.7
通讯作者:
Yin P
Yin P
中科院分区:
综合性期刊3区
文献类型:
--
作者:
He Y;Hao Q;Li W;Yan C;Yan N;Yin P

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脱落酸(阿坝)是调节植物逆境反应的一种重要激素。拟南芥中的阿坝受体(AtPYLs)已经通过结构、生化和体内研究得到了广泛的研究。相比之下,对水稻中阿坝信号转导级联反应的了解相对较少。此外,AtPYLs的差异表明拟南芥中积累的信息不能简单地适应水稻。因此,对水稻阿坝受体的研究是必不可少的。通过生物信息学方法,我们在水稻(Oryza sativa)中鉴定了12个阿坝受体同源基因(OsPYLs),命名为OsPYL 1 -12。我们成功表达并纯化了OsPYL 1 -3、6和10-12,检测了OsPYL 1 -3、6和10-12对水稻PP 2C的抑制作用,并测定了OsPYL 1 - 3、6和10 - 12的寡聚状态。OsPYL 1 -3主要以二聚体形式存在,需要阿坝来抑制PP 2C的活性。OsPYL 6和OsPYL 10 -11则主要以单体形式存在,且均表现出ABA非依赖性的磷酸酶抑制作用。有趣的是,虽然OsPYL 12似乎是二聚体,但它在不存在阿坝的情况下消除了PP 2Cs的磷酸酶活性。为了进一步了解OsPYLs对阿坝结合和PP 2C抑制的作用,我们测定了ABA-OsPYL 2-OsPP 2C 06复合物的晶体结构。水稻阿坝受体的生物信息学、生物化学和结构分析为设计合理的ABA类似物和培育抗逆水稻提供了重要依据。
Abscisic acid (ABA) is an essential phytohormone that regulates plant stress responses. ABA receptors in Arabidopsis thaliana (AtPYLs) have been extensively investigated by structural, biochemical, and in vivo studies. In contrast, relatively little is known about the ABA signal transduction cascade in rice. Besides, the diversities of AtPYLs manifest that the information accumulated in Arabidopsis cannot be simply adapted to rice. Thus, studies on rice ABA receptors are compulsory. By taking a bioinformatic approach, we identified twelve ABA receptor orthologs in Oryza sativa (japonica cultivar-group) (OsPYLs), named OsPYL1–12. We have successfully expressed and purified OsPYL1–3, 6 and 10–12 to homogeneity, tested the inhibitory effects on PP2C in Oryza sativa (OsPP2C), and measured their oligomerization states. OsPYL1–3 mainly exhibit as dimers and require ABA to inhibit PP2C’s activity. On the contrary, OsPYL6 retains in the monomer-dimer equilibrium state and OsPYL10–11 largely exist as monomers, and they all display an ABA-independent phosphatase inhibition manner. Interestingly, although OsPYL12 seems to be a dimer, it abrogates the phosphatase activity of PP2Cs in the absence of ABA. Toward a further understanding of OsPYLs on the ABA binding and PP2C inhibition, we determined the crystal structure of ABA-OsPYL2-OsPP2C06 complex. The bioinformatic, biochemical and structural analysis of ABA receptors in rice provide important foundations for designing rational ABA-analogues and breeding the stress-resistant rice for commercial agriculture.
脱甲酸受体的激素信号传导的栅极锁锁机制。
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