The six conserved serine/threonine sites of REPRESSOR OF ga1-3 protein are important for its functionality and stability in gibberellin signaling in Arabidopsis

The six conserved serine/threonine sites of REPRESSOR OF ga1-3 protein are important for its functionality and stability in gibberellin signaling in Arabidopsis
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REPRESSOR OF ga1-3 蛋白的六个保守丝氨酸/苏氨酸位点对其在拟南芥赤霉素信号传导中的功能和稳定性很重要

DOI:
10.1007/s00425-014-2113-3
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发表时间:
2014-07
期刊:
影响因子:
4.3
通讯作者:
Hou, Suiwen
Hou, Suiwen
中科院分区:
生物学2区
文献类型:
--
作者:
Huang, Bingyao;Xu, Xiufei;Yan, Longfeng;Hou, Suiwen

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我们的研究结果提供了进一步了解拟南芥DELLA蛋白的调控。我们阐明了六个保守位点的磷酸化修饰对于RGA功能和稳定性是重要的。DELLA蛋白是重要的植物生长发育抑制因子,参与调节赤霉素(GA)信号转导途径。尽管这些蛋白质在分子水平上表现出磷酸化和去磷酸化状态,但关于DELLA蛋白质的不同修饰对其在遗传水平上的生物活性和稳定性的调节的影响知之甚少。在这项研究中,6个保守的丝氨酸(Ser)/苏氨酸(Thr)的位点的修复ga 1 -3(RGA)被替换为丙氨酸(RGA 6A)或天冬氨酸(RGA 6D),以模拟组成性去磷酸化和磷酸化的状态,分别。我们发现,去磷酸模拟RGA在Col-0植物中的过量表达导致GA过量表型,这与DELLA缺陷突变体相似。这些表型可能归因于去磷酸化RGA,其保留了诱导GA生物合成基因的转录激活活性,但失去了抑制GA响应基因的转录抑制子功能。此外,去磷酸化的RGA不稳定,容易降解,不像野生型RGA,这表明去磷酸化的形式是其降解所必需的。与此相反,拟磷酸化RGA过度表达导致GA缺乏表型与不可降解的RGA。这些表型可能是由于磷酸模拟RGA,它抑制GA响应基因的表达,而不是诱导GA生物合成基因。此外,磷酸模拟RGA稳定且不易降解,加重了GA信号转导中RGA的抑制作用。总之,我们表明,六个保守的Ser/Thr位点是重要的RGA蛋白的不同的生物活性,调节GA的反应,也为RGA的稳定性,通过模仿磷酸化/去磷酸化。
Our results provide further insight into the regulation of DELLA proteins in Arabidopsis . We clarified that phosphorylation modification of the six conserved sites is important for RGA functions and stability. The DELLA proteins, important plant growth and development repressors mediate the gibberellin (GA) signaling pathway. Although these proteins exhibit phosphorylation and de-phosphorylation states at the molecular level, little is known regarding the effects of different modifications of DELLA proteins on the regulation of their bioactivity and stability at the genetic level. In this study, six conserved serine (Ser)/threonine (Thr) sites of REPRESSOR OF ga1-3 (RGA) were substituted with alanine (RGA6A) or aspartic acid (RGA6D) to mimic the states of constitutive de-phosphorylation and phosphorylation, respectively. We found that the overexpression of de-phosphomimic RGA in Col-0 plants caused GA-overdose phenotypes, which were similar to DELLA-deficient mutant. These phenotypes were probably attributed to de-phosphomimic RGA, which retained its transcriptional activation activity that induces GA biosynthetic genes, but lost the transcription repressor function that inhibits GA-responsive genes. Further, de-phosphomimic RGA was unstable and easily degradable unlike the wild-type RGA, suggesting that the de-phosphorylated form is necessary for its degradation. In contrast, phosphomimic RGA overexpression caused GA-deficient phenotypes with non-degradable RGA. These phenotypes were probably due to phosphomimic RGA, which represses GA-responsive gene expression instead of inducing GA biosynthetic genes. In addition, phosphomimic RGA was stable and hardly degradable, which aggravated the RGA-inhibiting function in GA signaling. In conclusion, we show that the six conserved Ser/Thr sites are important for the different bioactivities of the RGA protein that regulate the GA response, and also for RGA stability via the mimicking of phosphorylation/de-phosphorylation.
水稻早花 1 是一种 CKI,磷酸化 DELLA 蛋白 SLR1 以负向调节赤霉素信号传导
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发表时间: 2010-06-02
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