SMALL ACIDIC PROTEIN1 Acts with RUB Modification Components, the COP9 Signalosome, and AXR1 to Regulate Growth and Development of Arabidopsis

SMALL ACIDIC PROTEIN1 Acts with RUB Modification Components, the COP9 Signalosome, and AXR1 to Regulate Growth and Development of Arabidopsis
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DOI:
10.1104/pp.111.188409
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发表时间:
2012-09-01
期刊:
影响因子:
7.4
通讯作者:
Oono, Yutaka
Oono, Yutaka
中科院分区:
生物学1区
文献类型:
--
作者:
Nakasone, Akari;Fujiwara, Masayuki;Oono, Yutaka

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以前,小酸性蛋白1(SMAP 1)基因的功能障碍被鉴定为拟南芥(Arabidopsis thaliana)的抗生长素抗性1(aar 1)突变体的原因。SMAP 1参与合成生长素2,4-二氯苯氧乙酸的反应途径,并在生长素信号传导中的生长素/吲哚-3-乙酸蛋白降解步骤的上游起作用。然而,SMAP 1在生长素信号传导中发挥作用的确切机制仍然未知。在这里,我们证明SMAP 1是所需的正常植物生长和发育和根响应吲哚-3-乙酸或茉莉酸甲酯在生长素抗性1(axr 1)突变背景。缺失分析和绿色荧光蛋白/谷胱甘肽S-转移酶下拉分析表明,SMAP 1通过SMAP 1 F/D区与组成性光形态发生9信号体(CSN)发生物理相互作用。aar 1 -1 csn 5a-1双突变体的极端矮化表型证实了SMAP 1在植物生长和发育中在限制CSN功能下的功能作用。我们的研究结果表明,SMAP 1是参与生长素的反应,并可能在其他cullin-RING泛素连接酶调节的信号转导过程中,通过其与相关泛素修饰相关的组件的相互作用。
Previously, a dysfunction of the SMALL ACIDIC PROTEIN1 (SMAP1) gene was identified as the cause of the anti-auxin resistant1 (aar1) mutant of Arabidopsis (Arabidopsis thaliana). SMAP1 is involved in the response pathway of synthetic auxin, 2,4-dichlorophenoxyacetic acid, and functions upstream of the auxin/indole-3-acetic acid protein degradation step in auxin signaling. However, the exact mechanism by which SMAP1 functions in auxin signaling remains unknown. Here, we demonstrate that SMAP1 is required for normal plant growth and development and the root response to indole-3-acetic acid or methyl jasmonate in the auxin resistant1 (axr1) mutation background. Deletion analysis and green fluorescent protein/glutathione S-transferase pull-down assays showed that SMAP1 physically interacts with the CONSTITUTIVE PHOTOMORPHOGENIC9 SIGNALOSOME (CSN) via the SMAP1 F/D region. The extremely dwarf phenotype of the aar1-1 csn5a-1 double mutant confirms the functional role of SMAP1 in plant growth and development under limiting CSN functionality. Our findings suggest that SMAP1 is involved in the auxin response and possibly in other cullin-RING ubiquitin ligase-regulated signaling processes via its interaction with components associated with RELATED TO UBIQUITIN modification.