油松DELLA蛋白结合GID1关键位点的鉴定和验证
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国家自然科学基金(5164033, 31370657);


Identification and Validation of Interactive Sites in DELLA Proteins Combined within GID1 in Conifers
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    摘要:

    该研究从油松中分离出2个DELLA蛋白,分别命名为PtDPL和PtRGA;序列保守性分析表明,这2个蛋白具备DELLA和GRAS特异结构域,其进化地位处于石松门和水稻之间,且具有被子植物GID1DELLA蛋白互作关键位点Δ17结构域;双分子荧光互补结果显示,Δ17结构域是油松GID1与DELLA蛋白相互作用的关键位点。转化拟南芥结果表明,移除Δ17结构域后,PtdplΔ17PtrgaΔ17转基因植株对赤霉素响应迟钝,且表现出更低的萌发率,验证了Δ17结构域是油松DELLA蛋白结合GID1的关键作用位点。该实验结果为进一步研究针叶树中GID1DELLA蛋白互作及赤霉素信号通路调控机制研究奠定了基础。

    Abstract:

    DELLA proteins works as a repressor and GID1 is the soluble receptor in GA signaling pathways, but currently little is known about interactive sites of GID1DELLA in conifers. we cloned two DELLA proteins (PtDPL; PtRGA) from Pinus tabuliformis named PtDPL and PtRGA. Sequence analysis showed these two DELLA proteins have DELLA and GRAS specific domains and their evolution distance both are between the rice and lycophyte, and they also have GID1DELLA interactive sites Δ17 domain as angiosperm; BiFC proved that Δ17 domain was key sites of interactions between the PtGID1PtDELLA; Without Δ17 domain, PtdplΔ17 and PtrgaΔ17 mutants showed a strong GAinsensitive phenotype compared to wildtype, suggesting that Δ17 domain is the key interactive sites in conifers GID1DELLA interaction. This research provides the basis for GID1DELLA interaction and GA signaling pathways mechanism.

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杜 冉,孙新蕊,钮世辉,等.油松DELLA蛋白结合GID1关键位点的鉴定和验证[J].西北植物学报,2017,37(1):32-39

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  • 在线发布日期: 2017-02-23
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