The Arabidopsis thaliana TIR-NB-LRR R-protein, RPP1A; protein localization and constitutive activation of defence by truncated alleles in tobacco and Arabidopsis.

The Arabidopsis thaliana TIR-NB-LRR R-protein, RPP1A; protein localization and constitutive activation of defence by truncated alleles in tobacco and Arabidopsis.
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DOI:
10.1111/j.1365-313x.2006.02834.x
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发表时间:
2006-09
期刊:
The Plant journal : for cell and molecular biology
影响因子:
--
通讯作者:
L. Michael Weaver;M. Swiderski;Yan Li;Jonathan D. G. Jones
L. Michael Weaver;M. Swiderski;Yan Li;Jonathan D. G. Jones
中科院分区:
其他
文献类型:
--
作者:
L. Michael Weaver;M. Swiderski;Yan Li;Jonathan D. G. Jones

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拟南芥Ws-0对白粉病分离物Cala2的特异性识别是由抗性基因RPP1a介导的。不同截短的RPP1A在烟草叶片中的瞬时表达表明,其TIR-NB-ARC部分足以诱导非激发子非激发子依赖的细胞死亡。在稳定的拟南芥转基因株系中,利用35S启动子过表达RPP1ATIR-Nb-ARC结构域(E12),导致对寄生赤霉病和丁香假单胞菌DC3000强毒株的广谱抗性。TIR-NB-ARC介导的结构性免疫是由于水杨酸依赖的抗性途径被激活,并被EDS1的突变或水杨酸羟基酶基因NahG的存在所缓解。35S::E12植株的生长受到抑制,这是在许多成分抗性突变体中观察到的一种表型。RPP1A在其N端携带一个疏水肽,将RPP1A蛋白引导到膜中,尽管它可能不是介导RPP1A膜结合的唯一决定因素。两相分离和蔗糖密度梯度沉淀证实RPP1a存在于内质网和/或高尔基体。
Specific recognition of Hyaloperonospora parasitica isolate Cala2 by Arabidopsis thaliana Ws-0 is mediated by the resistance gene RPP1A. Transient expression of different truncations of RPP1A in tobacco leaves revealed that its TIR-NB-ARC portion is sufficient to induce an elicitor-independent cell death. In stable transgenic lines of Arabidopsis, overexpression of the RPP1A TIR-NB-ARC domains (E12) using the 35S promoter leads to broad-spectrum resistance to virulent strains of H. parasitica and Pseudomonas syringae DC3000. The TIR-NB-ARC-mediated constitutive immunity is due to activation of the salicylic acid-dependent resistance pathway and is relieved by either a mutation in EDS1 or the presence of the salicylate hydroxylase gene, NahG. Growth of 35S::E12 plants is reduced, a phenotype observed in many constitutively resistant mutants. RPP1A carries a hydrophobic peptide at its N-terminus that directs the RPP1A protein into membranes, though it may not be the sole determinant mediating membrane association of RPP1A. Two-phase partitioning and sucrose density gradient sedimentation established that RPP1A resides in the endoplasmic reticulum and/or Golgi apparatus.