Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
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DOI：
10.1093/emboj/cdg547
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发表时间：
2003-11-03
期刊：
影响因子：
11.4
通讯作者：
Dangl, JL
中科院分区：
文献类型：
--
作者：
Hubert, DA;Tornero, P;Dangl, JL
拟南芥蛋白RPM1通过细菌III型递送系统作用于宿主细胞内部的假单胞菌蛋白，激活抗病活性。我们证明了单个拟南芥胞质HSP90亚型的ATP结合域的特定突变损害了RPM1的功能。这些突变不会影响相关抗病蛋白的功能。在植物细胞中，RPM1与HSP90结合。拟南芥蛋白RAR1和SGT1是许多R蛋白作用所必需的，它们在结构上与HSP90辅助伴侣蛋白有一些相似之处。它们都与植物细胞中的HSP90有关。我们的数据表明：(I)RPM1是一种HSP90客户蛋白；(Ii)RAR1和SGT1可能作为HSP90辅助因子独立发挥作用。这些蛋白质之间的动态相互作用可以调节RPM1的稳定性和功能，也许类似于动物类固醇受体复合体的形成和调节。
The Arabidopsis protein RPM1 activates disease resistance in response to Pseudomonas syringae proteins targeted to the inside of the host cell via the bacterial type III delivery system. We demonstrate that specific mutations in the ATP-binding domain of a single Arabidopsis cytosolic HSP90 isoform compromise RPM1 function. These mutations do not affect the function of related disease resistance proteins. RPM1 associates with HSP90 in plant cells. The Arabidopsis proteins RAR1 and SGT1 are required for the action of many R proteins, and display some structural similarity to HSP90 co-chaperones. Each associates with HSP90 in plant cells. Our data suggest that (i) RPM1 is an HSP90 client protein; and (ii) RAR1 and SGT1 may function independently as HSP90 cofactors. Dynamic interactions among these proteins can regulate RPM1 stability and function, perhaps similarly to the formation and regulation of animal steroid receptor complexes.