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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The Pseudomonas syringae effector AvrRpt2 cleaves its C-terminally acylated target, RIN4, from Arabidopsis membranes to block RPM1 activation
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The Pseudomonas syringae effector AvrRpt2 cleaves its C-terminally acylated target, RIN4, from Arabidopsis membranes to block RPM1 activation

机译：丁香假单胞菌效应子AvrRpt2从拟南芥膜上裂解其C末端酰化靶标RIN4，以阻止RPM1激活

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摘要

Plant pathogenic Pseudomonas syringae deliver type Ⅲ effector proteins into the host cell, where they function to manipulate host defense and metabolism to benefit the extracellular bacterial colony. The activity of these virulence factors can be monitored by plant disease resistance proteins deployed to "guard" the targeted host proteins. The Arabidopsis RIN4 protein is targeted by three different type Ⅲ effectors. Specific manipulation of RIN4 by each of them leads to activation of either the RPM1 or RPS2 disease resistance proteins. The type Ⅲ effector AvrRpt2 is a cysteine protease that is autoprocessed inside the host cell where it activates RPS2 by causing RIN4 disappearance. RIN4 contains two sites related to the AvrRpt2 cleavage site (RCS1 and RCS2). We demonstrate that AvrRpt2-dependent cleavage of RIN4 at RCS2 is functionally critical in vivo. This event leads to proteasome-mediated elimination of all but a membrane-embedded ≈ 6.4-kDa C-terminal fragment of RIN4. One or more of three consecutive cysteines in this C-terminal fragment are required for RIN4 localization; these are likely to be palmitoylation and/or prenylation sites. AvrRpt2-dependent cleavage at RCS2, and release of the remainder of RIN4 from the membrane, consequently prevents RPM1 activation by AvrRpml or AvrB. RCS2 is contained within the smallest tested fragment of RIN4 that binds AvrB in vitro. Thus, at least two bacterial virulence factors target the same domain of RIN4, a ≈30-aa plant-specific signature sequence found in a small Arabidopsis protein family that may be additional targets for these bacterial virulence factors.
机译：植物致病性丁香假单胞菌将Ⅲ型效应蛋白传递到宿主细胞中，在其中它们发挥操纵宿主防御和代谢作用，从而有益于细胞外细菌菌落。这些毒力因子的活性可以通过植物抗病蛋白监控，以“保护”目标宿主蛋白。拟南芥RIN4蛋白被三种不同的Ⅲ型效应子靶向。它们中的每一个对RIN4的特异性操纵都会导致RPM1或RPS2疾病抗性蛋白的激活。 Ⅲ型效应子AvrRpt2是一种半胱氨酸蛋白酶，可在宿主细胞内自动加工，并通过引起RIN4消失而激活RPS2。 RIN4包含两个与AvrRpt2切割位点有关的位点（RCS1和RCS2）。我们证明在RCS2上RIN4的AvrRpt2依赖性裂解在体内功能至关重要。此事件导致蛋白酶体介导的RIN4除膜包埋的≈6.4 kDa C端片段外全部消除。 C端片段中三个连续的半胱氨酸中的一个或多个是RIN4定位所必需的。这些可能是棕榈酰化和/或异戊烯化位点。因此，在RCS2处依赖于AvrRpt2的切割，以及从膜中释放RIN4的其余部分，从而阻止了AvrRpml或AvrB激活RPM1。 RCS2包含在RIN4的最小测试片段中，该片段在体外与AvrB结合。因此，至少两个细菌毒力因子靶向RIN4的同一域，这是在一个小的拟南芥蛋白家族中发现的≈30-aa植物特异性特征序列，可能是这些细菌毒力因子的其他靶标。

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