Regulation of Nod1 by Hsp90 chaperone complex
Regulation of Nod1 by Hsp90 chaperone complex
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DOI：
10.1016/j.febslet.2005.07.024
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发表时间：
2005-08-15
期刊：
影响因子：
3.5
通讯作者：
Hahn, JS
中科院分区：
文献类型：
--
作者：
Hahn, JS
Nod1和Nod2蛋白作为细菌肽聚糖的细胞内传感器在哺乳动物先天免疫应答中起重要作用。Nod1和Nod2与许多参与植物抗病的R蛋白具有结构同源性。研究表明，植物Hsp90及其共同伴侣RAR1与r介导的抗病有关。在这里，编码植物RAR1的哺乳动物同源基因Chp-1被确定为热休克因子1 （HSF1）转录激活的新靶点，HSF1是一种应激反应性HSF异构体。此外，Nod1被证明是含有Chp-1的Hsp90伴侣复合体的客户蛋白。Chp-1通过两个不同的锌结合半胱氨酸和富组氨酸结构域（CHORDS）与蛋白磷酸酶5 （PP5）的四肽重复（TPR）结构域和Hsp90的三磷酸腺苷酶结构域相互作用。这些发现表明，在r介导的植物抗病和哺乳动物nod1介导的先天免疫应答中，Hsp90伴侣复合物参与了一个共同的调控机制。(c) 2005年由Elsevier B.V.代表欧洲生化学会联合会出版。
Nod1 and Nod2 proteins play important roles in mammalian innate immune responses as intracellular sensors for bacterial peptidoglycan. Nod1 and Nod2 share structural homology with many R proteins involved in plant disease resistance. It has been demonstrated that plant Hsp90 and its co-chaperone RAR1 are implicated in R-mediated disease resistance. Here the Chp-1 gene encoding a mammalian homologue of plant RAR1 was identified as a new target for transcriptional activation by heat shock factor 1 (HSF1), a stress-responsive HSF isoform. In addition, Nod1 is demonstrated to be a client protein of the Hsp90 chaperone complex containing the Chp-1. Chp-1 interacts with the tetratricopeptide repeat (TPR) domain of protein phosphatase 5 (PP5) and the ATPase domain of Hsp90 via two distinct zinc-binding cysteine and histidine rich domains (CHORDS). These findings suggest a common regulatory mechanism involving the Hsp90 chaperone complex in R-mediated disease resistance in plants and Nod1-mediated innate immune response in mammals. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.