PpHOS1, a RING E3 ubiquitin ligase, interacts with PpWRKY22 in the BABA-induced priming defense of peach fruit against Rhizopus stolonifer
PpHOS1, a RING E3 ubiquitin ligase, interacts with PpWRKY22 in the BABA-induced priming defense of peach fruit against Rhizopus stolonifer
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PpHOS1 是一种 RING E3 泛素连接酶，在 BABA 诱导的桃果实针对匍匐根霉的启动防御中与 PpWRKY22 相互作用
DOI：
10.1016/j.postharvbio.2019.111029
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发表时间：
2020-01-01
影响因子：
7
通讯作者：
Wang, Kaituo
中科院分区：
文献类型：
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作者：
Li, Chunhong;Wang, Jing;Wang, Kaituo
氨基丁酸（BABA）诱导的引发抗性是一种经济有效的保护采后果实免受病原菌感染的策略。然而，桃中E3泛素连接酶、WRKY转录因子和引发防御的交联作用研究仍然很少。在本研究中，50 mmol L-1 BABA至少可以诱导桃果实的抗病性，引发H2 O2含量的积累，随后根霉stolonifer培养，伴随着抑制发病率和病变直径在20 ℃下培养。同时，通过对桃转录组和蛋白质组数据库中差异表达基因和蛋白质的分析和总结，分别鉴定了一个WRKY TF（PpWRKY 22）和一个E3泛素连接酶（PpHOS 1）。此外，PpWRKY 22，一个IIe组WRKY TF，和PpHOS 1，一个RING型E3泛素连接酶，推定的特性进行了阐述。PpWRKY 22和PpHOS 1基因在桃果实对炭疽菌引发抗性中表达上调。stolonifer，和两个核定位的蛋白质在体内物理相互作用。综上所述，这些发现为E3泛素连接酶和WRKY TF在引发抗性中的功能联系带来了新的见解，并为提高桃的抗病性提供了新的视角。
The priming resistance induced by beta-aminobutyric acid (BABA) is a cost-effective strategy to protect postharvest fruit from pathogen infection. The cross-linking underlying E3 ubiquitin ligases, WRKY transcription factors (TFs) and priming defense in peaches, however, remains poorly researched. In the present study, 50 mmol L-1 BABA could induce disease resistance at least by priming peach fruit for an accumulation in H2O2 content following subsequent Rhizopus stolonifer incubation, accompanied by a suppression of the disease incidence and lesion diameter during the incubation at 20 degrees C. Meanwhile, a WRKY TF (PpWRKY22) and an E3 ubiquitin ligase (PpHOS1) were identified specifically based on analysis and summarization of the differentially expressed genes and proteins in the transcriptome and proteome database of peaches, respectively. Moreover, the putative characterization of PpWRKY22, a Group IIe WRKY TF, and PpHOS1, a RING-type E3 ubiquitin ligase, was expounded. The expression of PpWRKY22 and PpHOS1 was up-regulated in the priming resistance of peach fruit against R. stolonifer, and the two nucleus-localized proteins physically interacted in vivo. Taken together, these findings bring new insights into the functional link between E3 ubiquitin ligases and WRKY TFs in priming resistance, and they enable new perspectives on enhancing the disease resistance of peaches.