SAMDC3 enhances resistance to Barley stripe mosaic virus by promoting the ubiquitination and proteasomal degradation of viral gamma b protein

文献类型: 外文期刊

第一作者: Li, Zhaolei

作者: Li, Zhaolei;Yang, Xinxin;Li, Wenli;Wen, Zhiyan;Duan, Jiangning;Jiang, Zhihao;Zhang, Dingliang;Xie, Xialin;Wang, Xueting;Li, Dawei;Zhang, Yongliang;Li, Zhaolei;Yang, Xinxin;Li, Wenli;Wen, Zhiyan;Duan, Jiangning;Jiang, Zhihao;Zhang, Dingliang;Xie, Xialin;Wang, Xueting;Li, Dawei;Zhang, Yongliang;Li, Fangfang

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关键词: Barley stripe mosaic virus; degradation; interaction; Nicotiana benthamiana; nonlysine ubiquitination; S-adenosylmethionine decarboxylase 3; Triticum aestivum; gamma b

期刊名称:NEW PHYTOLOGIST ( 影响因子:10.323; 五年影响因子:10.768 )

ISSN: 0028-646X

年卷期: 2022 年 234 卷 2 期

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收录情况: SCI

摘要: Posttranslational modifications (PTMs) play important roles in virus-host interplay. We previously demonstrated that Barley stripe mosaic virus (BSMV) gamma b protein is phosphorylated by different host kinases to support or impede viral infection. However, whether and how other types of PTMs participate in BSMV infection remains to be explored. Here, we report that S-adenosylmethionine decarboxylase 3 (SAMDC3) from Nicotiana benthamiana or wheat (Triticum aestivum) interacts with gamma b. BSMV infection induced SAMDC3 expression. Overexpression of SAMDC3 led to the destabilization of gamma b and reduction in viral infectivity, whereas knocking out NbSAMDC3 increased susceptibility to BSMV. NbSAMDC3 positively regulated the 26S proteasome-mediated degradation of gamma b via its PEST domain. Further mechanistic studies revealed that gamma b can be ubiquitinated in planta and that NbSAMDC3 promotes the proteasomal degradation of gamma b by increasing gamma b ubiquitination. We also found evidence that ubiquitination occurs at nonlysine residues (Ser-133 and Cys-144) within gamma b. Together, our results provide a function for SAMDC3 in defence against BSMV infection through targeting of gamma b abundance, which contributes to our understanding of how a plant host deploys the ubiquitin-proteasome system to mount defences against viral infections.

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