Protein sulfenylation contributes to oxidative burst-triggered responses during the interaction between Botrytis cinerea and Nicotiana benthamiana

doi:10.1016/j.jprot.2021.104423

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	Protein sulfenylation contributes to oxidative burst-triggered responses during the interaction between Botrytis cinerea and Nicotiana benthamiana
	Wang, Ying 1; Li, Guangjin 1; Chen, Tong ; Tian, Shiping 1
刊名	JOURNAL OF PROTEOMICS
	2022
卷号	251
关键词	Oxidative stress Protein sulfenylation Reactive oxygen species Sulfenome Botrytis cinerea Nicotiana benthamiana
ISSN号	1874-3919
DOI	10.1016/j.jprot.2021.104423
文献子类	Article
英文摘要	Reactive oxygen species (ROS) play a crucial role as signaling molecules in plant responses to pathogen infection. It is highly reactive with cellular components such as DNA, lipids and proteins, thereby leading to serious oxidative damages. Cysteine residues are sensitive targets of ROS in a post-translational modification known as sulfenylation. However, during plant-pathogen interaction, it is still unclear which specific proteins can be oxidized by ROS and undergo sulfenic modification to regulate the interaction process. Here, we observed a biphasic production of ROS in Nicotiana benthamiana after inoculation with Botrytis cinerea. RT-qPCR results showed that the biphasic increase in ROS production was closely related to the expression of NbRbohA, NbRbohB and NbRbohC. Furthermore, a ROS-dependent sulfenome analysis was performed and finally 183 differentially sulfenylated proteins were identified. Their post-translational sulfenylation modification in response to B. cinerea infection was further confirmed by western blot and mass spectrometry analysis. Virus-induced gene silencing of those genes encoding sulfenylated proteins resulted in reduced resistance to B. cinerea. Taken together, our data demonstrate that B. cinerea infection induces ROS burst in N. benthamiana, which triggers protein sulfenylation to ensure the transduction of ROS signals and further function in plant-pathogen interaction. Significance: Reactive oxygen species (ROS) induced by Botrytis cinerea infection trigger changes in cellular redox status through protein sulfenylation to be involved in plant-pathogen interaction.
学科主题	Biochemical Research Methods
电子版国际标准刊号	1876-7737
出版地	AMSTERDAM
WOS关键词	TANDEM AFFINITY PURIFICATION ; FRUIT SENESCENCE ; ROS ; ETHYLENE ; SUSCEPTIBILITY ; BIOSYNTHESIS ; ACCUMULATION ; INFECTION ; PATHOGENS ; VIRULENCE
WOS研究方向	Science Citation Index Expanded (SCI-EXPANDED)
语种	英语
出版者	ELSEVIER
WOS记录号	WOS:000721676300004
资助机构	National Natural Science Foundation of China [31930086, 32072637] ; Beijing Natural Science Foundation [6212025]
内容类型	期刊论文
源URL	[http://ir.ibcas.ac.cn/handle/2S10CLM1/28798]
专题	中科院北方资源植物重点实验室
作者单位	1.Chinese Acad Sci, Innovat Acad Seed Design, Inst Bot, Key Lab Plant Resources, Beijing 100093, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Wang, Ying,Li, Guangjin,Chen, Tong,et al. Protein sulfenylation contributes to oxidative burst-triggered responses during the interaction between Botrytis cinerea and Nicotiana benthamiana[J]. JOURNAL OF PROTEOMICS,2022,251.
APA	Wang, Ying,Li, Guangjin,Chen, Tong,&Tian, Shiping.(2022).Protein sulfenylation contributes to oxidative burst-triggered responses during the interaction between Botrytis cinerea and Nicotiana benthamiana.JOURNAL OF PROTEOMICS,251.
MLA	Wang, Ying,et al."Protein sulfenylation contributes to oxidative burst-triggered responses during the interaction between Botrytis cinerea and Nicotiana benthamiana".JOURNAL OF PROTEOMICS 251(2022).