Journal Article

A novel plant protein-disulfide isomerase participates in resistance response against the TYLCV in tomato

Li, Tong, Xing, Guo-Ming, Li, Sen, Wang, Ya-Hui, Huang, Ying, Xu, Zhi-Sheng, Sun, Sheng, Xiong, Ai-Sheng, Liu, Jie-Xia

2020

Overview

Main conclusion Overexpression or silencing of the SlPDI could increase plants resistance or sensitivity to TYLCV through enhancing or reducing the plant’s antioxidant capacity. Tomato yellow leaf curl virus (TYLCV), a plant virus that could infect a variety of crops, is particularly destructive to tomato growth. Protein disulfide isomerase (PDI) is a member of the thioredoxin (Trx) superfamily, is capable of catalyzing the formation and heterogeneity of protein disulfide bonds and inhibiting the aggregation of misfolded proteins. Studies have shown that PDI plays important roles in plant response to abiotic stress, there is no research report on the function of PDI in response to biotic stress, especially TYLCV infection. Here, we identified a tomato PDI gene, SlPDI , was involved in regulating tomato plants resistance to TYLCV. Subcellular localization results showed that SlPDI was located at the endoplasmic reticulum (ER), and its location remained unchanged after infection with TYLCV virus. Overexpression or silencing of SlPDI could increase plants resistance or sensitivity to TYLCV. Transgenic plants that overexpressing SlPDI exhibit enhanced antioxidant activity evidenced by lower hydrogen peroxide (H 2 O 2 ) level and higher activity of superoxide dismutase (SOD) and peroxidase (POD) in comparison with WT plants, after infected by TYLCV. Moreover, the SlPDI- silencing plants showed opposite results. The promoter analyzes result showed that SlPDI was involved in response to salicylic acid (SA), and our experimental results also showed that the expression level of SlPDI was induced by SA. Taken together, our results indicated that SlPDI could regulate plant resistance to TYLCV through enhancing the protein folding function of ER and promoting the synthesis and conformation of antioxidant-related proteins.

• Publisher: Springer Berlin Heidelberg,Springer Nature B.V
• Subject: abiotic stress / Agriculture / Amino Acid Sequence / antioxidant activity / Antioxidants / Antioxidants - metabolism / Begomovirus - physiology / Biomedical and Life Sciences / biotic stress / Disease Resistance / Disulfide bonds / disulfides / Ecology / Endoplasmic reticulum / Forestry / Gene Expression Regulation, Plant / Gene Silencing / genes / Heterogeneity / Hydrogen peroxide / Leaf-curl / Life Sciences / Localization / Lycopersicon esculentum - enzymology / Lycopersicon esculentum - genetics / Lycopersicon esculentum - virology / Models, Biological / Original Article / Oxidative Stress / Peroxidase / Plant diseases / Plant Diseases - virology / Plant Proteins - chemistry / Plant Proteins - genetics / Plant Proteins - metabolism / Plant resistance / plant response / Plant Sciences / Plant virus diseases / Plant viruses / Plants, Genetically Modified / Promoter Regions, Genetic - genetics / Protein disulfide-isomerase / Protein Disulfide-Isomerases - chemistry / Protein Disulfide-Isomerases - genetics / Protein Disulfide-Isomerases - metabolism / Protein Domains / Protein folding / Proteins / Salicylic acid / Sensitivity enhancement / Subcellular Fractions - metabolism / Superoxide dismutase / Thioredoxin / thioredoxins / Tomato yellow leaf curl virus / Tomatoes / Transcription, Genetic / Transgenic plants / Viruses / Yellow leaf