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Screening of Wheat (Triticum aestivum) Thaumatin-like Protein TaTLP1 Interacting Proteins and Verification of Its Interaction with TaGF14 |
SHEN Song-Song1, FENG Yan1, MENG Lin-Shuo1, WANG Fei1, CUI Zhong-Chi1, MA Qiu-Ying1, LIU Da-Qun1, MA Li-Song2*, WANG Hai-Yan1* |
1 College of Plant Protection/Technological Innovation Center for Biological Control of Crop Diseases and Insect Pests of Hebei Province, Hebei Agricultural University, Baoding 071001, China; 2 College of Horticulture, Hebei Agricultural University, Baoding 071001, China |
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Abstract Thaumatin-like protein (TLP) belongs to pathogenesis-related proteins (PRPs), which plays an important role in plant resistance to biotic stresses and abiotic stress. Earlier studies have reported that TaTLP1 involved in wheat (Triticum aestivum) defense in response to Puccinia triticina (Pt). To further analyze the resistance mechanism of TaTLP1, in this study, GST-pull down and yeast two hybrid (Y2H) assays were conducted to identify the interacting proteins of TaTLP1 in wheat. 14-3-3-like protein (TaGF14) as a candidate interactor of TaTLP1 was identified by both techniques. The interaction between TaTLP1 and TaGF14 was confirmed by Y2H and co-localization. qPCR analysis showed that TaTLP1 and TaGF14 exhibited the similar expression profiles and were highly induced in the early stage of leaf rust infection. Moreover, the expression levels of both genes in the incompatible interaction were higher than that in the compatible interaction. The subcellular localization study showed that TaGF14 was localized in the nucleus. Further characteristic analysis of TaGF14 showed that it might have potential disease resistance function. This study provides a basis for further study on the molecular mechanism of TaTLP1 and participating in the defense response of wheat against leaf rust and exploring more disease resistance genes in the host and provides more excellent disease resistance resources for developing cultivated wheat resistant varieties.
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Received: 15 April 2022
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Corresponding Authors:
*lisong.ma@anu.edu.au; ndwanghaiyan@163.com
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