TaClpS1, negatively regulates wheat resistance against Puccinia striiformis f. sp. tritici
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RESEARCH ARTICLE
Open Access
TaClpS1, negatively regulates wheat resistance against Puccinia striiformis f. sp. tritici Qian Yang†, Md Ashraful Islam†, Kunyan Cai, Shuxin Tian, Yan Liu, Zhensheng Kang* and Jun Guo*
Abstract Background: The degradation of intracellular proteins plays an essential role in plant responses to stressful environments. ClpS1 and E3 ubiquitin ligase function as adaptors for selecting target substrates in caseinolytic peptidase (Clp) proteases pathways and the 26S proteasome system, respectively. Currently, the role of E3 ubiquitin ligase in the plant immune response to pathogens is well defined. However, the role of ClpS1 in the plant immune response to pathogens remains unknown. Results: Here, wheat (Triticum aestivum) ClpS1 (TaClpS1) was studied and resulted to encode 161 amino acids, containing a conserved ClpS domain and a chloroplast transit peptide (1–32 aa). TaClpS1 was found to be specifically localized in the chloroplast when expressed transiently in wheat protoplasts. The transcript level of TaClpS1 in wheat was significantly induced during infection by Puccinia striiformis f. sp. tritici (Pst). Knockdown of TaClpS1 via virus-induced gene silencing (VIGS) resulted in an increase in wheat resistance against Pst, accompanied by an increase in the hypersensitive response (HR), accumulation of reactive oxygen species (ROS) and expression of TaPR1 and TaPR2, and a reduction in the number of haustoria, length of infection hypha and infection area of Pst. Furthermore, heterologous expression of TaClpS1 in Nicotiana benthamiana enhanced the infection by Phytophthora parasitica. Conclusions: These results suggest that TaClpS1 negatively regulates the resistance of wheat to Pst. Keywords: TaClpS1, Puccinia striiformis f. sp. tritici, Wheat, Virus-induced gene silencing, Heterologous expression
Background To ensure their survival in nature, plants must evoke many complicated mechanisms to cope with biotic and abiotic stresses. An increasing number of studies reveal the essential role that the degradation of intracellular proteins plays in plant responses to stressful environments. The protein degradation pathways include ubiquitin–26S proteasome system (UPS) and caseinolytic peptidase (Clp) proteases [1, 2]. The two protein
* Correspondence: [email protected]; [email protected] † Qian Yang and Md Ashraful Islam contributed equally to this work. State Key Laboratory of Crop Stress Biology for Arid Areas, College of Plant Protection, Northwest A&F University, Yangling 712100, Shaanxi, P. R. China
degradation machineries both consist of large multisubunit proteolytic complexes. The first process in degradation of proteins by UPS is ATP-dependent ubiquitination, which involves the action of at least three main enzymes for selecting target substrates [3]: ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). Studies reveal that ubiquitination during UPS is implicated in many biological processes in plants, including hormone signaling, g
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