Abstract
N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are involved in plant resistance; however, the role of SYP71 in the regulation of plant–pathogen interactions is not well known. In this study, we characterized a plant-specific SNARE in wheat, TaSYP71, which contains a Qc-SNARE domain. Three homologs are localized on chromosome 1AL, 1BL, and 1DL. Using Agrobacterium-mediated transient expression, TaSYP71 was localized to the plasma membrane in Nicotiana benthamiana. Quantitative real-time PCR assays revealed that TaSYP71 homologs was induced by NaCl, H2O2 stress and infection by virulent and avirulent Puccinia striiformis f. sp. tritici (Pst) isolates. Heterologous expression of TaSYP71 in Schizosaccharomyces pombe elevated tolerance to H2O2. Meanwhile, H2O2 scavenging gene (TaCAT) was downregulated in TaSYP71 silenced plants treated by H2O2 compared to that in control, which indicated that TaSYP71 enhanced tolerance to H2O2 stress possibly by influencing the expression of TaCAT to remove the excessive H2O2 accumulation. When TaSYP71 homologs were all silenced in wheat by the virus-induced gene silencing system, wheat plants were more susceptible to Pst, with larger infection area and more haustoria number, but the necrotic area of wheat mesophyll cells were larger, one possible explanation that minor contribution of resistance to Pst was insufficient to hinder pathogen extension when TaSYP71 were silenced, and the necrotic area was enlarged accompanied with the pathogen growth. Of course, later cell death could not be excluded. In addition, the expression of pathogenesis-related genes were down-regulated in TaSYP71 silenced wheat plants. These results together suggest that TaSYP71 play a positive role in wheat defense against Pst.
Highlights
Eukaryotes have evolved a specialized class of proteins, the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), that functions as mediators of vesicle membrane fusion with specific organelles
A cDNA fragment (938 bp) with a SNARE domain was first isolated from the wheat-Puccinia striiformis f. sp. tritici (Pst) incompatible cDNA library constructed by our laboratory
The complete open reading frame (ORF) was obtained from cDNA of wheat cultivar Suwon11 infected by CYR23
Summary
Eukaryotes have evolved a specialized class of proteins, the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), that functions as mediators of vesicle membrane fusion with specific organelles. TaSYP71 Positively Regulated Wheat Resistance hetero-oligomeric complex to mediate membrane fusion between vesicles and target membranes, including vesicles, organelles of the endomembrane system, and the plasma membrane (PM). Based on their positions within the assembled fourhelix bundle, Q-SNAREs can be classified as Qa-SNARE motifs (occupy the syntaxin position), Qb-SNARE (SNAP-25 N-terminal) and Qc-SNARE (SNAP-25 C-terminal) (Bock et al, 2001). Tobacco (N. tabacum) PM SNARE SYP132 has been shown to contribute to defense against bacterial pathogens by mediating the secretion of pathogenesis-related protein 1 (Kalde et al, 2007). Golgi SNARE AtMEMB12 is targeted by miR393b∗ and regulates the exocytosis of an antimicrobial pathogenesis-related protein, PR1 (Zhang et al, 2011). In wheat (Triticum aestivum), knocking down TaNPSN11 (Qb-SNARE) expression reduced the resistance of wheat to an avirulent isolate of Puccinia striiformis f. sp. tritici (Pst) (Wang et al, 2014)
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