Journal
JOURNAL OF EXPERIMENTAL BOTANY
Volume 65, Issue 17, Pages 4807-4820Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jxb/eru241
Keywords
Bimolecular fluorescence complementation; immuno-localization; Puccinia striiformis f. sp tritici; qRT-PCR; SNARE; vesicle-mediated resistance; virus-induced gene silencing; wheat; yeast two-hybrid
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Funding
- National Basic Research Program of China [2013CB127700]
- earmarked fund for China Agriculture Research System [CARS-3-1-11]
- Ministry of Education of China [B07049]
- HHMI
- GBMF
- USDA-NIFA [2011-68002-30029]
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Subcellular localisation of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) and their ability to form SNARE complexes are critical for determining the specificity of vesicle fusion. NPSN11, a Novel Plant SNARE (NPSN) gene, has been reported to be involved in the delivery of cell wall precursors to the newly formed cell plate during cytokinesis. However, functions of NPSN genes in plant-pathogen interactions are largely unknown. In this study, we cloned and characterized three NPSN genes (TaNPSN11, TaNPSN12, and TaNPSN13) and three plant defence-related SNARE homologues (TaSYP132, TaSNAP34, and TaMEMB12). TaSYP132 showed a highly specific interaction with TaNPSN11 in both yeast two-hybrid and bimolecular fluorescence complementation (BiFC) assays. We hypothesize that this interaction may indicate a partnership in vesicle trafficking. Expressions of the three TaNPSNs and TaSYP132 were differentially induced in wheat leaves when challenged by Puccinia striiformis f. sp. tritici (Pst). In virus-induced gene silencing (VIGS) assays, resistance of wheat (Triticum aestivum) cultivar Xingzi9104 to the Pst avirulent race CYR23 was reduced by knocking down TaNPSN11, TaNPSN13 and TaSYP132, but not TaNPSN12, implying diversified functions of these wheat SNARE homologues in prevention of Pst infection and hyphal elongation. Immuno-localization results showed that TaNPSN11 or its structural homologues were mainly distributed in vesicle structures near cell membrane toward Pst hypha. Taken together, our data suggests a role of TaNPSN11 in vesicle-mediated resistance to stripe rust.
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