4.5 Article

A Conserved Puccinia striiformis Protein Interacts with Wheat NPR1 and Reduces Induction of Pathogenesis-Related Genes in Response to Pathogens

期刊

MOLECULAR PLANT-MICROBE INTERACTIONS
卷 29, 期 12, 页码 977-989

出版社

AMER PHYTOPATHOLOGICAL SOC
DOI: 10.1094/MPMI-10-16-0207-R

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资金

  1. Howard Hughes Medical Institute
  2. Gordon and Betty Moore Foundation
  3. United States Department of Agriculture National Institute of Food and Agriculture-NIFA [2011-68002-30029]
  4. Natinoal Science Foundation grant NSF [IOS-1237975]
  5. National Key Basic Research Program of China [2013CB127700]
  6. 111 Project from Ministry of Education of China [B07049]
  7. Direct For Biological Sciences [1237975] Funding Source: National Science Foundation
  8. Division Of Integrative Organismal Systems [1237975] Funding Source: National Science Foundation

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In Arabidopsis, NPR1 is a key transcriptional coregulator of systemic acquired resistance. Upon pathogen challenge, NPR1 translocates from the cytoplasm to the nucleus, in which it interacts with TGA-bZIP transcription factors to activate the expression of several pathogenesis-related (PR) genes. In a screen of a yeast two-hybrid library from wheat leaves infected with Puccinia striiformis f. sp. tritici, we identified a conserved rust protein that interacts with wheat NPR1 and named it PNPi (for Puccinia NPR1 interactor). PNPi interacts with the NPR1/NIIV11-like domain of NPR1 via its C-terminal DPBB_1 domain. Using bimolecular fluorescence complementation assays, we detected the interaction between PNPi and wheat NPR1 in the nucleus of Nicotiana benthamiana protoplasts. A yeast three -hybrid assay showed that PNPi interaction with NPR1 competes with the interaction between wheat NPR1 and TGA2.2. In barley transgenic lines overexpressing PNPi, we observed reduced induction of multiple PR genes in the region adjacent to Pseudomonas syringae pv. tomato DC3000 infection. Based on these results, we hypothesize that PNPi has a role in manipulating wheat defense response via its interactions with NPR1.

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