Arabidopsis 14‐3‐3 lambda is a positive regulator of RPW8‐mediated disease resistance
Open Access
- 28 October 2009
- journal article
- Published by Wiley in The Plant Journal
- Vol. 60 (3), 539-550
- https://doi.org/10.1111/j.1365-313x.2009.03978.x
Abstract
The RPW8 locus from Arabidopsis thaliana Ms-0 includes two functional paralogous genes (RPW8.1 and RPW8.2) and confers broad-spectrum resistance via the salicylic acid-dependent signaling pathway to the biotrophic fungal pathogens Golovinomyces spp. that cause powdery mildew diseases on multiple plant species. To identify proteins involved in regulation of the RPW8 protein function, a yeast two-hybrid screen was performed using RPW8.2 as bait. The 14-3-3 isoform lambda (designated GF14?) was identified as a potential RPW8.2 interactor. The RPW8.2–GF14? interaction was specific and engaged the C-terminal domain of RPW8.2, which was confirmed by pulldown assays. The physiological impact of the interaction was revealed by knocking down GF14? by T-DNA insertion, which compromised basal and RPW8-mediated resistance to powdery mildew. In addition, over-expression of GF14? resulted in hypersensitive response-like cell death and enhanced resistance to powdery mildew via the salicylic acid-dependent signaling pathway. The results from this study suggest that GF14? may positively regulate the RPW8.2 resistance function and play a role in enhancing basal resistance in ArabidopsisKeywords
This publication has 67 references indexed in Scilit:
- An Essential Role for 14-3-3 Proteins in Brassinosteroid Signal Transduction in ArabidopsisDevelopmental Cell, 2007
- Characterization of zinc finger protein 496 that interacts with Jumonji/Jarid2FEBS Letters, 2007
- Modifications to the Arabidopsis Defense Proteome Occur Prior to Significant Transcriptional Change in Response to Inoculation withPseudomonas syringaePlant Physiology, 2006
- C‐terminal binding: An expanded repertoire and function of 14‐3‐3 proteinsFEBS Letters, 2006
- Phytochrome-Specific Type 5 Phosphatase Controls Light Signal Flux by Enhancing Phytochrome Stability and Affinity for a Signal TransducerCell, 2005
- Members of 14-3-3 protein isoforms interacting with the resistance gene product N and the elicitor of Tobacco mosaic virusJournal of General Plant Pathology, 2004
- Association between molecular markers and blast resistance in an advanced backcross population of riceTheoretical and Applied Genetics, 2003
- Forward TransportCell, 2002
- Phosphorylation of Thr-948 at the C Terminus of the Plasma Membrane H+-ATPase Creates a Binding Site for the Regulatory 14-3-3 ProteinTHE PLANT CELL ONLINE, 1999
- 14‐3‐3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform‐specific manner and reduce dephosphorylation of Ser‐543 by endogenous protein phosphatasesFEBS Letters, 1996