Solution structure of the Magnaporthe oryzae avirulence protein AvrPiz-t
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Plants have evolved two major layers of defense mechanisms against invasion by diverse pathogens. When host membranes are exposed to pathogens, plants use extracellular surface receptors to identify pathogen-associated molecular patterns (PAMPs) and initiate so-called PAMP-triggered immunity (PTI) (Chisholm et al. 2006). Once pathogens gain hold in plants by suppressing this primary defense, plants express cytoplasmic resistance proteins that recognize pathogen-derived effector proteins and mount a more specialized defense mechanism referred to as effector-triggered immunity (ETI, Chisholm et al. 2006). To enable parasitism, pathogens usually use an arsenal of effector proteins that are delivered into plant cells to exert their primary function of interfering with the host immunity (Abramovitch et al. 2006; Feng et al. 2012; Wilton et al. 2010). However, effector proteins in some cases act as traitors by inducing effector-triggered immunity; these proteins are often...
KeywordsRice Blast Distance Restraint Chemical Shift Assignment Stable Fragment Side Chain Resonance Assignment
This work was supported by grants from the National Program on Key Basic Research of China (2009CB918600, to J. Z. and M. L.), the National Grand Project for Medicine Innovation (2011ZX09506-001) and the Natural Science Foundation in China (30971878, to B. Z.). We are grateful to Prof. Chunyang Cao and Yan Zhang for valuable suggestions in NMR structure determination. We also thank Dr. Wenyu Wen for her help on H/D exchange experiments.
- Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang J-S, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr Sect D 54:905–921CrossRefGoogle Scholar
- Gunčar G, Wang C-IA, Forwood JK, The T, Catanzariti A-M, Lawrence GJ, Loughlin FE, Mackay JP, Schirra HJ, Anderson PA, Ellis JG, Dodds PN, Kobe B (2007) Adaptive evolution has targeted the C-terminal domain of the RXLR effectors of plant pathogenic oomycetes. Plant Cell 19:2898–2912CrossRefGoogle Scholar
- Li W, Wang B, Wu J, Lu G, Hu Y, Zhang X, Zhang Z, Zhao Q, Feng Q, Zhang H, Wang Z, Wang G, Hna B, Wang Z, Zhou B (2009) The Magnaporthe oryzae avirulence gene AvrPiz-t encodes a predicted secreted protein that triggers the immunity in rice mediated by the blast resistance gene Piz-t. Mol Plant Microbe Interact 22:411–420CrossRefGoogle Scholar
- Li P, Dong B, Zhou H, Zhou B (2012) Functional analysis of cysteine residues of the Magnaporthe oryzae avirulence protein AvrPiz-t. Acta Phytopathologica Sinica 42:474–479Google Scholar
- Park C-H, Chen S, Shirsekar G, Zhou B, Khang CH, Songkumarn P, Ning Y, Bellizzi M, Valent B, Wang G-L (2012) The Magnaporthe oryzae effector AvrPiz-t targets the RING E3 ubiquitin ligase APIP6 to suppress pathogen-associated molecular pattern-triggered immunity in rice. Plant Cell. doi: 10.1105/tpc.112.105429
- Wishart DS, Sykes BD (1994) The 13C Chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180Google Scholar
- Zhou B, Qu S, Liu G, Dolan M, Sakai H, Lu G, Bellizzi M, Wang G-L (2006) The eight amino-acid differences within three leucine-rich repeats between Pi2 and Piz-t resistance proteins determine the resistance specificity to Magnaporthe grisea. Mol Plant Microbe Interact 19:1216–1228Google Scholar