scholarly journals Phosphorylation of an ERF Transcription Factor by Arabidopsis MPK3/MPK6 Regulates Plant Defense Gene Induction and Fungal Resistance

2013 ◽  
Vol 25 (3) ◽  
pp. 1126-1142 ◽  
Author(s):  
Xiangzong Meng ◽  
Juan Xu ◽  
Yunxia He ◽  
Kwang-Yeol Yang ◽  
Breanne Mordorski ◽  
...  
Author(s):  
Zi-Hui Zhang ◽  
Jinghao Jin ◽  
Gui-Lin Sheng ◽  
Yu-Ping Xing ◽  
Wang Liu ◽  
...  

Small cysteine-rich (SCR) proteins including fungal avirulence proteins play important roles in the pathogen-plant interactions. SCR protein-encoding genes have been discovered in the genomes of Phytophthora pathogens, but their functions during the pathogenesis remain obscure. Here, we report the characterization of one Phytophthora capsici SCR protein, namely SCR82 with similarity to Phytophthora cactorum phytotoxic protein PcF. The scr82 gene has 10 allelic sequences in the P. capsici population. Homologues of SCR82 were not identified in fungi or other organisms but in Phytophthora relative species. Initially scr82 was weakly expressed during the mycelium, sporangium and zoospore stages, but quickly upregulated when the infection initiated. Both ectopic expression of SCR82 and recombinant yeast-expressed protein (rSCR82) caused cell death on tomato leaves. Upon treatment, rSCR82 induced plant defense responses including the induction of defense gene expression, reactive oxygen species burst and callose deposition. Knockout of scr82 in P. capsici by CRISPR/Cas9 severely impaired its virulence on host plants and reduced significantly its resistance againstoxidative stress. Inversely, its overexpression increased the pathogen’s virulence and tolerance to oxidative stress. Our results collectively demonstrate that SCR82 functions as both an important virulence factor and plant defense elicitor, which is conserved across Phytophthora species.


2019 ◽  
Vol 274 ◽  
pp. 368-375 ◽  
Author(s):  
Qiang Huang ◽  
Meihong Sun ◽  
Tingpan Yuan ◽  
Yu Wang ◽  
Min Shi ◽  
...  

1986 ◽  
Vol 6 (5) ◽  
pp. 1615-1623
Author(s):  
J N Bell ◽  
T B Ryder ◽  
V P Wingate ◽  
J A Bailey ◽  
C J Lamb

Phenylalanine ammonia-lyase and chalcone synthase catalyze the first reaction of phenylpropanoid biosynthesis and the first reaction of a branch pathway specific for flavonoid-isoflavonoid biosynthesis, respectively. These enzymes are key control elements in the synthesis of kievitone, phaseollin, and related isoflavonoid-derived phytoalexins. RNA blot hybridization with 32P-labeled cDNA sequences was used to demonstrate marked accumulation of phenylalanine ammonia-lyase and chalcone synthase mRNAs in excision-wounded hypocotyls of Phaseolus vulgaris L. (dwarf French bean) and during race-cultivar-specific interactions between hypocotyls of P. vulgaris and the partially biotrophic fungus Colletotrichum lindemuthianum, the causal agent of anthracnose. In an incompatible interaction (host resistant), early concomitant accumulation of phenylalanine ammonia-lyase and chalcone synthase mRNAs, localized mainly but not entirely in tissue adjacent to the site of infection, was observed prior to the onset of phytoalexin accumulation and expression of localized, hypersensitive resistance. In contrast, in a compatible interaction (host susceptible) there was no early accumulation of these transcripts; instead, there was a delayed widespread response associated with phytoalexin accumulation during attempted lesion limitation. Two-dimensional gel electrophoresis of [35S]methionine-labeled polypeptides synthesized in vitro by translation of isolated polysomal RNA demonstrated stimulation of the synthesis of characteristic sets of phenylalanine ammonia-lyase and chalcone synthase isopolypeptides in directly infected tissue and distant, hitherto uninfected tissue in both compatible and incompatible interactions. Our data show that specific accumulation of plant defense gene transcripts is a key early component in the sequence of events leading to expression of defense responses in wounded tissue and in infected tissue during race-cultivar-specific interactions and that an elicitation signal is transmitted intercellularly in response to infection.


1990 ◽  
Vol 8 (9) ◽  
pp. 845-848 ◽  
Author(s):  
Peter W. Doerner ◽  
Bruce Stermer ◽  
Jürg Schmid ◽  
Richard A. Dixon ◽  
Christopher J. Lamb

Sign in / Sign up

Export Citation Format

Share Document