ORCID Profile
0000-0001-7813-2415
Current Organisations
University of Rochester
,
CSIRO Black Mountain Laboratories
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Publisher: Cold Spring Harbor Laboratory
Date: 10-09-2023
Publisher: Wiley
Date: 16-11-2017
DOI: 10.1111/MPP.12597
Publisher: Proceedings of the National Academy of Sciences
Date: 23-08-2016
Abstract: Stem rust caused by the fungus Puccinia graminis f. sp. tritici ( Pgt ) remains the major disease threat to wheat production. The Sr33 and Sr50 resistance proteins protect wheat against a broad spectrum of field isolates of Pgt and are closely related to the barley powdery mildew-resistance protein MLA10. Like MLA10, Sr33 and Sr50 possess signaling N-terminal domains that self-associate in planta and initiate cell-death signaling from the cytosol. However, Sr33 induces disease-resistance signaling from the cytosol but not from the nucleus of wheat cells, suggesting cytosolic activation of both cell death and stem rust resistance.
Publisher: Oxford University Press (OUP)
Date: 07-04-2006
Abstract: Limited information is available about the roles of specific WRKY transcription factors in plant defense. We report physical and functional interactions between structurally related and pathogen-induced WRKY18, WRKY40, and WRKY60 transcription factors in Arabidopsis thaliana. The three WRKY proteins formed both homocomplexes and heterocomplexes and DNA binding activities were significantly shifted depending on which WRKY proteins were present in these complexes. Single WRKY mutants exhibited no or small alterations in response to the hemibiotrophic bacterial pathogen Pseudomonas syringae and the necrotrophic fungal pathogen Botrytis cinerea. However, wrky18 wrky40 and wrky18 wrky60 double mutants and the wrky18 wrky40 wrky60 triple mutant were substantially more resistant to P. syringae but more susceptible to B. cinerea than wild-type plants. Thus, the three WRKY proteins have partially redundant roles in plant responses to the two distinct types of pathogens, with WRKY18 playing a more important role than the other two. The contrasting responses of these WRKY mutants to the two pathogens correlated with opposite effects on pathogen-induced expression of salicylic acid–regulated PATHOGENESIS-RELATED1 and jasmonic acid–regulated PDF1.2. While constitutive expression of WRKY18 enhanced resistance to P. syringae, its coexpression with WRKY40 or WRKY60 made plants more susceptible to both P. syringae and B. cinerea. These results indicate that the three WRKY proteins interact both physically and functionally in a complex pattern of overlapping, antagonistic, and distinct roles in plant responses to different types of microbial pathogens.
Publisher: Springer Science and Business Media LLC
Date: 06-09-2023
Publisher: Wiley
Date: 23-02-2022
DOI: 10.1111/NPH.18011
Abstract: Pathogen effectors are crucial players during plant colonisation and infection. Plant resistance mostly relies on effector recognition to activate defence responses. Understanding how effector proteins escape from plant surveillance is important for plant breeding and resistance deployment. Here we examined the role of genetic ersity of the stem rust ( Puccinia graminis f. sp. tritici ( Pgt )) AvrSr50 gene in determining recognition by the corresponding wheat Sr50 resistance gene. We solved the crystal structure of a natural variant of AvrSr50 and used site‐directed mutagenesis and transient expression assays to dissect the molecular mechanisms explaining gain of virulence. We report that AvrSr50 can escape recognition by Sr50 through different mechanisms including DNA insertion, stop codon loss or by amino‐acid variation involving a single substitution of the AvrSr50 surface‐exposed residue Q121. We also report structural homology of AvrSr50 to cupin superfamily members and carbohydrate‐binding modules indicating a potential role in binding sugar moieties. This study identifies key polymorphic sites present in AvrSr50 alleles from natural stem rust populations that play important roles to escape from Sr50 recognition. This constitutes an important step to better understand Pgt effector evolution and to monitor AvrSr50 variants in natural rust populations.
Publisher: Oxford University Press (OUP)
Date: 2016
DOI: 10.1105/TPC.15.00303
No related grants have been discovered for Chunhong Chen.