Verticillium dahliae effector VDAL protects MYB6 from degradation by interacting with PUB25 and PUB26 E3 ligases to enhance Verticillium wilt resistance

2021 ◽  
Author(s):  
Aifang Ma ◽  
Dingpeng Zhang ◽  
Guangxing Wang ◽  
Kai Wang ◽  
Zhen Li ◽  
...  
Keyword(s):  
Disease Resistance ◽  
Verticillium Wilt ◽  
Verticillium Dahliae ◽  
Plant Resistance ◽  
Plant Disease Resistance ◽  
Plant Disease ◽  
Wilt Resistance ◽  
E3 Ligases ◽  
Verticillium Wilt Resistance

Abstract Verticillium wilt is a severe plant disease that causes massive losses in multiple crops. Increasing the plant resistance to Verticillium wilt is a critical challenge worldwide. Here, we report that the hemibiotrophic Verticillium dahliae-secreted Asp f2-like protein VDAL causes leaf wilting when applied to cotton leaves in vitro but enhances the resistance to V. dahliae when overexpressed in Arabidopsis or cotton without affecting the plant growth and development. VDAL protein interacts with Arabidopsis E3 ligases plant U-box 25 (PUB25) and PUB26 and is ubiquitinated by PUBs in vitro. However, VDAL is not degraded by PUB25 or PUB26 in planta. Besides, the pub25 pub26 double mutant shows higher resistance to V. dahliae than the wild-type. PUBs interact with the transcription factor MYB6 in a yeast two-hybrid screen. MYB6 promotes plant resistance to Verticillium wilt while PUBs ubiquitinate MYB6 and mediate its degradation. VDAL competes with MYB6 for binding to PUBs, and the role of VDAL in increasing Verticillium wilt resistance depends on MYB6. Taken together, these results suggest that plants evolute a strategy to utilize the invaded effector protein VDAL to resist the V. dahliae infection without causing a hypersensitive response (HR); alternatively, hemibiotrophic pathogens may use some effectors to keep plant cells alive during its infection in order to take nutrients from host cells. This study provides the molecular mechanism for plants increasing disease resistance when overexpressing some effector proteins without inducing HR, and may promote searching for more genes from pathogenic fungi or bacteria to engineer plant disease resistance.

scholarly journals Verticillium dahliae effector VDAL protects MYB6 from degradation by interacting with PUB25/26 E3 ligases for enhancing Verticillium wilt resistance in Arabidopsis

2021 ◽  
Author(s):  
Zhizhong Gong ◽  
Junsheng Qi ◽  
Aifang Ma ◽  
Dingpeng Zhang ◽  
Guangxing Wang ◽  
...  
Keyword(s):  
Disease Resistance ◽  
Verticillium Wilt ◽  
Verticillium Dahliae ◽  
Plant Resistance ◽  
Plant Disease Resistance ◽  
Plant Disease ◽  
Effector Proteins ◽  
In Planta ◽  
E3 Ligases

Verticillium wilt is a severe plant disease, increasing the plant resistance to this disease is a critical challenge worldwide. Here, we report that the Verticillium dahliae (V. dahliae)-secreted Aspf2-like protein VDAL causes leaf wilting when applied to cotton leaves in vitro, but enhances the resistance to V. dahliae when overexpressed in Arabidopsis or cotton. VDAL interacts with Arabidopsis E3 ligases PUB25 and PUB26 (PUBs) and is ubiquitinated by PUBs in vitro. However, VDAL is not degraded by PUBs in planta. Besides, the pub25 pub26 shows higher resistance to V. dahliae than the wild type. PUBs interact with the transcription factor MYB6 in a yeast two-hybrid screen. MYB6 promotes plant resistance to Verticillium wilt while PUBs ubiquitinate MYB6 and mediate its degradation. VDAL competes with MYB6 for binding to PUBs, and the role of VDAL in increasing wilt disease depends on MYB6. These results suggest that plants evolute a strategy to utilize the invaded effector protein VDAL to resist the V. dahliae infection without causing a hypersensitive response. This study provides the molecular mechanism for plants increasing disease resistance when overexpressing some effector proteins, and may promote searching for more genes from pathogenic fungi or bacteria to engineer plant disease resistance.

SCREENING SWEET AND HOT PEPPERS FOR VERTICILLIUM WILT RESISTANCE

1962 ◽  
Vol 42 (3) ◽  
pp. 515-520 ◽  
Author(s):  
G. E. Woolliest ◽  
L. G. Denby ◽  
A. S. F. Hanson
Keyword(s):  
Capsicum Annuum ◽  
Verticillium Wilt ◽  
Verticillium Dahliae ◽  
Wilt Resistance ◽  
Verticillium Wilt Resistance ◽  
Local Isolate ◽  
Hot Peppers

A total of 456 varieties and strains of sweet and hot peppers (Capsicum annuum) was screened for resistance to Verticillium wilt by inoculating the roots of seedling plants in a suspension of a local isolate of Verticillium dahliae that had been found to cause severe wilt in susceptible pepper varieties. No accession proved immune; 100 per cent wilt developed in 361, and 70 to 95 per cent in 93. In one accession wilt affected 68 per cent of the plants and in another 46 per cent, the lowest rate of infection that occurred.

scholarly journals Biosynthesis of cabbage phytoalexins from indole glucosinolate

2017 ◽  
Vol 114 (8) ◽  
pp. 1910-1915 ◽  
Author(s):  
Andrew P. Klein ◽  
Elizabeth S. Sattely
Keyword(s):  
Disease Resistance ◽  
Plant Disease Resistance ◽  
Plant Disease ◽  
Biochemical Characterization ◽  
Edible Plant ◽  
Crop Species ◽  
Important Pathway ◽  
Indole Glucosinolate ◽  
The Impact

Brassicacrop species are prolific producers of indole–sulfur phytoalexins that are thought to have an important role in plant disease resistance. These molecules are conspicuously absent in the model plantArabidopsis thaliana, and little is known about the enzymatic steps that assemble the key precursor brassinin. Here, we report the minimum set of biosynthetic genes required to generate cruciferous phytoalexins starting from the well-studied glucosinolate pathway. In vitro biochemical characterization revealed an additional role for the previously described carbon–sulfur lyase SUR1 in processing cysteine–isothiocyanate conjugates, as well as theS-methyltransferase DTCMT that methylates the resulting dithiocarbamate, together completing a pathway to brassinin. Additionally, the β-glucosidase BABG that is present inBrassica rapabut absent inArabidopsiswas shown to act as a myrosinase and may be a determinant of plants that synthesize phytoalexins from indole glucosinolate. Transient expression of the entire pathway inNicotiana benthamianayields brassinin, demonstrating that the biosynthesis of indole–sulfur phytoalexins can be engineered into noncruciferous plants. The identification of these biosynthetic enzymes and the heterologous reconstitution of the indole–sulfur phytoalexin pathway sheds light on an important pathway in an edible plant and opens the door to using metabolic engineering to systematically quantify the impact of cruciferous phytoalexins on plant disease resistance and human health.

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