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A disulphide isomerase gene (PDI-V) from Haynaldia villosa contributes to powdery mildew resistance in common wheat
In this study, we report the contribution of a PDI-like gene from wheat wild relative Haynaldia villosa in combating powdery mildew. PDI-V protein contains two conserved thioredoxin (TRX) active domains (a and a′) and an inactive domain (b). PDI-V interacted with E3 ligase CMPG1-V protein, which is...
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Published in: | Scientific reports 2016-04, Vol.6 (1), p.24227-24227, Article 24227 |
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Main Authors: | , , , , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | In this study, we report the contribution of a
PDI-like
gene from wheat wild relative
Haynaldia villosa
in combating powdery mildew. PDI-V protein contains two conserved thioredoxin (TRX) active domains (a and a′) and an inactive domain (b). PDI-V interacted with E3 ligase CMPG1-V protein, which is a positive regulator of powdery mildew response. PDI-V was mono-ubiquitinated by CMPG1-V without degradation being detected.
PDI-V
was located on
H. villosa
chromosome 5V and encoded for a protein located in the endoplasmic reticulum.
Bgt
infection in leaves of
H. villosa
induced
PDI-V
expression. Virus induced gene silencing of
PDIs
in a
T. durum-H. villosa
amphiploid compromised the resistance. Single cell transient over-expression of
PDI-V
or a truncated version containing the active TXR domain a decreased the haustorial index in moderately susceptible wheat cultivar Yangmai 158. Stable transgenic lines over-expressing
PDI-V
in Yangmai 158 displayed improved powdery mildew resistance at both the seedling and adult stages. By contrast over-expression of point-mutated
PDI-V
C57A
did not increase the level of resistance in Yangmai 158. The above results indicate a pivotal role of
PDI-V
in powdery mildew resistance and showed that conserved TRX domain a is critical for its function. |
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ISSN: | 2045-2322 2045-2322 |
DOI: | 10.1038/srep24227 |