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A disulphide isomerase gene (PDI-V) from Haynaldia villosa contributes to powdery mildew resistance in common wheat.

Faheem M, Li Y, Arshad M, Jiangyue C, Jia Z, Wang Z, Xiao J, Wang H, Cao A, Xing L, Yu F, Zhang R, Xie Q, Wang X - Sci Rep (2016)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: The State Key Laboratory of Crop Genetics and Germplasm Enhancement, Cytogenetics Institute, Nanjing Agricultural University/JCIC-MCP, Nanjing, Jiangsu 210095, P.R. China.

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus

Structural features of the PDI-V cDNA sequence and its translation product.(A) Structure deduced from the full-length cDNA sequence of PDI-V. The size of each domain, signal peptide and 3′ and 5′- UTR sizes and position of the ATG and TAG stop codons are shown. (B) Graphical representation of domain organization as provided by the NCBI conserved domain database. (C) Deduced amino acid sequence of PDI-V. Thioredoxin catalytic motifs and ER retention signals are shown in red.
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f1: Structural features of the PDI-V cDNA sequence and its translation product.(A) Structure deduced from the full-length cDNA sequence of PDI-V. The size of each domain, signal peptide and 3′ and 5′- UTR sizes and position of the ATG and TAG stop codons are shown. (B) Graphical representation of domain organization as provided by the NCBI conserved domain database. (C) Deduced amino acid sequence of PDI-V. Thioredoxin catalytic motifs and ER retention signals are shown in red.

Mentions: CMPG1-V positively regulates powdery mildew resistance in common wheat1. To identify proteins interacting with CMPG1-V, a Y2H cDNA library of H. villosa was constructed and used to elucidate the resistance pathway mediated by CMPG1-V32. Using CMPG1-V as bait, 17 putative cDNA clones interacting with CMPG1-V were identified (Supplementary Table S1); one of them encoded a protein disulphide isomerase (PDI). Based on the cDNA sequence, the 1,615 bp full-length PDI gene was isolated from H. villosa. The gene has an ORF of 1,323 bp, encoding a protein with 440 amino acids (Fig. 1A,B). BLASTn analysis showed that the sequence was highly similar to the T. aestivum PDI-like genes TaPDIL5-1a & 1b, and hence was designated PDI-V.


A disulphide isomerase gene (PDI-V) from Haynaldia villosa contributes to powdery mildew resistance in common wheat.

Faheem M, Li Y, Arshad M, Jiangyue C, Jia Z, Wang Z, Xiao J, Wang H, Cao A, Xing L, Yu F, Zhang R, Xie Q, Wang X - Sci Rep (2016)

Structural features of the PDI-V cDNA sequence and its translation product.(A) Structure deduced from the full-length cDNA sequence of PDI-V. The size of each domain, signal peptide and 3′ and 5′- UTR sizes and position of the ATG and TAG stop codons are shown. (B) Graphical representation of domain organization as provided by the NCBI conserved domain database. (C) Deduced amino acid sequence of PDI-V. Thioredoxin catalytic motifs and ER retention signals are shown in red.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4829865&req=5

f1: Structural features of the PDI-V cDNA sequence and its translation product.(A) Structure deduced from the full-length cDNA sequence of PDI-V. The size of each domain, signal peptide and 3′ and 5′- UTR sizes and position of the ATG and TAG stop codons are shown. (B) Graphical representation of domain organization as provided by the NCBI conserved domain database. (C) Deduced amino acid sequence of PDI-V. Thioredoxin catalytic motifs and ER retention signals are shown in red.
Mentions: CMPG1-V positively regulates powdery mildew resistance in common wheat1. To identify proteins interacting with CMPG1-V, a Y2H cDNA library of H. villosa was constructed and used to elucidate the resistance pathway mediated by CMPG1-V32. Using CMPG1-V as bait, 17 putative cDNA clones interacting with CMPG1-V were identified (Supplementary Table S1); one of them encoded a protein disulphide isomerase (PDI). Based on the cDNA sequence, the 1,615 bp full-length PDI gene was isolated from H. villosa. The gene has an ORF of 1,323 bp, encoding a protein with 440 amino acids (Fig. 1A,B). BLASTn analysis showed that the sequence was highly similar to the T. aestivum PDI-like genes TaPDIL5-1a & 1b, and hence was designated PDI-V.

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: The State Key Laboratory of Crop Genetics and Germplasm Enhancement, Cytogenetics Institute, Nanjing Agricultural University/JCIC-MCP, Nanjing, Jiangsu 210095, P.R. China.

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus