4.3 Article

Binding of stress-responsive OsWRKY proteins through WRKYGQK heptapeptide residue with the promoter region of two rice blast disease resistance genes Pi2 and Pi54 is important for development of blast resistance

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3 BIOTECH
卷 13, 期 9, 页码 -

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SPRINGER HEIDELBERG
DOI: 10.1007/s13205-023-03711-y

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OsWRKY; Blast resistant genes; Molecular docking; Promoter elements; Binding residue; Zinc finger structure

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Molecular docking was used to investigate the interactions between differentially expressed rice WRKY proteins and blast resistance genes Pi2 and Pi54 under rice blast disease and drought stresses. The study revealed differential binding patterns of the WRKY proteins with the two resistance genes. Some WRKY proteins interacted with the genes involving the residues of the zinc finger structure, while others interacted involving the residues of the conserved WRKYGQK heptapeptide sequence. The findings suggest that the interaction between OsWRKY proteins and the two blast resistance genes is important for mitigating the blast challenge in rice under overlapping drought and blast stresses.
Molecular docking was done to investigate the interactions between five differentially expressed rice WRKY proteins when challenged with the rice blast disease caused by Magnaporthe oryzae and drought stresses applied either individually or overlapped, with the promoter region of two blast resistance genes (Pi2 and Pi54). Molecular docking was performed using the HDOCK server. Initially, the homology models for each of the five rice WRKY proteins were prepared using I-TASSER server, and then the secondary structure as well as the DNA-binding pockets were predicted using PSIPRED and BindUP servers, respectively. The molecular docking study revealed a differential binding pattern of the rice WRKYs with the two blast resistance genes. The WRKY proteins (OsWRKY88 and OsWRKY102), whose transcript levels decrease when drought and blast stresses are overlapped, interact with the two resistance genes mostly involving the residues of the zinc finger structure. On the other hand, the WRKY proteins (OsWRKY53-1 and OsWRKY113), whose transcript levels did not reduce significantly when challenged by drought and blast overlapped condition compared to individual treatment of blast, interact mostly involving the residues of the conserved WRKYGQK heptapeptide sequence. Interestingly, the protein OsWRKY74 whose transcript levels are unaffected in both individual and overlapped stresses, interacts with both the blast resistance genes involving few residues of both WRKYGQK heptapeptide and the zinc finger structure. The findings thus indicate that the interaction of OsWRKY proteins involving the conserved WRKYGQK heptapeptide sequence with the blast resistance genes Pi2 and Pi54 is important to mitigate the blast challenge in rice even during overlapping challenges of drought.

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