Magnaporthe oryzae is the causal agent of rice blast. Understanding how abiotic stress affects the resistance of plants to this disease is useful for designing disease control strategies. Here, the effects of temperature and light (supplied under an oscillating electric eld) on the effector complex comprising APikL2A from M. oryzae and sHMA25 from foxtail millet were investigated by molecular dynamic (MD) simulations using the GROMACS package. While the structure of APikL2A/sHMA25 remained relatively stable in a temperature range from 290 K (16.85°C) to 320 K (46.85°C), the dome shape of the temperature-dependent binding free energy curve indicated that there was minimum binding a nity between APikL2A and sHMA25 at 300 K -310 K. This coincided with the optimum infectivity temperature, suggesting that decoupling of the two polypeptides may play a role in the infection process. A strong oscillating electric eld destroyed the structure of APikL2A/sHMA25, although it was stable under weaker electric elds. An increase in binding free energy was discovered in these electric elddependent simulations.
Magnaporthe oryzae is the causal agent of rice blast. Understanding how abiotic stress affects the resistance of plants to this disease is useful for designing disease control strategies. Here, the effects of temperature and light (supplied under an oscillating electric field) on the effector complex comprising APikL2A from M. oryzae and sHMA25 from foxtail millet were investigated by molecular dynamic (MD) simulations using the GROMACS package. While the structure of APikL2A/sHMA25 remained relatively stable in a temperature range from 290 K (16.85°C) to 320 K (46.85°C), the dome shape of the temperature-dependent binding free energy curve indicated that there was minimum binding affinity between APikL2A and sHMA25 at 300 K – 310 K. This coincided with the optimum infectivity temperature, suggesting that decoupling of the two polypeptides may play a role in the infection process. A strong oscillating electric field destroyed the structure of APikL2A/sHMA25, although it was stable under weaker electric fields. An increase in binding free energy was discovered in these electric field-dependent simulations.
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