AI Article Synopsis
- * A specific genetic mutation (V75M) was identified in the resistant strain, which involves a change from valine to methionine at position 75 of the SDH protein.
- * Cloning experiments showed that the engineered SDH proteins from both strains had the same resistance profiles as their respective natural SDH, confirming that the V75M mutation is responsible for the reduced sensitivity to carpropamid in the resistant strain.
Article Abstract
The inhibitory activity of carpropamid on scytalone dehydratase (SDH) extracted from a carpropamid-resistant strain of Magnaporthe grisea (Hebert) Barr was dramatically reduced in comparison with that on SDH extracted from the sensitive strain. A single-point mutation (G to A) located at the upstream region (233 bp downstream from the ATG codon) resulting in a one-amino-acid substitution (valine [GTG] 75 to methionine [ATG]: V75M) was found in the resistant strain. To examine whether the V75M mutation is the primary reason for decreasing the sensitivity of SDH to carpropamid, the SDH cDNAs of both the sensitive and the resistant strain were cloned into a GST-fused protein expression vector-system. The recombinant SDHs of both strains exhibited the same sensitivities to carpropamid as those extracted from the mycelia of the respective strains. These data clearly revealed that the V75M mutation causes the low sensitivities of the SDHs of the carpropamid-resistant strains, and strongly suggests that the V75M mutation confers resistance of these strains to carpropamid.
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