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Mechanism of resistance to carpropamid in Magnaporthe grisea by Makiichi Takagaki; Koichiro Kaku; Satoshi Watanabe; Kiyoshi Kawai; Tsutomu Shimizu; Haruko Sawada; Kazuo Kumakura; Kozo Nagayama is a Agricultural and Biological Sciences article available to read on EtoBox.

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## 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. Copyright © 2004 Society of Chemical Industry

Who reads Mechanism of resistance to carpropamid in Magnaporthe grisea?

Author

Makiichi Takagaki; Koichiro Kaku; Satoshi Watanabe; Kiyoshi Kawai; Tsutomu Shimizu; Haruko Sawada; Kazuo Kumakura; Kozo Nagayama

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 1526-498X)

Published

2004

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)