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Michiyo Oshima Shinpei Banno Kiyotsugu Okada Taeko Takeuchi Makoto Kimura Akihiko Ichiishi Isamu Yamaguchi Makoto Fujimura 《Journal of General Plant Pathology》2006,72(1):65-73
Previously, we cloned a putative osmosensing histidine kinase gene (BcOS1) and revealed that a single amino acid substitution, isoleucine to serine at codon 365, conferred dicarboximide resistance
in field isolates of Botrytis cinerea. This point mutation (type I) occurred within the restriction enzyme TaqI site of the wild-type BcOS1 gene. Thus, a procedure was developed for detecting the type I mutation of the BcOS1 gene using a polymerase chain reaction (PCR) in combination with restriction fragment-length polymorphism (RFLP). Diagnosis
by PCR-RFLP was conducted on the 105 isolates isolated from 26 fields in Japan. All dicarboximide-sensitive isolates (49 isolates)
had the wild-type BcOS1 gene, and the 43 isolates with the type I mutation were resistant to dicarboximides without exception. These data indicate
that dicarboximide-resistant isolates with type I mutation are widespread throughout Japan. However, other types of dicarboximide
resistance were detected among isolates from Osaka; among the 24 resistant isolates from Osaka, 12 had the BcOS1 gene without the type I mutation. BcOS1 gene sequencing of these resistant isolates classified them into two groups, type II and type III. The type II isolates have
three amino acid substitutions within BcOS1p (368Val to Phe, 369Gln to His, and 447Thr to Ser). The type III isolates have two amino acid substitutions within BcOS1p (369Gln to Pro and 373Asn to Ser). These amino acid changes are located on the amino acid repeat domain in BcOS1p. The three types of resistant
isolates were all moderately resistant to dicarboximides without significant osmotic sensitivity, and their pathogenicity
on cucumber leaves was also very similar to that of the wild-type isolate. 相似文献