A mutant form of the succinate dehydrogenase iron-sulphur protein subunit confers resistance to carboxin in the maize smut pathogen Ustilago maydis.
نویسندگان
چکیده
234 A mutant form of the succinate dehydrogenase iron-sulphur protein subunit confers resistance to carboxin in the maize smut pathogen Ustilago maydis John P. R. Keon, P. L. Elaine Broomfield, Gordon A. White* and John A. Hargreaves Department of Agricultural Sciences, University of Bristol, A.F.R.C. Institute of Arable Crops Research, Long Ashton Research Station, Bristol BSI 8 9AF, U.K. and *Agriculture Canada, Research Centre, 1400 Western Road, London, Ontario N6G 2V4, Canada
منابع مشابه
QSARS OF ANTI-FUNGAL ACTIVITY OF FURAN CARBOXANILIDE DERIVATIVES AGAINST WILD AND MUTANT STRAINS OF USTILAGO MAYDIS
The structural requirements for the inhibitor activity of various furan carboxanilide derivatives against succinate dehydrogenase complex (SDC) activity in mitochondria of either wild or mutant strains of Ustilago maydis were investigated with the aid of Hansch QSAR analysis. It has been found that the inhibitor activity against both types of enzymes is best related to the ??? or ??M of th...
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The Ustilago maydis-maize pathosystem has emerged as the current model for plant pathogenic basidiomycetes and as one of the few models for a true biotrophic interaction that persists throughout fungal development inside the host plant. This is based on the highly advanced genetic system for both the pathogen and its host, the ability to propagate U. maydis in axenic culture, and its unique cap...
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ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 22 1 شماره
صفحات -
تاریخ انتشار 1994