A single amino-acid substitution in the iron-sulphur protein subunit of succinate dehydrogenase determines resistance to carboxin in Mycosphaerella graminicola
作者： W. Skinner , A. Bailey , A. Renwick , J. Keon , S. Gurr
关键词: Gene 、 Mycosphaerella graminicola 、 Biochemistry 、 Succinate dehydrogenase 、 Sequence analysis 、 Expression vector 、 Protein subunit 、 Promoter 、 Biology 、 Mutant
摘要: A gene encoding the iron-sulphur protein (Ip) subunit of succinate dehydrogenase (Sdh, EC 1.3.99.1) from Mycosphaerella graminicola (Septoria tritici) has been cloned and sequenced. The deduced amino-acid sequence exhibited a high degree homology to Ip subunits Sdh other organisms; three cysteine-rich clusters associated with centres involved in electron transport were particularly conserved. Expression studies using synthetic green fluorescent (SGFP) expression vector demonstrated that DNA also contained functional promoter region confirmed initiation codon could act as translational start site. Mutants resistant fungicide carboxin (Cbx), known inhibitor Sdh, found contain single substitution third domain protein. These mutations resulted conversion highly conserved His residue, located [3Fe-4 S] high-potential non-heme iron sulphur-redox (S3) centre, either Tyr or Leu. An containing → mutation was constructed shown confer Cbx resistance following co-transformation into Cbx-sensitive wild-type strain. This identified by analysis responsible for determining resistance.
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