2010
DOI: 10.1002/ps.2050
|View full text |Cite
|
Sign up to set email alerts
|

Localisation of the benzimidazole fungicide binding site of Gibberella zeae β2‐tubulin studied by site‐directed mutagenesis

Abstract: Mutations at codons 50, 167, 198 and 200 of G. zeae β(2)tub could cause resistance to carbendazim, and these codons may form a binding pocket.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
64
2

Year Published

2011
2011
2018
2018

Publication Types

Select...
8
1
1

Relationship

3
7

Authors

Journals

citations
Cited by 82 publications
(67 citation statements)
references
References 24 publications
1
64
2
Order By: Relevance
“…The sensitivity of all strains to carbendazim was measured as described [69]. Sensitive strains could not grow on PDA plates containing 1.4 μg/mL carbendazim, while resistant strains grew normally on this medium.…”
Section: Methodsmentioning
confidence: 99%
“…The sensitivity of all strains to carbendazim was measured as described [69]. Sensitive strains could not grow on PDA plates containing 1.4 μg/mL carbendazim, while resistant strains grew normally on this medium.…”
Section: Methodsmentioning
confidence: 99%
“…The resistance to MBC fungicides is caused by point mutations in the b2-tubulin [19,20]. Deletion of the b2-tubulin resulted in reduced conidiation, vegetative growth and pathogenicity, but increased sensitivity to carbendazim [19,21]. In addition, the b1-tubulin deletion mutants displayed also reduced vegetative growth and pathogenicity, produced shorten spores, and were resistant to carbendazim [22], indicating both b1-and b2-tubulins play important roles in vegetative growth, conidiation, and responses to fungicides in F. asiaticum.…”
Section: Introductionmentioning
confidence: 99%
“…In fact, many mutation sites at the β-tubulin locus have been found in benzimidazole-resistant plant-pathogenic fungi (e.g., Albertini et al 1999;Qiu et al 2011), but most molecular studies have focused on replacement of the amino acid at position 198 and/or 200 (e.g., Davidson et al 2006;Fujimura et al 1992;Hollomon et al 1998). …”
Section: Resultsmentioning
confidence: 99%