Transfer of the β-tubulin gene of Botrytis cinerea with resistance to carbendazim into Fusarium graminearum

2010 ◽  
Vol 66 (5) ◽  
pp. 482-489 ◽  
Author(s):  
Sheng-Ming Liu ◽  
Yu Chen ◽  
Jun-Jie Yu ◽  
Chang-Jun Chen ◽  
Jian-Xin Wang ◽  
...  
2013 ◽  
Vol 69 (5) ◽  
pp. 582-588 ◽  
Author(s):  
ShengMing Liu ◽  
YaBing Duan ◽  
ChangYan Ge ◽  
ChangJun Chen ◽  
MingGuo Zhou

2018 ◽  
Vol 108 (3) ◽  
pp. 352-361 ◽  
Author(s):  
Yuanye Zhu ◽  
Xiaoyu Liang ◽  
Yanjun Li ◽  
Yabing Duan ◽  
Zhitian Zheng ◽  
...  

β-Tubulin is the target of benzimidazole fungicides, the most widely used of which is carbendazim (methyl benzimidazol-2-ylcarbamate [MBC]). MBC sensitivity is determined by the differential affinity of MBC for β-tubulins. However, the mechanism of less sensitivity of Fusarium graminearum to MBC compared with other fungi, including Botrytis cinerea, Colletotrichum gloeosporioides, and Sclerotinia sclerotiorum, remains exclusive. Alignment of β-tubulin amino acid sequences showed that position 240 of β-tubulins is leucine (L) in most pathogenic fungi but is phenylalanine (F) in the Fgβ2-tubulin of the F. graminearum wild type. The effective concentration resulting in 50% inhibition (EC50) value of MBC against the Fgβ2F240L mutant of F. graminearum is 0.047 μg/ml, which was 10-fold lower than that of wild-type strain 2021. Moreover, The EC50 value of MBC against the BcβL“240”F (actually position 232) mutant of Botrytis cinerea was 0.44 μg/ml, which was ninefold higher than that of B. cinerea wild-type strain Bt4-1. In response to MBC treatment (0.15 μg/ml), microtubules were clearly visible in Fgβ2-enhanced green fluorescent protein (EGFP) but not in Fgβ2F240L-EGFP. Moreover, a molecular docking assay indicated that F240L mutation created a pi-pi interaction between Fgβ2-tubulin and MBC and increased the binding affinity of Fgβ2-tubulin to MBC. Our results suggest that F240 is responsible for the naturally less MBC sensitivity in F. graminearum compared with B. cinerea, C. gloeosporioides, and S. sclerotiorum by decreasing the binding affinity between Fgβ2-tubulin and MBC.


2018 ◽  
Vol 43 (1) ◽  
pp. 31-38
Author(s):  
Vijaya Gowri Esvaran ◽  
Aarthi Mohanasundaram ◽  
Shruthi Mahadeva ◽  
Tania Gupta ◽  
Kangayam M. Ponnuvel

Cell Reports ◽  
2012 ◽  
Vol 2 (6) ◽  
pp. 1554-1562 ◽  
Author(s):  
Martin Breuss ◽  
Julian Ik-Tsen Heng ◽  
Karine Poirier ◽  
Guoling Tian ◽  
Xavier Hubert Jaglin ◽  
...  

Genetics ◽  
1984 ◽  
Vol 108 (1) ◽  
pp. 143-164
Author(s):  
Tim Schedl ◽  
Judi Owens ◽  
William F Dove ◽  
Timothy G Burland

ABSTRACT The organization of the α- and β-tubulin gene families in Physarum was investigated by Mendelian analysis. Restriction endonuclease-generated DNA fragments homologous to α- and β-tubulin show length polymorphisms that can be used as markers for genetic mapping. Analysis of meiotic assortment among progeny of heterozygotes allowed α- and β-tubulin sequence loci to be defined. There are four unlinked α-tubulin sequence loci (altA, altB, altC and altD) and at least three unlinked β-tubulin sequence loci (betA, betB and betC). The α-tubulin loci are not linked to the β-tubulin loci. —Segregation of tubulin sequence loci with respect to ben mutations that confer resistance to antitubulin benzimidazole drugs was used to investigate whether any members of the α- or β-tubulin gene families are allelic to ben loci. The β-tubulin sequence locus betB is allelic to the resistance locus benD, the betA locus is probably allelic to benA and the α-tubulin sequence locus altC may be allelic to benC. The molecular implications of benzimidazole resistance phenotypes when only one of the expressed β-tubulin gene family members mutates to drug resistance are discussed in relation to tubulin function.


2020 ◽  
Vol 217 ◽  
pp. 107957 ◽  
Author(s):  
Paulius Baltrušis ◽  
Michaela Komáromyová ◽  
Marián Várady ◽  
Georg von Samson-Himmelstjerna ◽  
Johan Höglund

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