Functional analysis of the β 2 -tubulin gene of Fusarium graminearum and the β -tubulin gene of Botrytis cinerea by homologous replacement

2013 ◽  
Vol 69 (5) ◽  
pp. 582-588 ◽  
Author(s):  
ShengMing Liu ◽  
YaBing Duan ◽  
ChangYan Ge ◽  
ChangJun Chen ◽  
MingGuo Zhou
Keyword(s):  
Functional Analysis ◽  
Botrytis Cinerea ◽  
Fusarium Graminearum ◽  
Tubulin Gene ◽  
Β Tubulin

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 ◽  
...  
Keyword(s):  
Botrytis Cinerea ◽  
Fusarium Graminearum ◽  
Tubulin Gene ◽  
Β Tubulin

Cloning and functional analysis of a β-tubulin gene from a benomyl resistant mutant of Aspergillus parasiticus

Gene ◽  
1996 ◽  
Vol 182 (1-2) ◽  
pp. 7-12 ◽  
Author(s):  
Tzong-Shoon Wu ◽  
Christopher D. Skory ◽  
Jyh-Song Horng ◽  
John E. Linz
Keyword(s):  
Functional Analysis ◽  
Aspergillus Parasiticus ◽  
Resistant Mutant ◽  
Tubulin Gene ◽  
Β Tubulin

scholarly journals F240 of β2-Tubulin Explains why Fusarium graminearum is Less Sensitive to Carbendazim than Botrytis cinerea

2018 ◽  
Vol 108 (3) ◽  
pp. 352-361 ◽  
Author(s):  
Yuanye Zhu ◽  
Xiaoyu Liang ◽  
Yanjun Li ◽  
Yabing Duan ◽  
Zhitian Zheng ◽  
...  
Keyword(s):  
Botrytis Cinerea ◽  
Binding Affinity ◽  
Fusarium Graminearum ◽  
Type Strain ◽  
Wild Type Strain ◽  
Fluorescent Protein ◽  
Amino Acid Sequences ◽  
Wild Type ◽  
Benzimidazole Fungicides ◽  
Β Tubulin

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.

Bchex virulence gene of Botrytis cinerea: characterization and functional analysis

2011 ◽  
Vol 77 (4) ◽  
pp. 230-238 ◽  
Author(s):  
C. Aguayo ◽  
J. Riquelme ◽  
P. D. T. Valenzuela ◽  
M. Hahn ◽  
E. Silva Moreno
Keyword(s):  
Functional Analysis ◽  
Botrytis Cinerea ◽  
Virulence Gene

scholarly journals Molecular Characterization and Functional Analysis of PR-1-Like Proteins Identified from the Wheat Head Blight Fungus Fusarium graminearum

2018 ◽  
Vol 108 (4) ◽  
pp. 510-520 ◽  
Author(s):  
Shunwen Lu ◽  
Michael C. Edwards
Keyword(s):  
Functional Analysis ◽  
Fusarium Graminearum ◽  
Expression Patterns ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Transcriptional Analysis ◽  
Fungal Genome ◽  
Dimensional Structure ◽  
Head Blight ◽  
Fungal Virulence

The group 1 pathogenesis-related (PR-1) proteins originally identified from plants and their homologs are also found in other eukaryotic kingdoms. Studies on nonplant PR-1-like (PR-1L) proteins have been pursued widely in humans and animals but rarely in filamentous ascomycetes. Here, we report the characterization of four PR-1L proteins identified from the ascomycete fungus Fusarium graminearum, the primary cause of Fusarium head blight of wheat and barley (designated FgPR-1L). Molecular cloning revealed that the four FgPR-1L proteins are all encoded by small open reading frames (612 to 909 bp) that are often interrupted by introns, in contrast to plant PR-1 genes that lack introns. Sequence analysis indicated that all FgPR-1L proteins contain the PR-1-specific three-dimensional structure, and one of them features a C-terminal transmembrane (TM) domain that has not been reported for any stand-alone PR-1 proteins. Transcriptional analysis revealed that the four FgPR-1L genes are expressed in axenic cultures and in planta with different spatial or temporal expression patterns. Phylogenetic analysis indicated that fungal PR-1L proteins fall into three major groups, one of which harbors FgPR-1L-2-related TM-containing proteins from both phytopathogenic and human-pathogenic ascomycetes. Low-temperature sodium dodecyl sulfate polyacrylamide gel electrophoresis and proteolytic assays indicated that the recombinant FgPR-1L-4 protein exists as a monomer and is resistant to subtilisin of the serine protease family. Functional analysis confirmed that deletion of the FgPR-1L-4 gene from the fungal genome results in significantly reduced virulence on susceptible wheat. This study provides the first example that the F. graminearum–wheat interaction involves a pathogen-derived PR-1L protein that affects fungal virulence on the host.

scholarly journals Development and comparison of real-time and conventional PCR tools targeting β-tubulin gene for detection of Nosema infection in silkworms

2018 ◽  
Vol 43 (1) ◽  
pp. 31-38
Author(s):  
Vijaya Gowri Esvaran ◽  
Aarthi Mohanasundaram ◽  
Shruthi Mahadeva ◽  
Tania Gupta ◽  
Kangayam M. Ponnuvel
Keyword(s):  
Real Time ◽  
Conventional Pcr ◽  
Tubulin Gene ◽  
Nosema Infection ◽  
Β Tubulin

scholarly journals Mutations in the β-Tubulin Gene TUBB5 Cause Microcephaly with Structural Brain Abnormalities

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

GENETICS OF THE TUBULIN GENE FAMILIES OF PHYSARUM

Genetics ◽  
1984 ◽  
Vol 108 (1) ◽  
pp. 143-164
Author(s):  
Tim Schedl ◽  
Judi Owens ◽  
William F Dove ◽  
Timothy G Burland
Keyword(s):  
Drug Resistance ◽  
Genetic Mapping ◽  
Gene Family ◽  
Gene Families ◽  
Resistance Locus ◽  
Tubulin Gene ◽  
Length Polymorphisms ◽  
Mapping Analysis ◽  
Mendelian Analysis ◽  
Β Tubulin

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.

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