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Identification and characterization of the glycoside hydrolase family 18 genes from the entomopathogenic fungus Isaria cicadae genome

文献类型: 外文期刊

作者: Peng, Yao 1 ; Wang, Lifang 2 ; Gao, Yan 3 ; Ye, Liang 1 ; Xu, Huihui 1 ; Li, Shuangjiao 1 ; Jiang, Junqi 1 ; Li, Guiting; 1 ;

作者机构: 1.Anhui Agr Univ, Sch Plant Protect, Hefei 230036, Peoples R China

2.Anhui Agr Univ, Sch Hort, Hefei 230036, Peoples R China

3.Guangdong Acad Agr Sci, Guangdong Prov Key Lab High Technol Plant Protect, Guangzhou 510640, Peoples R China

关键词: Isaria cicadae; chitinase; domain structure; phylogenetic analysis; transcript analysis

期刊名称:CANADIAN JOURNAL OF MICROBIOLOGY ( 影响因子:2.419; 五年影响因子:2.35 )

ISSN: 0008-4166

年卷期: 2020 年 66 卷 4 期

页码:

收录情况: SCI

摘要: Fungal chitinases play essential roles in chitin degradation, cell wall remodeling, chitin recycling, nutrition acquisition, autolysis, and virulence. In this study, 18 genes of the glycoside hydrolase 18 (GH18) family were identified in the Isaria cicadae genome. Seventeen of the genes belonged to chitinases and one was an endo-beta-N-acetylglucosaminidase (ENGase). According to phylogenetic analysis, the 17 chitinases were designated as subgroups A (7 chitinases), B (7), and C (3). The exon-intron organizations of these genes were analyzed. The conserved regions DxxDxDxE and S/AxGG and the domains CBM1, CBM18, and CBM50 were detected in I. cicadae chitinases and ENGase. The results of analysis of expression patterns showed that genes ICchiA1, ICchiA6, ICchiB1, and ICchiB4 had high transcript levels in the different growth conditions or developmental stages. Subgroup A chitinase genes had higher transcript levels than the genes of all other chitinases. Subgroup B chitinase genes (except ICchiB7) presented higher transcript levels in chitin medium compared with other conditions. ICchiC2 and ICchiC3 were mainly transcribed in autolysis medium and in blastospores, respectively. Moreover, ICchiB1 presented higher transcript levels than genes of other chitinases. This work provides an overview of the GH18 chitinases and ENGase in I. cicadae and provides a context for the chitinolytic potential, functions, and biological controls of these enzymes of entomopathogenic fungi.

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