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ArticleMolecular biology reports2024

Genome-wide identification and biochemical characterization of glycoside hydrolase gene family members in Tilletia Horrida.

Xinyue Shu, Yuping Zhong, Xiaoqun Yi, Aijun Wang, Ping Li, Desuo Yin, Aiping Zheng

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Article in Molecular biology reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1 citing paper in PubMed.

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5 · Who and what money

Authors and funding

7 authors.

Xinyue Shu *College of Agronomy, Sichuan Agricultural University, Chengdu, China.
Yuping Zhong *Hubei Huichzhi Biotech Company, Wuhan, China.
Xiaoqun YiCollege of Agronomy, Sichuan Agricultural University, Chengdu, China.
Aijun WangCollege of Plant Protection, Henan Agricultural University, Zhengzhou, China.
Ping LiRice Research Institute, Sichuan Agricultural University, Chengdu, China.
Desuo YinFood Crop Research Institute, Hubei Academy of Agriculture Sciences, Wuhan, China. yindesuo@163.com.
Aiping ZhengCollege of Agronomy, Sichuan Agricultural University, Chengdu, China. apzh0602@gmail.com.

Funding

Key project of Wuhan science and Technology Bureau 2022022202015037National Natural Science Foundation of China 32001490
6 · The paper itself

Abstract

introductionRice kernel smut, caused by Tilletia horrida, is becoming an increasingly serious disease in hybrid rice planting, leading to production losses and quality decline of male-sterile rice varieties. Successful infection requires an efficient energy source that the pathogen obtains from rice plants, such as carbohydrates. Glycoside hydrolases (GHs), one of the largest sub-families in the cell wall-degrading enzyme family, play a key role in the infection progress of pathogens. To investigate their roles in facilitating infection, in this study, we identified and characterized genes encoding GH family proteins of T. horrida and further explored the functions and structures of these genes. MATERIALS AND

methodsThrough genome-wide sequencing and bioinformatics analyses, 52 GH genes were identified from T. horrida, named ThGhd_1 to ThGhd_52. The subcellular location, conserved motifs, and structures of ThGhds were identified by bioinformatics analyses.

resultsPhylogenetic analysis revealed that ThGhds with similar domains clustered together, although some proteins clustered in different branches, which might reflect functional diversity. Protein-protein interaction network analysis revealed that ThGhds interact with partner proteins involved in reactive oxygen species signaling, protein kinase activity, and plant hormone signal transduction pathways. RNA-sequencing analysis showed that the expression of ThGhd genes responded differently at different infection time points, with dynamic changes detected during the T. horrida infection process, indicating that these genes are involved in interactions with rice and have potential roles in pathogenic mechanisms.

conclusionsThe results of this study provide valuable resources for the structure elucidation of GH family proteins of T. horrida and can help to further elucidate their roles in pathogenesis.

Indexed as

Glycoside HydrolasesMultigene FamilyOryzaPhylogenyComputational BiologyGenome, PlantOrobanchaceaePlant DiseasesPlant ProteinsProtein Interaction MapsGlycoside HydrolasesPlant ProteinsExpression patternGlycoside hydrolasesPathogenicityRice kernel smutTilletia Horrida

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