An l- fucose-responsive transcription factor cross-regulates the expression of a diverse array of carbohydrate-active enzymes in Trichoderma reesei
文献类型： 外文期刊
作者： Zhao, Qinqin 1 ; Gao, Liwei 2 ; Xu, Nuo 1 ; Zhang, Xiuting 1 ; Qin, Yuqi 1 ; Qu, Yinbo 1 ; Liu, Guodong 1 ;
作者机构： 1.Shandong Univ, State Key Lab Microbial Technol, Qingdao, Shandong, Peoples R China
2.Chinese Acad Agr Sci, Tobacco Res Inst, Qingdao, Shandong, Peoples R China
3.Shandong Univ, Natl Glycoengn Res Ctr, Qingdao, Shandong, Peoples R China
期刊名称：PLOS GENETICS （ 影响因子：3.7； 五年影响因子：4.5 ）
ISSN： 1553-7404
年卷期： 2025 年 21 卷 8 期
页码：
收录情况： SCI
摘要： l-Fucose is a universal capping component of biomolecules found throughout all domains of life. Although fungi are renowned for their role in biomass recycling, the mechanisms by which they process l-fucose remain largely unknown. In this study, we elucidate a l-fucose-responsive system in Trichoderma reesei, a model fungus for plant cell wall degradation. Central to this system is the transcription factor FUR1, which is indispensable for growth on l-fucose. FUR1 orchestrates the expression of l-fucose catabolic enzymes, including an l-fucose dehydrogenase that exhibits distant homology to counterparts in bacteria and mammals. Through RNA sequencing and biochemical assays, we demonstrate that FUR1 also governs the enzymatic liberation of l-fucose by upregulating extracellular alpha-l-fucosidases. Intriguingly, FUR1 mediates l-fucose-triggered expression of a broad spectrum of enzymes that target diverse glycosidic bonds (e.g., beta-glucuronidic, alpha-galactosidic, and beta-xylosidic linkages) within complex carbohydrates. Expression of a constitutively active FUR1 mutant unlocked the production of otherwise silent glycosidases, substantially boosting the hydrolytic capacity of the fungal secretome on orange peel. These findings offer the first molecular insight into l-fucose sensing and metabolism in fungi, and advance our understanding of the fungal regulatory network for coordinated expression of biomass-degrading enzymes.
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