ArticleNature communications2025
Structural-guided identification of two modulators of β-1,3-glucan synthase FKS1.
Jialu Li, Jian Li, Angqi Zhu, Xinli Dai, Juxiu Liu, Huayi Liu, Zhili Xia, Yuefan Dong, Wenyu Qian, Lunzhi Dai and 5 more
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In one paragraphArticle in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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15 authors.
Jialu Li *Department of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University, Chengdu, China.ORCID http://orcid.org/0000-0002-0513-7597 Jian Li *State Key Laboratory of Synthetic Biology, Frontiers Science Center for Synthetic Biology (Ministry of Education), School of Synthetic Biology and Biomanufacturing, Tianjin University, Tianjin, China.ORCID http://orcid.org/0000-0002-3167-4265 Angqi Zhu *State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0002-3162-441X Xinli DaiDepartment of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University, Chengdu, China.
Juxiu LiuDepartment of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University, Chengdu, China.
Huayi LiuState Key Laboratory of Synthetic Biology, Frontiers Science Center for Synthetic Biology (Ministry of Education), School of Synthetic Biology and Biomanufacturing, Tianjin University, Tianjin, China.ORCID http://orcid.org/0000-0001-5179-1912 Zhili XiaThe First Clinical Medical College, Lanzhou University, Lanzhou, China.
Wenyu QianDepartment of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University, Chengdu, China.
Lunzhi DaiState Key Laboratory of Biotherapy, National Clinical Research Center for Geriatrics and General Practice Medical Center, West China Hospital, Sichuan University, Chengdu, China.ORCID http://orcid.org/0000-0002-3003-8910 Li GuoDepartment of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University, Chengdu, China.
Chuangye YanState Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China. yancy2019@tsinghua.edu.cn.ORCID http://orcid.org/0000-0001-9338-8048 Dong DengDepartment of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University, Chengdu, China. dengd@scu.edu.cn.ORCID http://orcid.org/0000-0002-8590-9525 Yunzi LuoState Key Laboratory of Synthetic Biology, Frontiers Science Center for Synthetic Biology (Ministry of Education), School of Synthetic Biology and Biomanufacturing, Tianjin University, Tianjin, China. yunzi.luo@tju.edu.cn.ORCID http://orcid.org/0000-0002-5860-6350 Xiang WangDepartment of Obstetrics, Key Laboratory of Birth Defects and Related Disease of Women and Children of MOE, State Key Laboratory of Biotherapy, West China Second Hospital, Sichuan University, Chengdu, China. xiangwang@scu.edu.cn.ORCID http://orcid.org/0000-0001-9348-7441 Funding
National Natural Science Foundation of China (National Science Foundation of China) 32071426
6 · The paper itselfAbstract
FKS1 is a β-1,3-glucan synthase critical for fungal cell wall formation and a target for antifungal drugs such as echinocandin and ibrexafungerp. However, the mechanisms regulating FKS1 activity remain largely unknown. Here, we reveal that transfer RNA (tRNA) acts as an endogenous inhibitor, whereas GSR1 functions as a stabilizer of FKS1. The cryo-EM structure of FKS1 adopts a tRNA-mediated homodimer configuration, representing a quiescent state of β-1,3-glucan synthase. Unexpectedly, the copurified endogenous tRNA is identified as a potent inhibitor that suppresses FKS1 activity. Moreover, high-resolution cryo-EM density analysis enable the identification of GSR1 as an additional binding partner of FKS1. Mutagenesis experiments confirm the interaction between FKS1 and GSR1. Evolutionarily conserved GSR1 is found to increase the stability of FKS1 in β-1,3-glucan biosynthesis. Collectively, our findings identify both tRNA and GSR1 as intrinsic modulators of β-1,3-glucan biosynthesis, thereby providing opportunities for the further development of FKS1-targeted antifungal drugs.
Indexed as
GlucosyltransferasesRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAntifungal Agentsbeta-GlucansCell WallCryoelectron MicroscopyEchinocandinsMembrane ProteinsProtein Binding1,3-beta-glucan synthaseAntifungal Agentsbeta-1,3-glucanbeta-GlucansEchinocandinsFKS1 protein, S cerevisiaeglucan synthaseGlucosyltransferasesMembrane ProteinsRNA, TransferSaccharomyces cerevisiae Proteins
Identifiers
PMID41354657
PMCPMC12808297
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