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Structural-guided identification of two modulators of β-1,3-glucan synthase FKS1
Jialu Li1,2, Jian Li3, Angqi Zhu4
1Department 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.
Nature Communications
|December 7, 2025
Summary
Transfer RNA (tRNA) inhibits fungal β-1,3-glucan synthase (FKS1), while GSR1 stabilizes it. This discovery offers new avenues for developing FKS1-targeted antifungal drugs.
Area of Science:
- Biochemistry
- Mycology
- Structural Biology
Background:
- FKS1 is a key enzyme in fungal cell wall synthesis and a target for antifungal medications.
- The regulatory mechanisms governing FKS1 activity are not well understood.
Purpose of the Study:
- To elucidate the intrinsic modulators of FKS1 activity and its structural configurations.
- To explore potential new targets for antifungal drug development.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was used to determine the structure of FKS1.
- Biochemical assays and mutagenesis experiments were performed to validate interactions and functions.
Main Results:
- The cryo-EM structure revealed FKS1 in a quiescent homodimer state mediated by transfer RNA (tRNA).
- Endogenous tRNA was identified as a potent inhibitor of FKS1 activity.
- GSR1 was identified as a FKS1 stabilizer, enhancing its function in β-1,3-glucan biosynthesis.
Conclusions:
- tRNA and GSR1 are identified as intrinsic regulators of fungal β-1,3-glucan biosynthesis.
- These findings provide novel insights into FKS1 regulation and present new opportunities for antifungal drug discovery.
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