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An acetyl-dependent proofreading mechanism governs synthetic fidelity in Phytophthora sojae chitin synthase

文献类型：期刊论文

作者Zhang, Xiaoyue2,4,5; Li, Pengwei2,5; Niu, Suhao2,5; Gao, Kun1,2,5; Sun, Mengsi3; Wu, Yujie3; Bi, Yunchen1,2,4,5,6
刊名BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
出版日期2026-04-30
卷号811页码:7
关键词Chitin synthase Synthetic fidelity Acetyl-dependent proofreading mechanism Cryo-EM
ISSN号0006-291X
DOI10.1016/j.bbrc.2026.153553
通讯作者Wu, Yujie(wuyj@szbl.ac.cn) ; Bi, Yunchen(yunchenbi@qdio.ac.cn)
英文摘要Chitin is an essential structural polysaccharide in fungal and oomycete cell walls, providing mechanical strength and integrity due to its crystalline, insoluble nature. Chitin synthase (CHS) is the key enzyme responsible for its biosynthesis, orchestrating the sequential steps of substrate binding, hydrolysis, glycosidic bond formation, and polymer translocation. However, the molecular mechanism that governs its synthetic fidelity remains unclear. To address this, we investigated whether Phytophthora sojae chitin synthase 1 (PsChs1) can utilize UDP-glucosamine (UDP-GlcN), a deacetylated substrate analog that closely resembles the natural substrate. Biochemical assays revealed that while PsChs1 binds and hydrolyzes UDP-GlcN, it fails to polymerize it. To uncover the structural basis of this stringent discrimination, we determined the cryo-EM structure of PsChs1 in complex with UDP-GlcN and GlcN. The structure, supported by molecular dynamics simulations, captures a non-productive state. In this state, a conserved arginine (Arg538) experiences electrostatic repulsion from the C2 ammonium group of UDP-GlcN. Concurrently, the loss of acetyl-dependent interactions displaces the 4 '-OH group of the acceptor GlcN beyond the distance required for nucleophilic attack. Together, these findings reveal an acetyl-dependent proofreading mechanism that dictates the strict synthetic fidelity of chitin synthase.
WOS关键词TRANSLOCATION
资助项目National Key R&D Program of China[2023YFE0125400] ; National Natural Science Foundation of China[42376136] ; Shandong Provincial Natural Science Foundation[ZR2024ZD32] ; Distinguished experts of Taishan Scholars of Shandong Province[tstp20240840]
WOS研究方向Biochemistry & Molecular Biology ; Biophysics
语种英语
WOS记录号WOS:001712714800001
出版者ACADEMIC PRESS INC ELSEVIER SCIENCE
源URL[http://ir.qdio.ac.cn/handle/337002/205006]  
专题海洋研究所_实验海洋生物学重点实验室
通讯作者Wu, Yujie; Bi, Yunchen
作者单位1.Chinese Acad Sci, AI Oceanog Res Ctr, Inst Oceanol, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, CAS, Qingdao 266071, Peoples R China
3.Shenzhen Bay Lab, Biomed Res Core Facil, Shenzhen 518055, Peoples R China
4.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
5.Chinese Acad Sci, Inst Oceanol, Shandong Prov Lab Expt Marine Biol, Qingdao 266071, Peoples R China
6.Qingdao Marine Sci & Technol Ctr, Lab Marine Biol & Biotechnol, Qingdao 266237, Peoples R China
推荐引用方式
GB/T 7714		 Zhang, Xiaoyue,Li, Pengwei,Niu, Suhao,et al. An acetyl-dependent proofreading mechanism governs synthetic fidelity in Phytophthora sojae chitin synthase[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2026,811:7.
APA Zhang, Xiaoyue.,Li, Pengwei.,Niu, Suhao.,Gao, Kun.,Sun, Mengsi.,...&Bi, Yunchen.(2026).An acetyl-dependent proofreading mechanism governs synthetic fidelity in Phytophthora sojae chitin synthase.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,811,7.
MLA Zhang, Xiaoyue,et al."An acetyl-dependent proofreading mechanism governs synthetic fidelity in Phytophthora sojae chitin synthase".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 811(2026):7.

入库方式： OAI收割

来源：海洋研究所

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