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Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells

文献类型：期刊论文

作者Hu, Hao7; Hu, Wei7; Guo, An-Di7; Zhai, Linhui6,7; Ma, Song7; Nie, Hui-Jun7; Zhou, Bin-Shan7; Liu, Tianxian7; Jia, Xinglong7; Liu, Xing4,5
刊名NATURE COMMUNICATIONS
出版日期2024-02-17
卷号15期号:1页码:15
DOI10.1038/s41467-024-45765-3
通讯作者Tan, Minjia(mjtan@simm.ac.cn) ; Chen, Xiao-Hua(xhchen@simm.ac.cn)
英文摘要Protein-modifying enzymes regulate the dynamics of myriad post-translational modification (PTM) substrates. Precise characterization of enzyme-substrate associations is essential for the molecular basis of cellular function and phenotype. Methods for direct capturing global substrates of protein-modifying enzymes in living cells are with many challenges, and yet largely unexplored. Here, we report a strategy to directly capture substrates of lysine-modifying enzymes via PTM-acceptor residue crosslinking in living cells, enabling global profiling of substrates of PTM-enzymes and validation of PTM-sites in a straightforward manner. By integrating enzymatic PTM-mechanisms, and genetically encoding residue-selective photo-crosslinker into PTM-enzymes, our strategy expands the substrate profiles of both bacterial and mammalian lysine acylation enzymes, including bacterial lysine acylases PatZ, YiaC, LplA, TmcA, and YjaB, as well as mammalian acyltransferases GCN5 and Tip60, leading to discovery of distinct yet functionally important substrates and acylation sites. The concept of direct capturing substrates of PTM-enzymes via residue crosslinking may extend to the other types of amino acid residues beyond lysine, which has the potential to facilitate the investigation of diverse types of PTMs and substrate-enzyme interactive proteomics. Here the authors report a strategy to directly capture substrates of lysine-modifying enzymes via post-translational modification (PTM)-acceptor residue crosslinking in living cells, enabling global profiling of substrates of PTM-enzymes and validation of PTM-sites in a straightforward manner.
WOS关键词PROTEIN-PROTEIN INTERACTIONS ; CROSS-LINKING ; MASS-SPECTROMETRY ; ESCHERICHIA-COLI ; AMINO-ACIDS ; IDENTIFICATION ; SPECIFICITY ; PLATFORM
资助项目National Natural Science Foundation of China (National Science Foundation of China)[92053106] ; National Natural Science Foundation of China (National Science Foundation of China)[22225702] ; National Natural Science Foundation of China (National Science Foundation of China)[92153302] ; National Natural Science Foundation of China (National Science Foundation of China)[2022YFA1303100] ; National Natural Science Foundation of China (National Science Foundation of China)[32090040] ; National Natural Science Foundation of China (National Science Foundation of China)[81821005] ; National Natural Science Foundation of China (National Science Foundation of China)[21907100] ; National Science Foundation of China[2019M661670] ; China Postdoctoral Science Foundation[2020YFE0202200] ; National Key Science & Technology Program of China[SHSMU-ZDCX20212700] ; Innovative Research Team of High-Level Local Universities in Shanghai
WOS研究方向Science & Technology - Other Topics
语种英语
WOS记录号WOS:001163800700007
出版者NATURE PORTFOLIO
源URL[http://119.78.100.183/handle/2S10ELR8/310394]  
专题新药研究国家重点实验室
通讯作者Tan, Minjia; Chen, Xiao-Hua
作者单位1.Univ Chinese Acad Sci, Hangzhou Inst Adv Study, Sch Pharmaceut Sci & Technol, Hangzhou 310024, Peoples R China
2.Chinese Acad Sci, Zhongshan Inst Drug Discovery, Shanghai Inst Mat Med, Zhongshan 528400, Guangdong, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.Univ Sci & Technol China, Hefei Natl Ctr Phys Sci Microscale, Hefei 230026, Peoples R China
5.Univ Sci & Technol China, MOE Key Lab Cellular Dynam, Hefei 230027, Peoples R China
6.Tongji Univ, Shanghai Peoples Hosp 4, Translat Res Inst Brain & Brain Like Intelligence, Sch Med, Shanghai 200434, Peoples R China
7.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China
推荐引用方式
GB/T 7714		 Hu, Hao,Hu, Wei,Guo, An-Di,et al. Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells[J]. NATURE COMMUNICATIONS,2024,15(1):15.
APA Hu, Hao.,Hu, Wei.,Guo, An-Di.,Zhai, Linhui.,Ma, Song.,...&Chen, Xiao-Hua.(2024).Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells.NATURE COMMUNICATIONS,15(1),15.
MLA Hu, Hao,et al."Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells".NATURE COMMUNICATIONS 15.1(2024):15.

入库方式： OAI收割

来源：上海药物研究所

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