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Characterization of diverse lysine acylations in Bacillus thuringiensis: Substrate profiling and functional exploration

文献类型：期刊论文

作者Liu, Tianxian5,6; Zhang, Mingya5; Fan, Yameng4; Zhao, Lei3,5; Huang, Dan6; Zhao, Liuchang6; Tan, Minjia1,2,3,4,5; Ye, Bang-Ce6; Xu, Jun-Yu1,2,3,5
刊名PROTEOMICS
出版日期2024-03-15
页码13
关键词Bacillus thuringiensis conservative analysis in various species lysine acylation regulatory mechanism substrate characterization
ISSN号1615-9853
DOI10.1002/pmic.202300350
通讯作者Tan, Minjia(mjtan@simm.ac.cn) ; Ye, Bang-Ce(bcye@ecust.edu.cn) ; Xu, Jun-Yu(jyxu@simm.ac.cn)
英文摘要Lysine acylation has been extensively investigated due to its regulatory role in a diverse range of biological functions across prokaryotic and eukaryotic species. In-depth acylomic profiles have the potential to enhance comprehension of the biological implications of organisms. However, the extent of research on global acylation profiles in microorganisms is limited. Here, four lysine acylomes were conducted in Bacillus thuringiensis by using the LC-MS/MS based proteomics combined with antibody-enrichment strategies, and a total of 3438 acetylated sites, 5797 propionylated sites, 1705 succinylated sites, and 925 malonylated sites were identified. The motif analysis of these modified proteins revealed a high conservation of glutamate in acetylation and propionylation, whereas such conservation was not observed in succinylation and malonylation modifications. Besides, conservation analysis showed that homologous acylated proteins in Bacillus subtilis and Escherichia coli were connected with ribosome and aminoacyl-tRNA biosynthesis. Further biological experiments showed that lysine acylation lowered the RNA binding ability of CodY and impaired the in vivo protein activity of MetK. In conclusion, our study expanded the current understanding of the global acylation in Bacillus, and the comparative analysis demonstrated that shared acylation proteins could play important roles in regulating both metabolism and RNA transcription progression.
WOS关键词METABOLIC-REGULATION ; GENE-EXPRESSION ; PROTEIN ; ACETYLATION ; CODY ; IDENTIFICATION ; SUCCINYLATION ; MALONYLATION ; COBB
资助项目National Natural Science Foundation of China ; Youth Science and Technology Talents in Shanghai Sail Plan of China[21YF1456000] ; Young Elite Scientists Sponsorship Program by CAST[2022QNRC001] ; Shanghai Rising-Star Program[22QA1411100] ; Youth Innovation Promotion Association[CAS2021276] ; Sanofi scholarship program ; Guangdong High-level New R&D Institute, China[:2019B090904008] ; Guangdong High-level Innovative Research Institute, China[:2021B0909050003] ; [32322048] ; [22134003]
WOS研究方向Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:001185787100001
出版者WILEY
源URL[http://119.78.100.183/handle/2S10ELR8/310154]  
专题新药研究国家重点实验室
通讯作者Tan, Minjia; Ye, Bang-Ce; Xu, Jun-Yu
作者单位1.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China
2.Jiangsu Ocean Univ, Coll Pharm, Jiangsu Key Lab Marine Pharmaceut Cpd Screening, Lianyungang, Peoples R China
3.Chinese Acad Sci, Zhongshan Inst Drug Discovery, Shanghai Inst Mat Med, Zhongshan, Peoples R China
4.Henan Univ, Sch Pharm, Kaifeng, Peoples R China
5.Chinese Acad Sci, State Key Lab Drug Res, Shanghai Inst Mat Med, Shanghai, Peoples R China
6.East China Univ Sci & Technol, Lab Biosyst & Microanal, State Key Lab Bioreactor Engn, Shanghai, Peoples R China
推荐引用方式
GB/T 7714		 Liu, Tianxian,Zhang, Mingya,Fan, Yameng,et al. Characterization of diverse lysine acylations in Bacillus thuringiensis: Substrate profiling and functional exploration[J]. PROTEOMICS,2024:13.
APA Liu, Tianxian.,Zhang, Mingya.,Fan, Yameng.,Zhao, Lei.,Huang, Dan.,...&Xu, Jun-Yu.(2024).Characterization of diverse lysine acylations in Bacillus thuringiensis: Substrate profiling and functional exploration.PROTEOMICS,13.
MLA Liu, Tianxian,et al."Characterization of diverse lysine acylations in Bacillus thuringiensis: Substrate profiling and functional exploration".PROTEOMICS (2024):13.

入库方式： OAI收割

来源：上海药物研究所

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