Substrate and functional characterization of the lysine acetyltransferase MsKat and deacetylase MsCobB in Mycobacterium smegmatis
文献类型：期刊论文
| 作者 | Kan, Yunbo1,4,5; Xie, Shuyu3; Sun, Yuwen2; Ye, Tong3; Bian, Yunxu2,4,5; Guo, Fang1; Zhang, Mingya4; Liu, Tianxian4; Liu, Tianqi2; Ji, Jing5 |
| 刊名 | JOURNAL OF PROTEOMICS
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| 出版日期 | 2024-05-30 |
| 卷号 | 300页码:10 |
| 关键词 | Lysine acetylation Mycobacteria Regulatory enzyme MsKat MsCobB |
| ISSN号 | 1874-3919 |
| DOI | 10.1016/j.jprot.2024.105177 |
| 通讯作者 | Liu, Bin(liubin@jou.edu.cn) ; Tan, Minjia(mjtan@simm.ac.cn) ; Xu, Jun- Yu(jyxu@simm.ac.cn) |
| 英文摘要 | Tuberculosis (TB) is a serious cause of infectious death worldwide. Recent studies have reported that about 30% of the Mtb proteome was modified post-translationally, indicating that their functions are essential for drug resistance, mycobacterial survival, and pathogenicity. Among them, lysine acetylation, reversibly regulated by acetyltransferase and deacetylase, has important roles involved in energy metabolism, cellular adaptation, and protein interactions. However, the substrate and biological functions of these two important regulatory enzymes remain unclear. Herein, we utilized the non-pathogenic M. smegmatis strain as a model and systematically investigated the dynamic proteome changes in response to the overexpressing of MsKat/MsCobB in mycobacteria. A total of 4179 proteins and 1236 acetylated sites were identified in our data. Further analysis of the dynamic changes involved in proteome and acetylome showed that MsKat/MsCobB played a regulatory role in various metabolic pathways and nucleic acid processes. After that, the quantitative mass spectrometric method was utilized and proved that the AMP-dependent synthetase, Citrate synthase, ATP-dependent specificity component of the Clp protease, and ATP-dependent DNA/RNA helicases were identified to be the substrates of MsKat. Overall, our study provided an important resource underlying the substrates and functions of the acetylation regulatory enzymes in mycobacteria. Significance: In this study, we systematically analyzed the dynamic molecular changes in response to the MsKat/ MsCobB overexpression in mycobacteria at proteome and lysine acetylation level by using a TMT-based quantitative proteomic approach. Pathways related with glycolysis, degradation of branched chain amino acids, phosphotransferase system were affected after disturbance of the two regulates enzymes involved in lysine acetylation. We also proved that AMP-dependent synthetase Clp protease, ATP-dependent DNA/RNA helicases and citrate synthase was the substrate of MsKat according to our proteomic data and biological validation. Together, our study underlined the substrates and functions of the acetylation regulatory enzymes in mycobacteria. |
| WOS关键词 | REVERSIBLE ACETYLATION ; PROPIONATE METABOLISM ; ANALYSIS REVEALS ; FATTY-ACID ; TUBERCULOSIS ; PROTEIN ; INVOLVEMENT ; ACETATE |
| 资助项目 | National Natural Science Foundation of China[32322048] ; 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] |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:001233123700001 |
| 出版者 | ELSEVIER |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/311809]  |
| 专题 | 新药研究国家重点实验室 |
| 通讯作者 | Liu, Bin; Tan, Minjia; Xu, Jun- Yu |
| 作者单位 | 1.Shanghai Easymass Co Ltd, Shanghai 201318, Peoples R China 2.Chinese Acad Sci, Zhongshan Inst Drug Discovery, Shanghai Inst Mat Med, Guangzhou, Guangdong, Peoples R China 3.Nanjing Univ Chinese Med, Sch Chinese Mat Med, Nanjing 210023, Jiangsu, Peoples R China 4.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China 5.Jiangsu Ocean Univ, Coll Pharm, Jiangsu Key Lab Marine Pharmaceut Cpd Screening, Lianyungang, Peoples R China |
| 推荐引用方式 GB/T 7714 | Kan, Yunbo,Xie, Shuyu,Sun, Yuwen,et al. Substrate and functional characterization of the lysine acetyltransferase MsKat and deacetylase MsCobB in Mycobacterium smegmatis[J]. JOURNAL OF PROTEOMICS,2024,300:10. |
| APA | Kan, Yunbo.,Xie, Shuyu.,Sun, Yuwen.,Ye, Tong.,Bian, Yunxu.,...&Xu, Jun- Yu.(2024).Substrate and functional characterization of the lysine acetyltransferase MsKat and deacetylase MsCobB in Mycobacterium smegmatis.JOURNAL OF PROTEOMICS,300,10. |
| MLA | Kan, Yunbo,et al."Substrate and functional characterization of the lysine acetyltransferase MsKat and deacetylase MsCobB in Mycobacterium smegmatis".JOURNAL OF PROTEOMICS 300(2024):10. |
入库方式： OAI收割
来源：上海药物研究所
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