中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Protein Acylation is a General Regulatory Mechanism in Biosynthetic Pathway of Acyl-CoA-Derived Natural Products

文献类型:期刊论文

作者Xu, Jun-Yu1,2,3; Xu, Ya3; Xu, Zhen3; Zhai, Lin-Hui1; Ye, Yang1; Zhao, Yingming1,4; Chu, Xiaohe2; Tan, Minjia1; Ye, Bang-Ce2,3
刊名CELL CHEMICAL BIOLOGY
出版日期2018-08-16
卷号25期号:8页码:984-+
ISSN号2451-9448
DOI10.1016/j.chembiol.2018.05.005
文献子类Article
英文摘要Coenzyme A (CoA) esters of short fatty acids (acyl-CoAs) function as key precursors for the biosynthesis of various natural products and the dominant donors for lysine acylation. Herein, we investigated the functional interplay between beneficial and adverse effects of acyl-CoA supplements on the production of acyl-CoA-derived natural products in microorganisms by using erythromycin-biosynthesized Saccharopolyspora erythraea as a model: accumulation of propionyl-CoA benefited erythromycin biosynthesis, but lysine propionylation inhibited the activities of important enzymes involved in biosynthetic pathways of erythromycin. The results showed that the overexpression of NAD(+)-dependent deacylase could circumvent the inhibitory effects of high acyl-CoA concentrations. In addition, we demonstrated the similar lysine acylation mechanism in other acyl-CoA-derived natural product biosynthesis, such as malonyl-CoA-derived alkaloid and butyryl-CoA-derived bioalcohol. These observations systematically uncovered the important role of protein acylation on interaction between the accumulation of high concentrations of acyl-CoAs and the efficiency of their use in metabolic pathways.
WOS关键词S-ADENOSYLMETHIONINE SYNTHETASE ; LYSINE ACETYLATION ; ESCHERICHIA-COLI ; SACCHAROPOLYSPORA-ERYTHRAEA ; QUANTITATIVE PROTEOMICS ; BACTERIAL PRODIGININES ; METABOLIC-REGULATION ; POLYKETIDE SYNTHASE ; STRAIN IMPROVEMENT ; SYSTEMS BIOLOGY
资助项目National Natural Science Foundation of China[31730004] ; National Natural Science Foundation of China[21335003] ; National Natural Science Foundation of China[21575089] ; National Natural Science Foundation of China[91753203] ; Special Project on Precision Medicine under National Key RD Program[SQ2017YFSF090210]
WOS研究方向Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:000441791200008
出版者CELL PRESS
源URL[http://119.78.100.183/handle/2S10ELR8/279618]  
专题化学蛋白质组学研究中心
中科院受体结构与功能重点实验室
新药研究国家重点实验室
通讯作者Tan, Minjia; Ye, Bang-Ce
作者单位1.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China;
2.Zhejiang Univ Technol, Coll Pharmaceut Sci, Collaborat Innovat Ctr Yangtze River Delta Reg Gr, Hangzhou 310014, Zhejiang, Peoples R China;
3.East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Lab Biosyst & Microanal, Shanghai 200237, Peoples R China;
4.Univ Chicago, Ben May Dept Canc Res, Chicago, IL 60637 USA
推荐引用方式
GB/T 7714
Xu, Jun-Yu,Xu, Ya,Xu, Zhen,et al. Protein Acylation is a General Regulatory Mechanism in Biosynthetic Pathway of Acyl-CoA-Derived Natural Products[J]. CELL CHEMICAL BIOLOGY,2018,25(8):984-+.
APA Xu, Jun-Yu.,Xu, Ya.,Xu, Zhen.,Zhai, Lin-Hui.,Ye, Yang.,...&Ye, Bang-Ce.(2018).Protein Acylation is a General Regulatory Mechanism in Biosynthetic Pathway of Acyl-CoA-Derived Natural Products.CELL CHEMICAL BIOLOGY,25(8),984-+.
MLA Xu, Jun-Yu,et al."Protein Acylation is a General Regulatory Mechanism in Biosynthetic Pathway of Acyl-CoA-Derived Natural Products".CELL CHEMICAL BIOLOGY 25.8(2018):984-+.

入库方式: OAI收割

来源:上海药物研究所

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