Characterization of Protein Lysine Propionylation in Escherichia coli: Global Profiling, Dynamic Change, and Enzymatic Regulation

doi:10.1021/acs.jproteome.6b00798

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	Characterization of Protein Lysine Propionylation in Escherichia coli: Global Profiling, Dynamic Change, and Enzymatic Regulation
	Sun, Mingwei 1,2,3; Xu, Junyu 1,2,6; Wu, Zhixiang 5; Zhai, Linhui 1,2,3; Liu, Chengxi 7; Cheng, Zhongyi 8; Xu, Guofeng 5; Tao, Shengce 7; Ye, Bang-Ce 6; Zhao, Yingming1,2,4
刊名	JOURNAL OF PROTEOME RESEARCH
	2016-12
卷号	15 期号:12 页码:4696-4708
关键词	post-translational modification(s) lysine propionylation SILAC CobB PatZ
ISSN号	1535-3893
DOI	10.1021/acs.jproteome.6b00798
文献子类	Article
英文摘要	Propionylation at protein lysine residue is characterized to be present in both eukaryotic and prokaryotic species. However, the majority of lysine propionylation substrates still remain largely unknown. Using affinity enrichment and mass spectrometric-based proteomics, we identified 1467 lysine propionylation sites in 603 proteins in E. coli. Quantitative propionylome analysis further revealed that global lysine propionylation level was drastically increased in response to propionate treatment, a carbon source for many microorganisms and also a common food preservative. The results indicated that propionylation may play a regulatory role in propionate metabolism and propionyl-CoA degradation. In contrast with lysine acetylation and succinylation, our results revealed that the lysine propionylation level of substrates showed an obvious decrease in response to high glucose, suggesting a distinct role of propionylation in bacteria carbohydrate metabolism. This study further showed that bacterial lysine deacetylase CobB and acetyltransferase PatZ could also have regulatory activities for lysine propionylation in E. coli. Our quantitative propionylation substrate analysis between cobB wild-type and cobB knockout strain led to the identification of 13 CobB potentially regulated propionylation sites. Together, these findings revealed the broad propionylation substrates in E. coli and suggested new roles of lysine propionylation in bacterial physiology.
资助项目	National Basic Research Program of China (973 Program)[2014CBA02004] ; Natural Science Foundation of China[31670066] ; Natural Science Foundation of China[31370813] ; National Science & Technology Major Project[2014ZX09507-002] ; Shanghai Municipal Science and Technology Commission[14DZ2261100] ; Shanghai Municipal Science and Technology Commission[16YF1414000] ; Shanghai Municipal Science and Technology Commission[15410723100] ; Strategic Priority Research Program of the Chinese Academy of Sciences, "Personalized Medicines-Molecular Signature-based Drug Discovery and Development"[XDA12020314] ; National Institutes of Health (NIH) of the United States[GM105933] ; National Institutes of Health (NIH) of the United States[CA160036]
WOS关键词	ACETYL-COA SYNTHETASE ; POSTTRANSLATIONAL MODIFICATIONS ; INTERACTION NETWORKS ; PROTEOMICS ; IDENTIFICATION ; SUCCINYLATION ; MALONYLATION ; METABOLISM ; PROPIONATE ; OXIDATION
WOS研究方向	Biochemistry & Molecular Biology
语种	英语
出版者	AMER CHEMICAL SOC
WOS记录号	WOS:000389396500045
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/275780]
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
作者单位	1.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China; 2.Chinese Acad Sci, Shanghai Inst Mat Med, Chem Prote Ctr, Shanghai 201203, Peoples R China; 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China; 4.Univ Chicago, Ben May Dept Canc Res, Chicago, IL 60637 USA; 5.Shanghai Jiao Tong Univ, Xinhua Hosp, Dept Pediat Surg, Sch Med, 1665 Kongjiang Rd, Shanghai 200092, Peoples R China; 6.East China Univ Sci & Technol, Lab Biosyst & Microanal, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China; 7.Shanghai Jiao Tong Univ, Shanghai Ctr Syst Biomed, Key Lab Syst Biomed, Minist Educ, Shanghai 200240, Peoples R China; 8.Jingjie PTM BioLab Hangzhou Co Ltd, Hangzhou 310018, Zhejiang, Peoples R China
推荐引用方式 GB/T 7714	Sun, Mingwei,Xu, Junyu,Wu, Zhixiang,et al. Characterization of Protein Lysine Propionylation in Escherichia coli: Global Profiling, Dynamic Change, and Enzymatic Regulation[J]. JOURNAL OF PROTEOME RESEARCH,2016,15(12):4696-4708.
APA	Sun, Mingwei.,Xu, Junyu.,Wu, Zhixiang.,Zhai, Linhui.,Liu, Chengxi.,...&Tan, Minjia.(2016).Characterization of Protein Lysine Propionylation in Escherichia coli: Global Profiling, Dynamic Change, and Enzymatic Regulation.JOURNAL OF PROTEOME RESEARCH,15(12),4696-4708.
MLA	Sun, Mingwei,et al."Characterization of Protein Lysine Propionylation in Escherichia coli: Global Profiling, Dynamic Change, and Enzymatic Regulation".JOURNAL OF PROTEOME RESEARCH 15.12(2016):4696-4708.