Characterization of Protein Lysine Propionylation in Escherichia coli: Global Profiling, Dynamic Change, and Enzymatic Regulation.
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.
The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203, P. R. China.|University of Chinese Academy of Sciences , Beijing 100049, P. R. China.
Mingwei
M
Sun
The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203, P. R. China.|Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology , Shanghai 200237, P. R. China.
Junyu
J
Xu
Pediatric Surgery Department, Xinhua Hospital, Shanghai Jiao Tong University School of Medicine , 1665 Kongjiang Road, Shanghai 200092, P. R. China.
Zhixiang
Z
Wu
The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203, P. R. China.|University of Chinese Academy of Sciences , Beijing 100049, P. R. China.
Linhui
L
Zhai
Shanghai Center for Systems Biomedicine, Key Laboratory of Systems Biomedicine (Ministry of Education), Shanghai Jiao Tong University , Shanghai 200240, P. R. China.
Chengxi
C
Liu
Jingjie PTM BioLab (Hangzhou) Co. Ltd , Hangzhou 310018, P. R. China.
Zhongyi
Z
Cheng
Pediatric Surgery Department, Xinhua Hospital, Shanghai Jiao Tong University School of Medicine , 1665 Kongjiang Road, Shanghai 200092, P. R. China.
Guofeng
G
Xu
Shanghai Center for Systems Biomedicine, Key Laboratory of Systems Biomedicine (Ministry of Education), Shanghai Jiao Tong University , Shanghai 200240, P. R. China.
Shengce
S
Tao
Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology , Shanghai 200237, P. R. China.
Bang-Ce
BC
Ye
The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203, P. R. China.|Ben May Department for Cancer Research, University of Chicago , Chicago, Illinois 60637, United States.
Yingming
Y
Zhao
The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203, P. R. China.|University of Chinese Academy of Sciences , Beijing 100049, P. R. China.
Minjia
M
Tan
D000123:Acetyltransferases / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism / Q000502:physiology; D008239:Lysine / Q000378:metabolism*; D011422:Propionates / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D040901:Proteomics; D037761:Sirtuins / Q000502:physiology
D029968:Escherichia coli Proteins; D011422:Propionates; D000123:Acetyltransferases; D037761:Sirtuins; C483998:cobB protein, E Coli; C029658:propionic acid; D008239:Lysine
CobB; PatZ; SILAC; lysine propionylation; post-translational modification(s)