2016-J Proteome Res-大肠杆菌中丙二酰化组谱的分析揭示其参与细胞代谢过程.pdfVIP

Article /jpr Global Profiling of Protein Lysine Malonylation in Escherichia coli Reveals Its Role in Energy Metabolism Lili Qian,†,‡, ∥ Litong Nie,†,‡, ∥ Ming Chen,†,‡ Ping Liu,†,‡ Jun Zhu, # Linhui Zhai,†,‡ Sheng-ce Tao,⊥ Zhongyi Cheng,# Yingming Zhao,†,‡,§ and Minjia Tan*,†,‡ †The Chemical Proteomics Center and State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, PR China ‡University of Chinese Academy of Sciences, Beijing 100049, PR China # Jingjie PTM BioLab (Hangzhou) Co. Ltd, Hangzhou 310018, PR China ⊥Shanghai Center for Systems Biomedicine, Key Laboratory of Systems Biomedicine (Ministry of Education), Shanghai Jiao Tong University, Shanghai 200240, PR China §Ben May Department for Cancer Research, University of Chicago, Chicago, Illinois 60637, United States S *Supporting Information ABSTRACT: Protein lysine malonylation is a recently identified post-translational modification (PTM), which is evolutionarily conserved from bacteria to mammals. Although analysis of lysine malonylome in mammalians suggested that this modification was related to energy metabolism, the substrates and biological roles of malonylation in prokaryotes are still poorly understood. In this study, we performed qualitative and quantitative analyses to globally identify lysine malonylation substrates in Escherichia coli. We identified 1745 malonylation sites in 594 proteins in E. coli, representing the first and largest malonylome data set in prokaryotes up to date. Bioinformatic analyses showed that