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Molecular & Cellular Proteomics 8:215-225, 2009.
© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Lysine Acetylation Is a Highly Abundant and Evolutionarily Conserved Modification in Escherichia Coli^*,S

Junmei Zhang^,, Robert Sprung^,,¶, Jimin Pei^,||, Xiaohong Tan^**, Sungchan Kim, Heng Zhu, Chuan-Fa Liu^**, Nick V. Grishin^,|| and Yingming Zhao^,¶¶

From the Department of Biochemistry, ^|| Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390, ^** Division of Chemical Biology and Biotechnology, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, the Department of Biochemistry, College of Medicine, Hallym University, Chuncheon, Kangwon-Do, Korea 200-702, and the Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Lysine acetylation and its regulatory enzymes are known to have pivotal roles in mammalian cellular physiology. However, the extent and function of this modification in prokaryotic cells remain largely unexplored, thereby presenting a hurdle to further functional study of this modification in prokaryotic systems. Here we report the first global screening of lysine acetylation, identifying 138 modification sites in 91 proteins from Escherichia coli. None of the proteins has been previously associated with this modification. Among the identified proteins are transcriptional regulators, as well as others with diverse functions. Interestingly, more than 70% of the acetylated proteins are metabolic enzymes and translation regulators, suggesting an intimate link of this modification to energy metabolism. The new dataset suggests that lysine acetylation could be abundant in prokaryotic cells. In addition, these results also imply that functions of lysine acetylation beyond regulation of gene expression are evolutionarily conserved from bacteria to mammals. Furthermore, we demonstrate that bacterial lysine acetylation is regulated in response to stress stimuli.

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