ORIGINAL RESEARCH published: 27 November 2017 doi: 10.3389/fmolb.2017.00077 Acetylome of Acinetobacter baumannii SK17 Reveals a Highly-Conserved Modification of Histone-Like Protein HU Jiahn-Haur Liao 1†, Cheng-Han Tsai 2†, Sanjay G. Patel 3†, Jhih-Tian Yang 1, 4, I-Fan Tu 1, Matteo Lo Cicero 3, Magdalena Lipka-Lloyd 3, Wan-Ling Wu 1, Wen-Jie Shen 2, Meng-Ru Ho 1, Chi-Chi Chou 1, Garima R. Sharma 3, 5, Hiroki Okanishi 6, Louis Y. P. Luk 3, Yu-Hsuan Tsai 3* and Shih-Hsiung Wu 1, 2, 7* 1 Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, 2 Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan, 3 School of Chemistry, Cardiff University, Cardiff, United Kingdom, 4 Ph.D. Program in Microbial Genomics, National Chung Hsing University, Academia Sinica, Taipei, Taiwan, 5 Republic Polytechnic, Singapore, Singapore, 6 Department of Tumor Genetics and Biology, Kumamoto University, Kumamoto, Japan, 7 Department of Chemistry, National Taiwan University, Taipei, Taiwan Edited by: Xuechen Li, Lysine acetylation is a prevalent post-translational modification in both eukaryotes and University of Hong Kong, Hong Kong prokaryotes. Whereas this modification is known to play pivotal roles in eukaryotes, the Reviewed by: Qiang Wang, function and extent of this modification in prokaryotic cells remain largely unexplored. Institute of Hydrobiology (CAS), China Here we report the acetylome of a pair of antibiotic-sensitive and -resistant nosocomial Xiang David Li, pathogen Acinetobacter baumannii SK17-S and SK17-R. A total of 145 lysine acetylation University of Hong Kong, Hong Kong sites on 125 proteins was identified, and there are 23 acetylated proteins found in *Correspondence: Yu-Hsuan Tsai both strains, including histone-like protein HU which was found to be acetylated
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