Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance

BMC Microbiology

Research Article

Wan-Ling Wu¹  Shu-Jung Lai¹  I-Fan Tu¹  Shih-Hsiung Wu²  Jhih-Tian Yang³  Mei-Chin Lai⁴  Louis Y. P. Luk⁵  Yu-Hsuan Tsai⁵ 

[1] Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan;Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan;Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Academia Sinica, Taipei, Taiwan;Department of Chemistry, National Taiwan University, Taipei, Taiwan;PhD Program in Microbial Genomics, National Chung Hsing University and Academia Sinica, Taichung, Taiwan;PhD Program in Microbial Genomics, National Chung Hsing University and Academia Sinica, Taichung, Taiwan;Department of Life Sciences, National Chung Hsing University, Taichung, Taiwan;School of Chemistry, Cardiff University, Cardiff, UK;

关键词: Proteomics;    Post-translational modification;    Histidine phosphorylation;    Aspartate phosphorylation;    Pathogenic bacteria;    Drug resistance;   

DOI  :  10.1186/s12866-017-1034-2

 received in 2017-02-10, accepted in 2017-05-15,  发布年份 2017

来源: Springer

【 摘 要 】

BackgroundPhosphorylation of amino acid residues on proteins is an important and common post-translational modification in both eukaryotes and prokaryotes. Most research work has been focused on phosphorylation of serine, threonine or tyrosine residues, whereas phosphorylation of other amino acids are significantly less clear due to the controversy on their stability under standard bioanalytical conditions.ResultsHere we applied a shotgun strategy to analyze the histidine and aspartate phosphorylations in different microbes. Our results collectively indicate that histidine and aspartate phosphorylations frequently occur also in proteins that are not part of the two-component systems. Noticeably, a number of the modified proteins are pathogenesis-related or essential for survival in host. These include the zinc ion periplasmic transporter ZnuA in Acinetobacter baumannii SK17, the multidrug and toxic compound extrusion (MATE) channel YeeO in Klebsiella pneumoniae NTUH-K2044, branched amino acid transporter AzlC in Vibrio vulnificus and the RNA-modifying pseudouridine synthase in Helicobacter pylori.ConclusionsIn summary, histidine and aspartate phosphorylation is likely to be ubiquitous and to take place in proteins of various functions. This work also sheds light into how these functionally important proteins and potential drug targets might be regulated at a post-translational level.

【 授权许可】

CC BY   
© The Author(s). 2017