Abstract
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.
Highlights
Phosphorylation of amino acid residues on proteins is an important and common post-translational modification in both eukaryotes and prokaryotes
We previously performed phosphoproteome analyses of various bacterial species [13,14,15], and showed that trypsindigested phosphorylated peptides could be enriched by titanium dioxide (TiO2) chromatography [23, 24] followed by liquid chromatography (LC)-Mass spectrometry (MS)/MS analysis (Fig. 1)
We showed that Ser/Thr/ Tyr phosphorylations can be clearly characterized, but phosphorylation of other amino acid residues remains unclear
Summary
Phosphorylation of amino acid residues on proteins is an important and common post-translational modification in both eukaryotes and prokaryotes. Various amino acid residues within a protein, including serine, threonine, tyrosine, histidine and aspartate, can be modified with a phosphate group [5, 6]. A plethora of data related to serine, threonine and tyrosine phosphorylations have already been reported. They are shown to be involved in changing metabolic behaviors, inducing capsule formation and initiating sporulation [5]. The knowledge of histidine and aspartate phosphorylations are mostly limited to the two-component systems [7], in which phosphor-relaying signaling events were induced by external environmental stimuli, including
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