Abstract
Reversible protein phosphorylation at serine, threonine and tyrosine is a well-known dynamic post-translational modification with stunning regulatory and signalling functions in eukaryotes. Shotgun phosphoproteomic analyses revealed that this post-translational modification is dramatically lower in bacteria than in eukaryotes. However, Ser/Thr/Tyr phosphorylation is present in all analysed bacteria (24 eubacteria and 1 archaea). It affects central processes, such as primary and secondary metabolism development, sporulation, pathogenicity, virulence or antibiotic resistance. Twenty-nine phosphoprotein orthologues were systematically identified in bacteria: ribosomal proteins, enzymes from glycolysis and gluconeogenesis, elongation factors, cell division proteins, RNA polymerases, ATP synthases and enzymes from the citrate cycle. While Ser/Thr/Tyr phosphorylation exists in bacteria, there is a consensus that histidine phosphorylation is the most abundant protein phosphorylation in prokaryotes. Unfortunately, histidine shotgun phosphorproteomics is not possible due to the reduced phosphohistidine half-life under the acidic pH conditions used in standard LC-MS/MS analysis. However, considering the fast and continuous advances in LC-MS/MS-based phosphoproteomic methodologies, it is expected that further innovations will allow for the study of His phosphoproteomes and a better coverage of bacterial phosphoproteomes. The characterisation of the biological role of bacterial Ser/Thr/Tyr and His phosphorylations might revolutionise our understanding of prokaryotic physiology.
Highlights
Phosphoproteomics involves the analysis of a complete set of phosphorylation sites present in a cell
We review the state of the art and the challenges of bacterial Ser/Thr/Tyr and His phosphoproteomics
We describe the state of the art of a large bacterial dataset of Ser/Thr/Tyr phosphorylation identified using gel-based and LC-mass spectrometry (MS)/MS-based methodologies
Summary
Phosphoproteomics involves the analysis of a complete set of phosphorylation sites present in a cell. Mycobacterium tuberculosis harbours the largest bacterial pohosphoproteome described as consisting of 500 Ser/Thr/Tyr phosphorylation sites from 301 proteins [3]. While Ser/Thr/Tyr phosphorylation exists in bacteria, there is a consensus about that histidine phosphorylation is the most abundant protein phosphorylation in prokaryotes [4] These residues have almost not been subjected to phosphoproteomic analyses. Classical protein chemistry phosphoproteomic approaches require protein purification, peptide mapping and identification of phosphorylated peptide regions and sites by N-terminal sequence analysis. These kinds of analyses are tedious, and they could cover only one phosphoprotein or a few phosphoproteins. We describe the state of the art of a large bacterial dataset of Ser/Thr/Tyr phosphorylation identified using gel-based and LC-MS/MS-based methodologies
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