title: Analysis of the serine/threonine/tyrosine phosphoproteome of the pathogenic bacterium Listeria monocytogenes reveals phosphorylated proteins related to virulence.
abstract: Phosphorylation is the most common and widely studied post-translational protein modification in bacteria. It plays an important role in all kinds of cellular processes and controls key regulatory mechanisms, including virulence in certain pathogens. To gain insight into the role of protein phosphorylation in the pathogen Listeria monocytogenes, the serine (Ser), threonine (Thr) and tyrosine (Tyr) phosphoproteome of this bacterium was determined. We used the "gel free" proteomic approach with high accuracy mass spectrometry after enrichment of phosphopeptides. A total of 143 sites of phosphorylation were clearly identified, on 155 unique peptides of 112 phosphoproteins. The Ser/Thr/Tyr phosphorylation site distribution was 93:43:7. All identified phosphopeptides are monophosphorylated, except one and many identified phosphoproteins are related to virulence, translation, phosphoenolpyruvate:sugar phosphotransferase system, glycolysis and stress response. A description of these phosphoproteins is provided together with a comparison of the phosphosites in the L. monocytogenes proteins and in their homologues of other bacteria for which the phosphoproteome has been determined. Compared with the previous studies, we noticed a more extended conservation of the phosphorylation sites in glycolytic enzymes as well as ribosomal proteins.
authors.affiliation: INRA, UMR Micalis, Jouy-en-Josas, France. sandeepkmisra@gmail.com
authors.forename: Sandeep K
authors.initials: SK
authors.lastname: Misra
authors.forename: Eliane
authors.initials: E
authors.lastname: Milohanic
authors.forename: Francine
authors.initials: F
authors.lastname: Aké
authors.forename: Ivan
authors.initials: I
authors.lastname: Mijakovic
authors.forename: Josef
authors.initials: J
authors.lastname: Deutscher
authors.forename: Véronique
authors.initials: V
authors.lastname: Monnet
authors.forename: Céline
authors.initials: C
authors.lastname: Henry
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism*; D008089:Listeria monocytogenes / Q000378:metabolism / Q000472:pathogenicity*; D008969:Molecular Sequence Data; D010748:Phosphopeptides / Q000032:analysis / Q000378:metabolism; D010750:Phosphoproteins / Q000032:analysis / Q000378:metabolism*; D010766:Phosphorylation; D040901:Proteomics / Q000379:methods*; D012694:Serine / Q000032:analysis / Q000378:metabolism*; D013912:Threonine / Q000032:analysis / Q000378:metabolism*; D014443:Tyrosine / Q000032:analysis / Q000378:metabolism*; D014774:Virulence
chemical_list: D001426:Bacterial Proteins; D010748:Phosphopeptides; D010750:Phosphoproteins; D013912:Threonine; D014443:Tyrosine; D012694:Serine