O-sulfonation of serine and threonine: mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes.

Medzihradszky KF, Darula Z, Perlson E, Fainzilber M, Chalkley RJ, Ball H, Greenbaum D, Bogyo M, Tyson DR, Bradshaw RA, Burlingame AL
Mol Cell Proteomics. 2004 3 (5): 429-40

PMID: 14752058 · DOI:10.1074/mcp.M300140-MCP200

Protein sulfonation on serine and threonine residues is described for the first time. This post-translational modification is shown to occur in proteins isolated from organisms representing a broad span of eukaryote evolution, including the invertebrate mollusk Lymnaea stagnalis, the unicellular malaria parasite Plasmodium falciparum, and humans. Detection and structural characterization of this novel post-translational modification was carried out using liquid chromatography coupled to electrospray tandem mass spectrometry on proteins including a neuronal intermediate filament and a myosin light chain from the snail, a cathepsin-C-like enzyme from the parasite, and the cytoplasmic domain of the human orphan receptor tyrosine kinase Ror-2. These findings suggest that sulfonation of serine and threonine may be involved in multiple functions including protein assembly and signal transduction.

MeSH Terms (15)

Animals Chromatography, Liquid Cloning, Molecular Humans Lymnaea Mass Spectrometry Myosin Light Chains Peptides Plasmodium falciparum Protein Processing, Post-Translational Protozoan Proteins Receptors, Cell Surface Receptor Tyrosine Kinase-like Orphan Receptors Serine Threonine

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