Abstract
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.
Original language | English (US) |
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Pages (from-to) | 429-443 |
Number of pages | 15 |
Journal | Molecular and Cellular Proteomics |
Volume | 3 |
Issue number | 5 |
DOIs | |
State | Published - May 2004 |
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry
- Molecular Biology