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Submitted on December 23, 2003
Dept. of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143-0446
Corresponding Author: alb{at}itsa.ucsf.edu
Protein sulfonation on serine and threonine residues is described for the first time. This posttranslational 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 posttranslational modification was carried out using liquid chromatography coupled to electrospray tandem mass spectrometry on proteins including a neuronal intermediate filament and 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.
Revised on January 28, 2004
Accepted on January 29, 2004
O-Sulfonation of serine and threonine - mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes
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