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Molecular & Cellular Proteomics 3:429-440, 2004.
© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

O-Sulfonation of Serine and Threonine

Mass Spectrometric Detection and Characterization of a New Posttranslational Modification in Diverse Proteins Throughout the Eukaryotes^*

From the ^a Department of Pharmaceutical Chemistry and Mass Spectrometry Facility, University of California, San Francisco, CA 94143; ^c Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel; ^d Institute for Neuroscience and ^f Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143; and ^h Department of Physiology and Biophysics, University of California, Irvine, CA 92697

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.

^e Current address: Department of Biochemistry, Southwestern Medical Center, University of Texas, Dallas, TX 75390-9050

^g Current address: Department of Pathology, Stanford University Medical School, Stanford, CA 94305-5324

ⁱ To whom correspondence should be addressed: Department of Pharmaceutical Chemistry, University of California, 513 Parnassus Avenue, San Francisco, CA 94143-0446. Tel.: 415-476-5641; Fax: 415-476-0688; E-mail: alb{at}itsa.ucsf.edu

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