MCP Agilent Technologies
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/mcp.M300140-MCP200 on January 29, 2004.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
M300140-MCP200v1
3/5/429    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Glossary
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Medzihradszky, K. F.
Right arrow Articles by Burlingame, A. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Medzihradszky, K. F.
Right arrow Articles by Burlingame, A. L.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

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

Research

O-Sulfonation of Serine and Threonine

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

K. F. Medzihradszkya, Z. Darulaa,b, E. Perlsonc, M. Fainzilberc, R. J. Chalkleya, H. Balld,e, D. Greenbaumf, M. Bogyof,g, D. R. Tysonh, R. A. Bradshawh and A. L. Burlingamea,i

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.

b Current address: Proteomics Research Group, Biological Research Center of the Hungarian Academy of Sciences, H-6726, Szeged, Temesvari krt. 62, Hungary

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


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M.-A. Frese, S. Schulz, and T. Dierks
Arylsulfatase G, a Novel Lysosomal Sulfatase
J. Biol. Chem., April 25, 2008; 283(17): 11388 - 11395.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
L. E. Ball, M. N. Berkaw, and M. G. Buse
Identification of the Major Site of O-Linked {beta}-N-Acetylglucosamine Modification in the C Terminus of Insulin Receptor Substrate-1
Mol. Cell. Proteomics, February 1, 2006; 5(2): 313 - 323.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
F. Chu, D. A. Nusinow, R. J. Chalkley, K. Plath, B. Panning, and A. L. Burlingame
Mapping Post-translational Modifications of the Histone Variant MacroH2A1 Using Tandem Mass Spectrometry
Mol. Cell. Proteomics, January 1, 2006; 5(1): 194 - 203.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Zhang, P. V. Baranov, J. F. Atkins, and V. N. Gladyshev
Pyrrolysine and Selenocysteine Use Dissimilar Decoding Strategies
J. Biol. Chem., May 27, 2005; 280(21): 20740 - 20751.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
K. M. Loyet, J. T. Stults, and D. Arnott
Mass Spectrometric Contributions to the Practice of Phosphorylation Site Mapping through 2003: A Literature Review
Mol. Cell. Proteomics, March 1, 2005; 4(3): 235 - 245.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
B. A. Ballif, J. Villen, S. A. Beausoleil, D. Schwartz, and S. P. Gygi
Phosphoproteomic Analysis of the Developing Mouse Brain
Mol. Cell. Proteomics, November 1, 2004; 3(11): 1093 - 1101.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Wells, L. K. Kreppel, F. I. Comer, B. E. Wadzinski, and G. W. Hart
O-GlcNAc Transferase Is in a Functional Complex with Protein Phosphatase 1 Catalytic Subunits
J. Biol. Chem., September 10, 2004; 279(37): 38466 - 38470.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
E. Perlson, K. F. Medzihradszky, Z. Darula, D. W. Munno, N. I. Syed, A. L. Burlingame, and M. Fainzilber
Differential Proteomics Reveals Multiple Components in Retrogradely Transported Axoplasm After Nerve Injury
Mol. Cell. Proteomics, May 1, 2004; 3(5): 510 - 520.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.