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Molecular & Cellular Proteomics 7:132-144, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

In Vivo Identification of Human Small Ubiquitin-like Modifier Polymerization Sites by High Accuracy Mass Spectrometry and an in Vitro to in Vivo Strategy^*,S

Ivan Matic^,, Martijn van Hagen^,¶, Joost Schimmel^¶, Boris Macek, Stephen C. Ogg^||, Michael H. Tatham^**, Ronald T. Hay^**, Angus I. Lamond^**,, Matthias Mann^, and Alfred C. O. Vertegaal^¶,¶¶

From the Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany, ^¶ Department of Molecular Cell Biology, Leiden University Medical Center, 2300 RC Leiden, the Netherlands, ^|| Centre for Molecular Medicine, 61 Biopolis Drive (Proteos), Singapore 138673, Singapore, and ^** Wellcome Trust Biocentre, University of Dundee, Dundee DD1 5EH, United Kingdom

The length and precise linkage of polyubiquitin chains is important for their biological activity. Although other ubiquitin-like proteins have the potential to form polymeric chains their identification in vivo is challenging and their functional role is unclear. Vertebrates express three small ubiquitin-like modifiers, SUMO-1, SUMO-2, and SUMO-3. Mature SUMO-2 and SUMO-3 are nearly identical and contain an internal consensus site for sumoylation that is missing in SUMO-1. Combining state-of-the-art mass spectrometry with an "in vitro to in vivo" strategy for post-translational modifications, we provide direct evidence that SUMO-1, SUMO-2, and SUMO-3 form mixed chains in cells via the internal consensus sites for sumoylation in SUMO-2 and SUMO-3. In vitro, the chain length of SUMO polymers could be influenced by changing the relative amounts of SUMO-1 and SUMO-2. The developed methodology is generic and can be adapted for the identification of other sumoylation sites in complex samples.

^¶¶ To whom correspondence may be addressed. Tel.: 31-71-526-9621; Fax: 31-7-526-8270; E-mail: vertegaal{at}lumc.nl

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