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J. Biol. Chem., Vol. 279, Issue 32, 33791-33798, August 6, 2004

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A Proteomic Study of SUMO-2 Target Proteins^*

Alfred C. O. Vertegaal, Stephen C. Ogg¶||, Ellis Jaffray**, Manuel S. Rodriguez**, Ronald T. Hay**, Jens S. Andersen¶, Matthias Mann, and Angus I. Lamond, Wellcome Trust Principal Research Fellow

From the Wellcome Trust Biocentre, University of Dundee, Dundee DD1 5EH, United Kingdom, the ^**Centre for Biomolecular Sciences, University of St. Andrews, North Haugh, St. Andrews KY16 9ST, United Kingdom, and the Center for Experimental BioInformatics, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark

The SUMO family in vertebrates includes at least three distinct proteins (SUMO-1, -2, and -3) that are added as post-translational modifications to target proteins. A considerable number of SUMO-1 target proteins have been identified, but little is known about SUMO-2. A stable HeLa cell line expressing His₆-tagged SUMO-2 was established and used to label and purify novel endogenous SUMO-2 target proteins. Tagged forms of SUMO-2 were functional and localized predominantly in the nucleus. His₆-tagged SUMO-2 conjugates were affinity-purified from nuclear fractions and identified by mass spectrometry. Eight novel potential SUMO-2 target proteins were identified by at least two peptides. Three of these proteins, SART1, heterogeneous nuclear ribonucleoprotein (RNP) M, and the U5 small nuclear RNP 200-kDa helicase, play a role in RNA metabolism. SART1 and heterogeneous nuclear RNP M were both shown to be genuine SUMO targets, confirming the validity of the approach.

Received for publication, April 15, 2004 , and in revised form, June 1, 2004.

^* This work was supported in part by a Danish National Research Foundation grant (to the Centre for Experimental BioInformatics) and by the Medical Research Council, the Biotechnology and Biological Sciences Research Council, and the Wellcome Trust (to the Wellcome Trust Biocentre and Centre for Biomolecular Sciences). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Table A.

Dutch Cancer Society Fellow. Present address: Dept. of Molecular Cell Biology, Leiden University Medical Centre, 2333 AL Leiden, The Netherlands.

^¶ Both authors contributed equally to this work.

^|| Supported by the Wellcome Trust.

To whom correspondence should be addressed: Wellcome Trust Biocentre, MSI/WTB Complex, University of Dundee, Dundee DD1 5EH, Scotland, UK. Tel.: 44-1382-345-473; Fax: 44-1382-345-695; E-mail: a.i.lamond{at}dundee.ac.uk.

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