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Originally published In Press as doi:10.1074/jbc.M409203200 on August 23, 2004

J. Biol. Chem., Vol. 279, Issue 44, 45662-45668, October 29, 2004
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Global Analysis of Protein Sumoylation in Saccharomyces cerevisiae*{boxs}

James A. Wohlschlegel{ddagger}§, Erica S. Johnson¶, Steven I. Reed§, and John R. Yates, III{ddagger}||

From the {ddagger}Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, the Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson, University, Philadelphia, Pennsylvania 19107, and the §Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037

Although the modification of cellular factors by SUMO is an essential process in Saccharomyces cerevisiae, the identities of the substrates remain largely unknown. Using a mass spectrometry-based approach, we have identified 271 new SUMO targets. These substrates play roles in a diverse set of biological processes and greatly expand the scope of SUMO regulation in eukaryotic cells. Transcription appears to be the most prevalent process associated with sumoylation with novel SUMO substrates found in basal transcription machinery for RNA polymerases I, II, and III, pol II transcriptional elongation complexes, and a variety of chromatin remodeling, chromatin modifying, and chromatin silencing complexes. Additionally, our global analysis has revealed a number of interesting biological patterns in the list of SUMO targets including a clustering of sumoylation targets within macromolecular complexes.

Received for publication, August 11, 2004

* This work was supported by an American Cancer Society Postdoctoral Fellowship (to J. A. W.) and National Institutes of Health Grants RR11823-08 (to J. R. Y.), ES012021-02 (to J. R. Y.), CA85487 (to S. I. R.), and GM62268-04 (to E. S. J.). 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.

{boxs} The on-line version of this article (available at http://www.jbc.org) contains supplemental material.

|| To whom correspondence should be addressed: Dept. of Cell Biology, Mail Drop: SR11, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-784-8862; Fax: 858-784-8883, jyates{at}scripps.edu.


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