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J. Biol. Chem., Vol. 279, Issue 31, 32262-32268, July 30, 2004

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Global Analyses of Sumoylated Proteins in Saccharomyces cerevisiae

INDUCTION OF PROTEIN SUMOYLATION BY CELLULAR STRESSES^*

Weidong Zhou, Jennifer J. Ryan, and Huilin Zhou¶

From the Ludwig Institute for Cancer Research and the Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093

We have undertaken a global analysis of sumoylated proteins in Saccharomyces cerevisiae by tandem mass spectrometry. Exposure of cells to oxidative and ethanol stresses caused large increases in protein sumoylation. A large number of new sumoylated proteins were identified in untreated, hydrogen peroxide-treated, and ethanol-treated cells. These proteins are known to be involved in diverse cellular processes, including gene transcription, protein translation, DNA replication, chromosome segregation, metabolic processes, and stress responses. Additionally, the known enzymes, including E1, E2, and E3 of the sumoylation cascade were found to be auto-sumoylated. Taken together, these results show that protein sumoylation is broadly involved in many cellular functions and this mass spectrometry-based proteomic approach is useful in studying the regulation of protein sumoylation in the cells.

Received for publication, April 14, 2004 , and in revised form, May 20, 2004.

^* This work was supported in part by the Ludwig Institute for Cancer Research. 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.

^¶ Supported by a Faculty Transitional Award from the National Human Genome Research Institute. To whom correspondence should be addressed: Ludwig Institute for Cancer Research, University of California at San Diego, 9500 Gilman Dr., CMM-East, Rm. 3050, La Jolla, CA 92093-0660. Tel.: 858-534-7808; Fax: 858-534-7750; E-mail: huzhou{at}ucsd.edu.

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