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Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses.

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.

Pubmed ID: 15166219


  • Zhou W
  • Ryan JJ
  • Zhou H


The Journal of biological chemistry

Publication Data

July 30, 2004

Associated Grants

  • Agency: NHGRI NIH HHS, Id: K22 HG002604
  • Agency: NHGRI NIH HHS, Id: K22 HG002604-02

Mesh Terms

  • Blotting, Western
  • Cell Division
  • DNA
  • Electrophoresis, Polyacrylamide Gel
  • Ethanol
  • Genotype
  • Histone Acetyltransferases
  • Hydrogen Peroxide
  • Mass Spectrometry
  • Oxidative Stress
  • Oxygen
  • Peptide Elongation Factors
  • Peptides
  • Plasmids
  • Protein Biosynthesis
  • Proteins
  • SUMO-1 Protein
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Silver Staining
  • Transcription, Genetic