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 per...

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Bibliographic Details
Published in:The Journal of biological chemistry 2004-07, Vol.279 (31), p.32262-32268
Main Authors: Zhou, Weidong, Ryan, Jennifer J, Zhou, Huilin
Format: Article
Language:English
Subjects:
Blotting, Western
Cell Division
DNA - chemistry
Electrophoresis, Polyacrylamide Gel
Ethanol - pharmacology
Genotype
Histone Acetyltransferases
Hydrogen Peroxide - pharmacology
Mass Spectrometry - methods
Oxidative Stress
Oxygen - metabolism
Peptide Elongation Factors - metabolism
Peptides - chemistry
Plasmids - metabolism
Protein Biosynthesis
Proteins - chemistry
Proteins - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Silver Staining
SUMO-1 Protein - metabolism
Transcription, Genetic
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M404173200