Identification of Saccharomyces Cerevisiae YPR1 as a Methylglyoxal Reducing Enzyme: Over-expression Enhances Oxidative Stress Tolerance in E. Coli
Methylglyoxal, generated from the triosephosphates of glycolysis, is a toxic electrophile that can modify proteins and nucleic acids and cause oxidative stress in cells, consequently causes dysfunction of cells and tissues. Its levels increase in many pathological conditions in humans and, in plants, when under environmental stress. Aiming to look for new enzymes to detoxify methylglyoxal and utilize these enzymes to protect plants against environmental stress, we identified Saccharomyces cerevisiae YPR1 as a methylglyoxal reducing enzyme. By four steps of partial purification, we located a few protein candidates on a SDS-PAGE gel. The genes encoding these proteins were identified by mass spectrometry MALDI-TOF. By excluding those genes with known functions, the most possible gene YPR1 was selected to express in E. coli. Protein crude extract of YPR1 expressing E. coli had about 120-fold increase in methylglyoxal reducing activity compared to the control strain. Tolerance of the YPR1 expressing E. coli against oxidative stress was improved. The results demonstrate that yeast YPR1 has the potential to enhance environmental stress tolerance of plants and other organisms.
M. Firestone et al., "Identification of Saccharomyces Cerevisiae YPR1 as a Methylglyoxal Reducing Enzyme: Over-expression Enhances Oxidative Stress Tolerance in E. Coli," Journal of Genetics and Molecular Biology, Official Publication of the Chinese Society of Genetics, Jan 2007.
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