Abstract
ABSTRACTSuperoxide dismutase (SOD) enzymes were explored in three Saccharomyces cerevisiae strains during batch-wise growth on standard YPD medium. Yeasts were grown till late exponential, early stationary phase when cells were highly enriched in peroxisomes and mitochondria. Furthermore, activity of SOD enzyme was measured in isolated mitochondrial and peroxisomal fractions after Nycodenz fractionation. The type of SOD enzyme localized in peroxisomes was investigated through in silico analysis. Sod1p and Sod2p amino acid sequences revealed that Mn SOD of S. cerevisiae possesses putative PTS1 signal (GKI), which could successively targeted the protein into yeasts peroxisomes. Results indicated that in peroxisomes of Saccharomyces cerevisiae exist in situ mechanism for scavenging of ROS, which probably comprises a cooperative action of Mn SOD and catalase.
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