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KMID : 0364820150510040319
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Korean Journal of Microbiology
2015 Volume.51 No. 4 p.319 ~ p.328
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Defensive roles of Sdu1, a PPPDE superfamily member with ubiquitin C-terminal hydrolase activity, against thermal stress in Schizosaccharomyces pombe
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Han Hee
Heo Tae-Young
Ryu In-Wang
Kim Kyung-Hoon
Lim Chang-Jin
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Abstract
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The sdu1+ gene encodes Sdu1, a PPPDE superfamily member of deubiquitinating enzymes (DUBs) in Schizosaccharomyces pombe. Sdu1 was previously shown to contain an actual ubiquitin C-terminal hydrolase (UCH) activity using the recombinant plasmid pYSTP which harbors the sdu1+ gene. This work was designed to assess a thermotolerant role of Sdu1 against high incubation temperatures. In the temperature-shift experiments, the S. pombe cells harboring pYSTP grew much better after the shifts to 37˚C and 42˚C, when compared with the vector control cells. After being shifted to 37˚C and 42˚C for 6 h, the S. pombe cells harboring pYSTP contained lower reactive oxygen species (ROS) levels, compared with the vector control cells. The nitric oxide (NO) levels of the S. pombe cells harboring pYSTP were slightly lower than those of the vector control cells in the absence or presence of the temperature shifting. The total glutathione (GSH) levels of the S. pombe cells harboring pYSTP were significantly higher than those of the vector control cells. Total superoxide dismutase (SOD) and GSH peroxidase activities were also higher in the S. pombe cells harboring pYSTP after the temperature shifts than in the vector control cells. In brief, the S. pombe Sdu1 plays a thermotolerant role against high incubation temperature through the down-regulation of ROS and NO and the up-regulation of total GSH content, total SOD and GSH peroxidase activities.
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KEYWORD
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Schizosaccharomyces pombe, glutathione, reactive oxygen species, Sdu1, thermal stress
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