• Title/Summary/Keyword: S. pombe

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Changes of Chemical Components during Seibel White Grape Must Fermentation by Different Yeast Strains (Seibel 백포도즙 발효중 화학성분의 변화)

  • Koh, Kyung-Hee;Chang, Woo-Young
    • Korean Journal of Food Science and Technology
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    • v.30 no.3
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    • pp.487-493
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    • 1998
  • This study was attempted to investigate the changes of chemical components by different yeast strains during alcohol fermentation at $12^{\circ}C$. Saccharomyces cerevisiae, Saccharomyces cerevisiae+Schizosaccharomyces pombe, and Schizosaccharomyces pombe were inoculated in the Seibel grape must, respectively. Sch. pombe began to metabolize malic acid after 4 days fermentation actively and utilized approximately 54% of initial malic acid. Ethanol contents of S. cerevisiae, S. cerevisiae+Sch.. pombe and Sch. pombe were 11.5%, 11.2%, and 10.0%, respectively. The fermentability of Sch. pombe was slower than that of S. cerevisiae. The production of sulfite showed a positive linear relationship with the yeast growth (P<0.01). Sensory scores indicated that the wine samples fermented by S. cerevisiae and Sch. pombe were not significantly different in color, odor, after taste and overall acceptability. Especially, the taste of Sch. pombe was significantly better than that of S. cerevisiae (P<0.05).

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Drug Target Identification of a natural anticancer agent plumbagin using $GPScreen^{TM}$: An innovative Technology for Drug Target Discovery using Drug-induced haploinsufficiency in S. pombe Genome-wide Heterozygous Deletion Mutant Library ($GPScreen^{TM}$ 이용한 천연 항암물질인 plumbagin의 약물 작용점 연구: 분열 효모인 S. pombe 유전체 이종 결손 변이 라이브러리에서의 약물에 의한 haploinsufficiency를 이용한 약물 작용점 규명을 위한 혁신 기술)

  • Lee, Ju-Hee;Yeon, Ji-Hyun;Yoon, Pyoung-Oh;Roh, Whi-Jae;Park, Han-Oh;Kim, Dong-Myung
    • 한국약용작물학회:학술대회논문집
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    • 2011.04a
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    • pp.106-107
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    • 2011
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Defensive roles of Sdu1, a PPPDE superfamily member with ubiquitin C-terminal hydrolase activity, against thermal stress in Schizosaccharomyces pombe (카르복시 말단 유비퀴틴 가수분해 효소 활성 보유 PPPDE superfamily member인 Schizosaccharomyces pombe Sdu1의 열 스트레스에 대한 방어적 역할)

  • Han, Hee;Heo, Tae Young;Ryu, In Wang;Kim, Kyunghoon;Lim, Chang-Jin
    • Korean Journal of Microbiology
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    • v.51 no.4
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    • pp.319-328
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    • 2015
  • 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 $37^{\circ}C$ and $42^{\circ}C$, when compared with the vector control cells. After being shifted to $37^{\circ}C$ and $42^{\circ}C$ 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.

Cloning and Sequencing Analysis of the Septin Gene in Schizosaccharomyces pombe (Schizosaccharomyces pombe의 septin 유전자의 클로닝과 염기서열분석)

  • Kim, Seong-chul;Kim, Hyoog Bai
    • Korean Journal of Microbiology
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    • v.33 no.4
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    • pp.232-236
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    • 1997
  • It is known that septin gene encodes the filament in Saccharomyces cerevisiae and it has importants roles in bud formation and cytokinesis. Four septin genes have been cloned in S. cerevisiae and it was found in Drosophila melanogaster and mouse. In this study, we cloned the septin gene in Schizosaccahromyces pombe by use of PCR technique. The septin gene in S. pombe has an 1,143 bp open reading frame and encodes a protein of 380 amino acids with a molecular weight of 42 kd. Comparison of the predicted amano acid sequences between the septin gene in S. pombe and CDC12 gene in S. cerevisiae reveals the 51.8% of simility.

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Catalase, Glutathione S-Transferase and Thioltransferase Respond Differently to Oxidative Stress in Schizosaccharomyces pombe

  • Cho, Young-Wook;Park, Eun-Hee;Lim, Chang-Jin
    • BMB Reports
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    • v.33 no.4
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    • pp.344-348
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    • 2000
  • The logarithmically growing Schizosaccharomyces pombe cells were subjected to high heat ($40^{\circ}C$), hydrogen peroxide, and heavy metals such as mercuric chloride and cadmium chloride. Then, the stress responses of catalase, glutathione S-transferase and thioltransferase were investigated. The high heat and cadmium chloride enhanced the catalase activity. The glutathione S-transferase activity of S. pombe cells was increased after treatments with heavy metals. The thioltransferase activity of S. pombe cells was completely abolished by mercuric chloride. Hydrogen peroxide caused no effect on the activities of glutathione S-transferase and thioltransferase. These results suggest that the response of S. pombe cells against oxidative stress is very complicated.

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A unique thioredoxin reductase plays defensive roles against oxidative, nitrosative and nutritional stresses in Schizosaccharomyces pombe (Schizosaccharomyces pombe의 유일한 치오레독신 환원효소의 산화적, 일산화질소 및 영양 스트레스에 대한 방어적 역할)

  • Ji, Dam-Jung;Lim, Chang-Jin;Kim, Kyunghoon
    • Korean Journal of Microbiology
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    • v.52 no.1
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    • pp.1-9
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    • 2016
  • A unique Schizosaccharomyces pombe $TrxR^+$ gene encoding thioredoxin reductase (TrxR) was found to be positively regulated by stress-inducing agents through the stress-responsive transcription factor Pap1. In the present study, the protective roles of S. pombe TrxR were evaluated using the TrxR-overexpressing recombinant plasmid pHSM10. In the presence of hydrogen peroxide ($H_2O_2$) and superoxide anion-generating menadione (MD), S. pombe TrxR increased cellular growth and the total glutathione (GSH) level, while it reduced levels of intracellular reactive oxygen species (ROS). The nitric oxide (NO) levels of the TrxR-overexpressing cells, in the presence of $H_2O_2$ and MD, were maintained to be similar to those of the corresponding non-treated cells. Although S. pombe TrxR was able to scavenge NO generated by sodium nitroprusside (SNP), it had no significant modulating effects on cellular growth, ROS levels, or the total GSH level of SNP-exposed yeast cells, compared with the differences in those of the two non-treated cell cultures. TrxR increased the cellular growth and total GSH level, which were diminished by nitrogen starvation. It also scavenged ROS and NO produced during nitrogen starvation. Taken together, the S. pombe TrxR protects against oxidative, nitrosative, and nutritional stresses.

Thermoresistant properties of bacterioferritin comigratory protein against high temperature stress in Schizosaccharomyces pombe (Schizosaccharomyces pombe에 존재하는 bacterioferritin comigratory protein의 고온 스트레스에 대한 열저항적 성질)

  • Ryu, In Wang;Lee, Su Hee;Lim, Hye-Won;Ahn, Kisup;Park, Kwanghark;Sa, Jae-Hoon;Jeong, Kyung Jin;Lim, Chang-Jin;Kim, Kyunghoon
    • Korean Journal of Microbiology
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    • v.52 no.4
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    • pp.398-405
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    • 2016
  • The Schizosaccharomyces pombe structural gene encoding bacterioferritin comigratory protein (BCP) was previously cloned using the shuttle vector pRS316 to generate the BCP-overexpressing plasmid pBCP10. The present work aimed to evaluate the thermoresistant properties of BCP against high temperature stress using the plasmid pBCP10. When the S. pombe cells were grown to the early exponential phase and shifted from $30^{\circ}C$ to $37^{\circ}C$ or $42^{\circ}C$, the S. pombe cells harboring pBCP10 grew significantly more at both $37^{\circ}C$ and $42^{\circ}C$ than the vector control cells. After 6 h of the shifting to higher incubation temperatures, they contained the lower reactive oxygen species (ROS) and nitrite content, an index of nitric oxide (NO), than the vector control cells. After the temperature shifts, total glutathione (GSH) content and total superoxide dismutase (SOD) activities were much higher in the S. pombe cells harboring pBCP10 than in the corresponding vector control cells. Taken together, the S. pombe BCP plays a thermoresistant role which might be based upon its ability both to down-regulate ROS and NO levels and to up-regulate antioxidant components, such as total GSH and SOD, and subsequently to maintain thermal stability.

Reactive oxygen species-dependent down-regulation of ubiquitin C-terminal hydrolase in Schizosaccharomyces pombe (Schizosaccharomyces pombe에서의 유비퀴틴 C-말단 가수분해효소의 활성산소종 의존성 하향조절)

  • Jo, Hannah;Lim, Hye-Won;Kwon, Hee-Souk;Lim, Chang-Jin;Park, Kwang Hark;Jin, Chang Duck;Kim, Kyunghoon
    • Korean Journal of Microbiology
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    • v.52 no.2
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    • pp.236-241
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    • 2016
  • The Schizosaccharomyces pombe $sdu1^+$ gene, belonging to the PPPDE superfamily of deubiquitinating enzyme (DUB) genes, was previously shown to encode a protein with ubiquitin C-terminal hydrolase (UCH) activity and to participate in the response against oxidative and nitrosative stresses. This work focused on the reactive oxygen species (ROS)-dependent regulation of the S. pombe $sdu1^+$ gene. UCH activities, encoded by the $sdu1^+$ gene, were attenuated in the S. pombe cells exposed to $H_2O_2$, superoxide radical-generating menadione (MD), and nitric oxide (NO)-generating sodium nitroprusside (SNP). Reduced glutathione (GSH) and its precursor N-acetylcysteine (NAC) were able to significantly enhance the UCH activities in the absence or presence of $H_2O_2$. However, the influences of both GSH and NAC on the ROS levels in the absence or presence of $H_2O_2$ were opposite to their effects on the UCH activities under the same conditions. The UCH activities in the Sdu1-overexpressing S. pombe cells were also diminished under exposure to $H_2O_2$, MD and SNP, but still remained to be higher than those in the vector control cells. In brief, it is proposed that the S. pombe $sdu1^+$ gene is regulated by ROS in a negative manner, the meaning of which largely remains elusive.

The Schizosaccharomyces pombe Proteins that Bind to the Human HnRNPA1 Winner RNA

  • Kim, Jeong-Kook
    • Journal of Microbiology
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    • v.35 no.4
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    • pp.327-333
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    • 1997
  • Although extensively characterized in human cells, no heterogeneous nuclear ribonucleoprotein(hnRNP) has been found in the fission yeast Schizosaccharomyces pombe which is amenable to genetic studies and more similar to mammals than Saccharomyces cerevisiae is in terms of RNA processing. As a first step to characterize hnRNPs from S. pombe, attempt was made to find human hnRNP A1 homologs from S. pombe. The RNA molecule (A1 winner) containing the consensus high-affinity hnRNP A1 binding site (UAGGGA/U) was synthesized in vitro and used in an ultraviolet(UV) light-induced protein-RNA cross-linking assay. A number of S, pombe proteins bound to the A1 winner RNA. An approximately 50-kDa protein(p50) cross-linked more efficiently to the A1 winner RNA than other proteins. The p50 protein did not cross-link to a nonspecific RNA, but rather to the A1-5’ SS RNA in which the consensus 5’ splice junction sites of S. pombe introns were abolished. This suggests that the p50 protein, however, did not bind to the single-stranded DNA to shich the human hnRNP A1 could bind and be eluted with 0.5M NaCl. Further analysis should reveal more features of this RNA-binding protein.

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Expression, Characterization and Regulation of a Saccharomyces cerevisiae Monothiol Glutaredoxin (Grx6) Gene in Schizosaccharomyces pombe

  • Lee, Jae-Hoon;Kim, Kyunghoon;Park, Eun-Hee;Ahn, Kisup;Lim, Chang-Jin
    • Molecules and Cells
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    • v.24 no.3
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    • pp.316-322
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    • 2007
  • Glutaredoxins (Grxs), also known as thioltransferases (TTases), are thiol oxidoreductases that regulate cellular redox state in a variety of organisms. In the budding yeast Saccharomyces cerevisiae, Grx1 and 2 are cytosolic dithiol Grxs, while Grx3, 4 and 5 are monothiol Grxs. A gene encoding a new monothiol Grx, Grx6, was cloned from the genomic DNA of S. cerevisiae by PCR. Its DNA sequence contains 1,080 bp, and encodes a putative protein of 203 amino acid residues containing Cys-Phe-Tyr-Ser at the active site. Grx6 is similar to other monothiol Grxs in the same organism and to Grx3 in the fission yeast Schizosaccharomyces pombe. and its predicted three-dimensional structure resembles that of S. pombe Grx3. S. pombe cells harboring plasmid pFGRX6 containing the Grx6 gene had about 1.3-fold elevated Grx activity in the exponential phase, and grew better than the control cells under some stressful conditions. Synthesis of ${\beta}$-galactosidase from a Grx6-lacZ fusion gene in S. pombe was enhanced by potassium chloride, aluminum chloride and heat ($37^{\circ}C$) treatment. S. pombe cells harboring plasmid pFGRX6 had elevated ROS levels whereas S. pombe cells harboring extra copies of Grx3 had reduced ROS levels.