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Regulation of thioltransferase activity from Schizosaccharomyces pombe

Authors
Cho, YWPark, EHLim, CJ
Issue Date
Sep-2000
Publisher
SPRINGER-VERLAG SINGAPORE PTE LTD
Keywords
fission yeast; glutaredoxin; Schizosaccharomyces pombe; temperature; thioltransferase
Citation
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.33, no.5, pp 422 - 425
Pages
4
Journal Title
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY
Volume
33
Number
5
Start Page
422
End Page
425
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16737
ISSN
1225-8687
Abstract
Thioltransferase (TTase), also known as glutaredoxin (Grx), is an enzyme catalyzing the reduction of a variety of disulfide compounds and acting as a cofactor for various enzymes such as ribonucleotide reductase. The Schizosaccharomyces pombe cells, exponentially grown in rich medium at 30 degrees C, were shifted to 20 degrees C and 35 degrees C. The yeast cells, shifted to 35 degrees C, showed higher TTase activity than the cells continuously grown at 30 degrees C, whereas the yeast cells, shifted to 20 degrees C, gave lower TTase activity. The S. pombe cells, exponentially grown in minimal medium and shifted from 30 degrees C to 35 degrees C and 40 degrees C, produced higher TTase activity. When the S. pombe cells were initially incubated in rich and minimal media at three different temperatures (25 degrees C, 30 degrees C and 35 degrees C), they showed higher TTase activity at higher temperature. These results suggest that the TTase activity of S. pombe is regulated by temperature.
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