• BMB Reports
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• 제34권5호
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• pp.395-401
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• 2001

Schizosaccharomyces pombe gene encoding redox enzymes, such as thioltransferase (TTase) and thioredoxin (TRX), were previously cloned and induced by oxidative stress. In this investigation, their expressions were examined using $\beta$-galactosidase fusion plasmids. The expression of the two cloned genes appeared to be growth-dependent. The synthesis of $\beta$-galactosidase from the TTase-lacZ fusion was increased in the medium with the low glucose level, whereas it was significantly decreased in the medium without glucose or with galactose. It was also decreased in the nitrogen-limited medium. The synthesis of galactosidase from the TRX-lacZ fusion was unaffected by galactose or low glucose. However, it was lowered the absence of glucose. The synthesis of $\beta$-galactosidase from the TTase-lacZ fusion was shown to be enhanced in a higher medium pH. Our findings indicate that S. pombe TTase and TRX genes may be regulated by carbon and nitrogen sources, as well as medium pH.

• BMB Reports
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• 제33권6호
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• pp.514-518
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• 2000

Two open reading frames of Haemophilus influenzae, HI0572 and HI0751, showing homology to a yeast thioredoxin peroxidase II (TPx II) and an E. coli thiol peroxidase $P_{20}$, respectively, were cloned and expressed in E. coli, and then the proteins were subsequently purified and characterized. HI0751 protein showed the thioredoxin (Trx)-dependent peroxidase activity, whereas HI0572 protein showed glutathione-dependent peroxidase. The HI0572 is the first peroxiredoxin with glutathione peroxidase activity rather than thioredoxin peroxidase. Purified HI0572 and HI0751 proteins protected specifically the inactivation of glutamine synthetase by metal catalyzed oxidation (MCO) systems composed of $Fe^{3+}$, $O_2$ and mercaptans such as dithiothreitol, ${\beta}-mercaptoethanol$ and glutathione (GSH). Unlike the HI0751 protein, the HI0572 protein was more effective in protecting glutamine synthetase from inactivation by the $GSH/Fe^{3+}/O_2$ system. It seems that these unique properties of the HI0572 protein are due to the structure containing a glutaredoxin domain at it's C-terminal in addition to a peroxiredoxin domain.

• 한국자기공명학회논문지
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• 제8권1호
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• pp.1-18
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• 2004

A thioredoxin from hyperthermophile, Methanococcus jannashii (MjTRX) was characterized by use of the differential scanning calorimetry to understand the mechanisms of thermodynamic stability. MjTRX has an unfolding transition temperature of 116.5$^{\circ}C$, although the maximum free energy of the unfolding (9.9 Kcal/mol) is similar to that of E. coli thioredoxin (ETRX, 9.0 Kcal/mol). However, the temperature of maximum stability is higher than ETRX by 20$^{\circ}C$, indicating that the unfolding transition temperature increased by shifting the temperature of maximum stability. MjTRX has lower enthalpy and entropy of the unfolding compared to ETRX maintaining a similar free energy of the unfolding. From the structure and the thermodynamic parameters of MjTRX, we showed that the unfolding transition temperature of MjTRX is increased due to the decreased entropy of the unfolding. Decreasing the unfolded state entropy and increasing the folded state entropy can decrease the entropy of the unfolding. In the case of MjTRX, the increased number of proline residues decreased the unfolded state entropy and the increased enthalpy in the folded state increased the folded state entropy.

• Tuberculosis and Respiratory Diseases
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• 제62권3호
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• pp.197-202
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• 2007

흡연물질로서 benzopyrene, nicotine 및 cotinine등은 기관지상피세포인 Beas2B에서 CuZnSOD, thioredoxin, glutathione reductase 등의 발현량에 영향을 주며 특히 thioredoxin 및 glutathione reductase의 발현량을 노출 후 30분에서 4시간 경과 시간대에 증가시켰다가 24시간 이후에는 억제하는 특징을 나타내었다. 상기한 흡연물질에 의한 항산화효소의 조절기전에는 전사인자인 NNF-${\kappa}B$가 관여하는 것으로 추정되었다.

• Biotechnology and Bioprocess Engineering:BBE
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• 제8권2호
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• pp.89-93
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• 2003

human renin binding protein (hRnBp), showing N-acetylglucosamine-2-epimerase activity, was over-expressed in E. coli, but was mainly present as an inclusion body. To improve its solubility and activity, ubiquitin (Ub), thioredoxin (Trx), maltose binding protein (MBP) and NusA, were used as fusion partners. The comparative solubilities of the fusion proteins were, from most to least soluble: NusA, MBP, Trx, Ub. Only the MBP fusion did not significantly reduce the activity of hRnBp, but enhanced the stability. The Origami (DE3), permitting a more oxidative environment for the cytoplasm in E. coli; helped to increase its functional activity.

• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2003년도 International Symposium of Silkworm/Insect Biotechnology and Annual Meeting of Korea Society of Sericultural Science
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• pp.80-84
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• 2003

The thioredoxin peroxidase (TPx) is an antioxidant member of the peroxiredoxin family of enzymes. The TPx enzyme system has been implicated in the elimination of hydrogen peroxide and hydroxyl radicals generated during cellular processes. Such reactive molecules have been shown to cause damage to all major classes of biological macromolecules, including lipid, protein and DNA. Compared to mammalian peroxiredoxin genes, little is known about the insect TPx. (omitted)

• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2003년도 International Symposium of Silkworm/Insect Biotechnology and Annual Meeting of Korea Society of Sericultural Science
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• pp.130-133
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• 2003

Peroxiredoxins are a family of antioxidant proteins ubiquitously found in all living organisms. A type of peroxidase enzyme, named thioredoxin peroxidase (TPx), that reduces $H_2O$$_2$ with the use of electrons from thioredoxin and contains two essential cysteines was identified in a wide variety of organisms ranging from prokaryotes to mammals. TPx homologs, termed peroxiredoxin (Prx), have also been identified and include several proteins, designated 1-Cys Prx, that contain only one conserved cysteine. (omitted)

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2002년도 제9회 학술 발표회 프로그램과 논문초록
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• pp.54-54
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• 2002

$\sigma$$\^$R/ is a sigma factor responsible for inducing the thioredoxin system in response to oxidative stress in Streptomyces coelicolor. RsrA, an anti-sigma factor, specifically binds to $\sigma$$\^$R/ and inhibits $\sigma$$\^$R/-directed transcription under reducing conditions. Exposure to H$_2$O$_2$ or thiol-specific oxidant diamide dissociates $\sigma$$\^$R/-RsrA complex. The redox-dependent regulation of $\sigma$$\^$R/-RsrA binding has been reported to involve thiol-disulfide exchange in RsrA, which contains 7 cysteines in 105 amino acid residues.(omitted)

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2001년도 학술 발표회 진행표 및 논문초록
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• pp.63-63
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• 2001

SigR ($\sigma$$\^$R/) is a sigma factor responsible for inducing the thioredoxin system in response to oxidative stress in Streptomyces coelicolor. RsrA specifically binds to $\sigma$$\^$R/ and inhibits $\sigma$$\^$R/-directed transcription under reducing conditions. Exposure to H$_2$O$_2$ or thiol-specific oxidant diamide dissociates $\sigma$$\^$R/-RsrA complex. RsrA contains 7 cysteine residues in 105 total amino acid residues.(omitted)

• 한국잠사학회:학술대회논문집
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• 한국잠사학회 2005년도 제48회 춘계 학술연구 발표회
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• pp.19-19
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• 2005