• 제목/요약/키워드: thiol-specific

검색결과 70건 처리시간 0.024초

Characterization of Mouse Peroxiredoxin III Genomic DNA and Its Expression

  • Lee, Tae-Hoon;Kim, Sun-Uk;Lee, Kyung-Kwang;Yu, Dae-Yeul
    • 한국동물번식학회:학술대회논문집
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    • 한국동물번식학회 2002년도 춘계학술발표대회 발표논문초록집
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    • pp.64-64
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    • 2002
  • Peroxiredoxins (Prxs) possess protective activity against oxygen radicals generated by thiol-catalyzed oxidative systems. We already reported the genomic structure and its expression of mouse Prx Ⅰ, Ⅱ, and 1-Cys Prx. However, the Prx Ⅲ has not been determined. That was initially defined transiently expressed gene, mouse MER5, of murine erythroleukaemia cell differentiation. In addition, this protein was recently redefined a member of the thiol-specific antioxidant gene family. (omitted)

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Redox-Dependent Modulation of RsrA, an Anti-Sigma Factor Regulating Thioredoxin Operons in Streptomyces coelicolor

  • Bae, Jae-Bum;Park, Joo-Hong;Roe, Jung-Hye
    • 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)

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가황(加黃)고무의 물리적(物理的) 성질(性質)에 미치는 가교구조(架橋構造)의 영향(影響) (The Effect of Crosslink Structures on the Physical Properties of Carbon Black Filled NR and SBR Vulcanizates)

  • 김상구
    • Elastomers and Composites
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    • 제23권4호
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    • pp.299-307
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    • 1988
  • The mono-, di- and polysulfidic concentrations of the carbon black filled NR and SBR vucanizates which have different cure systems were determined. The n-decane was used as a swelling solvent. The propane-2-thiol and hexane thiol were used as specific chemical probes to cleavage the chemical crosslinks such as di- and polysulfide. In order to understand the effect of crosslink structure on the physical properties of vulcanizates, the tensile properties, fatigue failure, heat build up, compression set and viscoelastic properties were measured. From the results, the significant relationships between crosslink sturctures and physical properties, especially a gins resistance were obtained. Therefore, the better performances of the product can be satisfied by using the interpretations and approaches in this study.

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설피리독신과 알파-만노시다제 간의 단백질 결합 특성에 관한 고찰 (Characterization of the Interaction of Sulfiredoxin (Srx1) with a Vacoular Protein $\alpha$-Mannosidase (Ams1) in Saccharomyces cerevisiae)

  • 바란독카랜;김일한
    • 자연과학논문집
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    • 제17권1호
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    • pp.13-29
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    • 2006
  • 산화-환원 활성 단백질중에 하나인 설피레독신과의 결합 단백질을 효모 Two-hybrid 기법을 이용하여 탐색한 결과, 알파-만노시다제가 설피레독신과 특이적으로 결합함을 밝혔다. 알파-만노시다제는 D-만노스 당을 비환원성 말단으로부터 유리시키는 가수분해 효소로서, 세포 원형질에 다량체 형태로 존재한다. 본 연구에서는 설피레독신과 알파-만노시다제간의 단백질결합을 설피레독신의 새로운 생리기능 관점에서 토의했다.

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Cysteine Participates in Cell Proliferation by Inhibiting Caspase3-like Death Protease

  • Lee, Sang-Han;Hong, Soon-Duck
    • Journal of Life Science
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    • 제9권1호
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    • pp.9-13
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    • 1999
  • Reduced thiols were important compounds for the maintenance of leukemia and lymphoma cell survival (and growth). In the course of examining the microenvirn-mental effects on lymphoma and leukemia cell growth, we found that cysteine suppressed apoptosis in these cells. In a present study, in order to investigate the role of cystein on the suppression of apoptotic cell death, we used CS21, P388, and L1210 cell lines. The addition of BSO, an inhibitor of glutathione synthase, induced apoptosis of these cells by blocking the cellular uptake of cysteine in CS21 cells. Although L1210 cells underwent apoptosis without thiol compounds, the addition of these compounds suppressed the apoptosis and promoted the growth or L1210 cells. When specific inhibitors of caspase3-like proteases, but not caspase1-like proteases, were activated during the L1210 cell apoptosis but the addition of thiol compounds suppressed the activation of caspase3-like proteases. These results suggest that reduced thiols including cysteine play an important role in the suppression of cell apoptosis by inhibiting the activation of caspase3-like proteases.

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Streptomyces griseus HH1, An A-factor Deficient Mutant Produces Diminished Level of Trypsin and Increased Level of Metalloproteases

  • Kim, Jung-Mee;Hong, Soon-Kwang
    • Journal of Microbiology
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    • 제38권3호
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    • pp.160-168
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    • 2000
  • A-factor I a microbial hormone that can positively control cell differentiation leading to spore formation and secondary metabolite formation in Streptomyces griseus. to identify a protease that is deeply involved in the morphological and physiological differentiation of Streptomyces, the proteases produced by Streptomyces griseus IFO 13350 and its A-factor deficient mutant strain, Streptomyces griseus HH1, as well as Streptomyces griseus HH1 transformed with the afsA gene were sturdied. In general Streptomyces griseus showed a higher degree of cell growth and protease activity in proportion to its ability to produce a higher amount of A-factor. In particular, the specific activity of the trypsin of Streptomyces griseus IFO 13350 was greatly enhanced more than twice compared with that of Streptomyces griseus HH1 in the later stage of growth. The specific activity of the metalloprotease of Streptomyces griseus HH1 was greatly enhanced more than twice compared with that of Streptomyces griseus IFO 13350, and this observation was reversed in the presence of thiostreptione, However, Streptomyces griseus HH1 transformed with the afsA gene showed a significantly decreased level of trypsin and metalloprotease activity compared with that of the HH1 strain. There was no significant difference between Streptomyces griseus IFO 13350 and HH1 strain in their chymotrypsin and thiol protease activity, yet the level of leu-amionpeptidase activity was 2 times higher in Streptomyces griseus HH1 than in strain IFO 13350 . Streptomyces griseus HH1 harboring afsA showed a similar level of enzyme activity , however, all the three protease activities sharply increased and the thiol protease activity was critically increased at the end of the fermentation. When a serine protease inhibitor, pefabloc SC, and metalloprotease inhibitor, EDTA, were applied to strain IFO 13350 to examine the in vivo effects of the protease inhibitors on the morpholofical differentiation, the formation of aerial meycelium and spores was delayed by two or three days.

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Identification of Proteins Affected by Iron in Saccharomyces cerevisiae Using Proteome Analysis

  • Lieu Hae-Youn;Song Hyung-Seok;Yang Seung-Nam;Kim Jae-Hwan;Kim Hyun-Joong;Park Young-Doo;Park Cheon-Seok;Kim Hae-Yeong
    • Journal of Microbiology and Biotechnology
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    • 제16권6호
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    • pp.946-951
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    • 2006
  • To study the effect of iron on Saccharomyces cerevisiae, whole-cell proteins of Saccharomyces cerevisiae were extracted and subjected to two-dimensional polyacrylamide gel electrophoresis (2D-PAGE), and differentially expressed proteins were identified. The proteins separated were further identified by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry and were compared with a protein database. Of more than 300 spots separated by molecular weight and isoelectric points, 27 differentially expressed spots were identified. Ten proteins were found to be differentially expressed at high iron concentration. Triosephosphate isomerase (TPI), YDR533C hypothetical protein, superoxide dismutase (SOD), 60 kDa heat-shock protein (HSP60), pyruvate dehydrogenase beta subunit 1 (PDB1), and old yellow enzyme 2 (OYE2) were upregulated, whereas thiol-specific antioxidant (TSA), regulatory particle non-ATPase subunit 8 (RPN8), thiol-specific peroxiredoxin 1 (AHP1), and fructose-1, 6-bisphosphate adolase (FBA) were downregulated by iron. Based on the result, we propose that SOD upregulated by iron would protect the yeast from oxidative stress by iron, and that TSA downregulated by iron would render cells hypersensitive to oxidative stress.

Yeast Prx의 스트레스의존 구조적 변화의 기작 (Mechanism of Stress-dependent Structural Change of Yeast Prx)

  • 강지선;정강원
    • Applied Microscopy
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    • 제35권4호
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    • pp.16-23
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    • 2005
  • 티올특이성 산화환원 단백질인 peroxiredoxin (thiolspecific peroxiredoxin, Prx) 은 거의 모든 생명체에 존재하며, reactive oxgen species (ROS)을 제거하는 역할을 수행한다. 전자현미경/image processing을 이용하여 세포의 방어기작에 중요한 기능을 수행하는 Prx의 구조를 분석하였다. Yeast-Prx는 크게 세 가지의 다른 형태 즉, 구 형태, ring 형태의 구조와 비 규칙적인 적은 입자로 구성되어 있음을 확인하였다. 또한 산화/환원 상태에서의 구조적 변화를 관찰하기위해 DTT와 $H_2O_2$를 처리 후 전자현미경을 관찰 하였다. 환원상태의(DTT 처리 후) yeast-Prx는 많은 decamer 구조를 보여주는 반면, 산화상태에서는 ($H_2O_2$ 처리 후) dimer나 구 형태의 구조를 보여 주고 있다. 또한 dimeric subunit간의 ionic interaction이 yeast-Prx의 oligomerization에 중요한 인자임을 확인하였다.