• 제목/요약/키워드: Y-protein

검색결과 31,661건 처리시간 0.065초

Arabidopsis nucleoside diphosphate kinase-2 as a plant GTPase activating protein

  • Shen, Yu;Han, Yun-Jeong;Kim, Jeong-Il;Song, Pill-Soon
    • BMB Reports
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    • 제41권9호
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    • pp.645-650
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    • 2008
  • Nucleoside diphosphate kinase (NDPK) is involved in multiple signaling pathways in mammalian systems, including G-protein signaling. Arabidopsis NDPK2, like its mammalian counterparts, is multifunctional despite its initial discovery phytochrome-interacting protein. This similarity raises the possibility that NDPK2 may play a role in G-protein signaling in plants. In the present study, we explore the potential relationship between NDPK2 and the small G proteins, Pra2 and Pra3, as well as the heterotrimeric G protein, GPA1. We report a physical interaction between NDPK2 and these small G proteins, and demonstrate that NDPK2 can stimulate their GTPase activities. Our results suggest that NDPK2 acts as a GTPase-activating protein for small G proteins in plants. We propose that NDPK2 might be a missing link between the phytochrome-mediated light signaling and G protein-mediated signaling.

RAS inhibitor를 이용한 항암제의 개발에 관하여

  • 어미숙
    • 미생물과산업
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    • 제19권4호
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    • pp.32-35
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    • 1993
  • ras는 활성화 형태인 GTP bound form과 비활성화 형태인 GDP bound form의 두 형태로 존재하며 두 형태를 매개하는 regulatory protein들에 의해 그 activity가 조절된다. 또한 ras는 GTP와 GDP에 강한 친화성이 있으며 세포내에는 GTP보다 GDP가 더 많이 있어서 평소에는 ras가 GDP와 결합하고 있다가 활성화될때만 GTP와 결합하는 것으로 추정된다. GDP bound ras는 guanine nucloetide exchange protein(GEP)에 의해 활성화된 GTP bound form으로 전환되며 ras의 기능이 발휘된 후에는 GTPase activating protein(GAP)에 의해 비활성화된다. Yeast의 경우 IRA1과 2의 product가 GAP의 역할을 하는 것으로 알려져 있고 CDC25 gene의 product가 GEP의 기능을 담당하는 것으로 알려져 있다. NF1 gene은 Von Recklinghausen Neurofibromatosis Type I 질병을 가진 환자에게서 발견되었는데 부분적으로 sequencing한 결과에 따르면 yeast의 IRA1/2, mammalian GAP gene product와 protein homology가 높은 것으로 나타났다. Yeast의 경우 IRA1/2 gene의 손실이나 mammalian ras gene의 transformation으로 인한 heat shock sensitivity가 NF1 gene(2,3) 혹은 GAP(4)의 expression으로 suppression된 것으로 보아 NF1이 GAP protein으로서 ras를 불활성화 시킨다는 것이 판명되었다. 결론적으로 ras의 활성은 GTP bound 혹은 GDP bound의 양쪽형태를 이동하면서 조절되는데 이 기능은 GAP과 GEP 또는 그의 유사 protein들에 의해 수행되며 이러한 regulatory protein들은 growth factor, cytokine 그리고 protein kinase 같은 signal에 의해 활성화된다고 생각된다. 본 총설에서는 ras protein의 여러가지 성질보다는 ras의 modification과 관련하여 항암제로 사용할 수 있는 ras에 specific한 약품개발의 가능성과 현재 알려진 ras의 inhibitor를 중심으로 논하고자 한다.

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Purification and Cloning of o Protein Secreted from Lactobacillus acidophilus

  • 한서영;이영선;임정빈;황덕수
    • Animal cells and systems
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    • 제2권3호
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    • pp.355-359
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    • 1998
  • Among the proteins secreted from Lactobacillus acidophilus KCTC 3151, a 36 kDA and 24 kDa protein, whose amounts were relatively abundant, were purified and their N-terminal amino acid sequences determined. The N-terminal amino acid sequence of 36 kDa protein exhibited high homology with thymidine phosphorylase and glyceraldehyde-3-phosphate dehydrogenase. The N-terminal amino acid sequence of the 24 kDa protein did not show significant homology with proteins in Protein Data Base nor Gene Bank. Nucleotide sequence of the gene encoding 36 kDa protein indicates that the protein possesses the domains for a-helical, phosphate binding and pyrimidine binding sites, which are also shown in thymidine phosphorylases. Also, the protein contains conserved domains of dehydrogenase II and III. However, the activity of thymidine phosphorylase or glyceraldehyde-3-puospnate dehydrogenase could not be detected in the purified fractions of the 36 kDa protein.

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Functional Analysis of the Tomato Spotted Wilt Virus(TSWV) NSm Protein by Using Immunoblotting and Immunogold Labelling Assay

  • Choi, Tae-Jin
    • Journal of Microbiology and Biotechnology
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    • 제6권6호
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    • pp.468-473
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    • 1996
  • The genome of tomato spotted wilt virus (TSWV) is composed of three RNA segments, S, M, and L RNA and the 5.0 kb M RNA encodes two glycoproteins Gl, G2 and NSm protein of unknown function. In an effort to investigate the function of the NSm protein, antibody was raised against NSm fusion protein overexpressed in Escherichia coli. This antibody was used to detect the NSm protein by using western blot analysis and electron microscopic observation after immunogold labelling. For the cloning of the NSm gene, total RNA extracted from a TSWV infected plant was used for cDNA synthesis and polymerase chain reaction (PCR) instead of going through time-consuming virus purification. A protein band specifically reacting to the NSm antibody was detected from TSWV inoculated plants. The NSm protein was detected in the cell wall fraction and in pellet from low speed centrifugation when the infected plant tissue was fractionated into 4 fractions. In the immuno-electron microscopic observation, gold particles were found around the plasmodesmata of infected plant tissue. These results suggest that the NSm protein of TSWV plays some role in cell-to-cell movement of this virus.

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쌀단백질의 L-lysin.HCI 강화에 관한 연구 (Effeet of L-lysin.HCI Fortification on the Quality of Rice Protein)

  • 이숙희
    • 한국식품영양과학회지
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    • 제8권1호
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    • pp.21-24
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    • 1979
  • 쌀단백질(蛋白質)의 아미노 강화효과와 과잉강화에 의한 쌀단백질(蛋白質)의 아미노산(酸) 불균형 현상(現像)을 살펴보기 위하여 시판(市販) 백미(白米)에 $0.25{\sim}1.0%$ 수준으로 L-lysin HCI를 강화하여 동물(動物) 사육실험(飼育實驗)을 행(行)한 결과(結果) 다음과 같은 결과(結果)를 얻었다. 1. 강화력이 0.25%일 때 체중증가량(增加量) 및 PER이 가장 높았다. 2. $0.5%{\sim}1.0%$ 수준에선 첨가하지 않은 대조군보다 PER이 높았으나 0.25% 보다는 낮았다. 3. 강화수준 1.0%까지는 아미노산(酸) 불균형으로 인한 강화 역효과는 나타나지 않았다.

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돼지 간장 조직에서 얻은 단백질 메칠라제 저해제의 정제와 특성 (Protein Methylase Inhibitor from Porcine Liver : Purification and Properties)

  • 박선미;박연호;백운기;이향우
    • 약학회지
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    • 제37권2호
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    • pp.149-157
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    • 1993
  • Protein methylase inhibitor which is a modulator of biological methylation has been purified and characterized from porcine liver soluble fraction by cell fractionation, Sephadex G25 chromatography, reverse phase HPLC, size exclusion HPLC. The results are summarized as follows. 1) The purified inhibitor shows apparent homogeneity, as judged by HPLC. 2) A molecular weight of the purified inhibitor which is composed of 18 amino acid residues is about 1,400 daltons. 3) A single absorption peak of ultraviolet spectrum was observed at 260nm. 4) The inhibitor was not inactivated by heating at $100^{\circ}C$ until 60min. and its activity was not influenced by treatment with digestive enzymes, such as trypsin, pepsin, pronase, chymotrypin, lysozyme, DNase, and RNase. 5) The purified inhibitor inhibited protein rnethylase I, II, III and phospholipid methyltransferase activities. 6) The purified inhibitor inhibited noncompetitively protein methylase II from porcine liver, spleen, and testis. 7) The $K_{i}$ values for protein methylase II from porcine liver, spleen, and testis were 300nM, 250nM, 297nM, respectively.

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Changes in ruminal fermentation and blood metabolism in steers fed low protein TMR with protein fraction-enriched feeds

  • Choi, Chang Weon
    • 농업과학연구
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    • 제43권3호
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    • pp.379-386
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    • 2016
  • Four ruminally cannulated Holstein steers (BW $482.9{\pm}8.10kg$), fed low protein TMR (CP 11.7%) as a basal diet, were used to investigate changes in rumen fermentation and blood metabolism according to protein fraction, cornell net carbohydrates and protein system (CNCPS), and enriched feeds. The steers, arranged in a $4{\times}4$ Latin square design, consumed TMR only (control), TMR supplemented with rapeseed meal (AB1), soybean meal (B2), and perilla meal (B3C), respectively. The protein feeds were substituted for 23.0% of CP in TMR. Ruminal pH, ammonia-N, and volatile fatty acids (VFA) in rumen digesta, sampled through ruminal cannula at 1 h-interval after the morning feeding, were analyzed. For plasma metabolites analysis, blood was sampled via the jugular vein after the rumen digesta sampling. Different N fraction-enriched protein feeds did not affect (p > 0.05) mean ruminal pH except AB1 being numerically lower 1 - 3 h post-feeding than the other groups. Mean ammonia-N was statistically (p < 0.05) higher for AB1 than for the other groups, but VFA did not differ among the groups. Blood urea nitrogen was statistically (p < 0.05) higher for B2 than for the other groups, which was rather unclear due to relatively low ruminal ammonia-N. This indicates that additional studies on relationships between dietary N fractions and ruminant metabolism according to different levels of CP in a basal diet should be required.

Identification and Purification of a Normal Rat Liver Plasma Membrane Surface Protein which Disappears after Chemical Carcinogenesis

  • Kim, Min-Young;Lee, Myung-Kyu;Hahm, Kyung-Soo
    • BMB Reports
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    • 제28권6호
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    • pp.504-508
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    • 1995
  • The electrophoretic patterns of plasma membrane surface proteins of normal rat liver cells and rat hepatomas were compared in 10% non-denaturing and 7-15% gradient non-denaturing gel. Chemical carcinogens, 2-Me DAB (2-methyl-4-dimethylaminoazobenzene) and DENA (diethylnitrosamine), were used to induce hepatoma in rats. One protein which disappeared in hepatoma was identified in normal rat liver by non-denaturing gel electrophoresis. Rabbit antisera were raised against this specific protein, and the protein was purified by Sephacryl S-200 column and immunoaffinity chromatography using the purified antibody. The purified protein showed two bands of molecular weights approximately 50 $kD_{\alpha}$ and 52 $kD_{\alpha}$ by SDS-polyacrylamide gel electrophoresis, which reacted specifically with the antibody. However only one band was observed in non-denaturing gel and also in isoelectric focusing with a pI value of 6.6. This study showed the existence of an unique protein on the plasma membrane surface of normal rat liver cells which disappeared in rat hepatomas induced by chemical carcinogens.

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Localization of F plasmid SopB protein and Gene silencing via protein-mediated subcellular localization of DNA

  • Kim Sook-Kyung;James C. Wang
    • 한국미생물학회:학술대회논문집
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    • 한국미생물학회 2000년도 추계학술발표대회
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    • pp.15-23
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    • 2000
  • The subcellular localization of the SopB protein, which is encoded by the Escherichia coli F plasmid and is involved in the partition of the single-copy plasmid, was directly visualized through the expression of the protein fused to the jellyfish green fluorescent protein (GFP). The fusion protein was found to localize to positions close but not at the poles of exponentially growing cells. Examination of derivatives of the fusion protein lacking various regions of SopB suggests that the signal for the cellular localization of SopB resides in a region close to its N terminus. Overexpression of SopB led to silencing of genes linked to, but well-separated from, a cluster of SopB-binding sites termed sopC. In this SopB-mediated repression of sopC-linked genes, all but the N-terminal 82 amino acids of SopB can be replaced by the DNA-binding domain of a sequence-specific DNA -binding protein, provided that the sopC locus is also replaced by the recognition sequence of the DNA-binding domain. These results suggest a mechanism of gene silencing: patches of closely packed DNA-binding protein is localized to specific cellular sites; such a patch can capture a DNA carrying the recognition site of the DNA -binding domain and sequestrate genes adjacent to the recognition site through nonspecific binding of DNA.

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프로테아제와 리파제의 혼합에 따른 세척성의 변화 (Effects of Mixing Protease and Lipase on Detergency)

  • 서수진;박정희
    • 한국의류학회지
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    • 제24권2호
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    • pp.205-213
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    • 2000
  • This study investigated the effect of mixing protease and lipase on detergency. The detergency of protein soiled, oil soiled and protein-oil soiled cloths and the relative hydrolytic activity of enzymes were examined. The protease-lipase added detergent solution was most effective for the removal of protein in protein-oil soiled cloths. This is because the lipase removed the protein that was physically bound to oil as well as the protease removed the protein. The protease added detergent solution was second effective, the lipase added detergent solution was third effective, and the detergent solution without protease and lipase was the least effective. The protease-lipase added detergent solution was also most effective in the oil removal from protein-oil soiled cloths. Unlike in protein removal, however, the protease added detergent solution was more effective in oil removal than the lipase added detergent solution. This is because the removal of oil bound to protein by protease was more effective than the removal of oil by lipase. In soiling-washing cycles, however, the effects of lipase increased, and as a result, the detergency of protease added detergent solution and the lipase added detergent solution became similar.

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