• 한국식물학회:학술대회논문집
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• 한국식물학회 1996년도 제10회 식물생명공학심포지움 고등식물 발생생물학의 최근 진보
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• pp.40-47
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• 1996

The promoters of a variety of plant genes are characterized by the presence of TGACG motif-containing sequences. These genes often exhibit quite diverse expression characteristics and in many case the TGACG-motif has been demonstrated to be essential for expression. Here we report the isolation and characterization of a soybean cDNA that encodes a novel basic/leucine zipper (bZIP) protein, STF1, that specifically interacts with Hex (TGACGTGG) and CRE (TGACGTCA) sequences. This protein contains a bZIP motif at C-teminus and an acidic domain at N-terminus. DNA binding specificities, heterodimer formation, and expression characteristics of STF1 were compared with a soybean TGA1 protein, STGA1. The soybean STF1 interacts with TGACG-sequences containing an ACGT core, while STGA1 requires TGACG as a sufficient binding sequence. The flanking sequences to the TGACG motif affected DNA binding of STF1 siginificantly. The STF1 mRNA is found mainly in dark grown soybean seedling with higher expression in apical and elongating hypocotyl, while STGA1 mRNA is highly abundant in roots of light grown plants. Furthermore, we demonstrate that STF1 heterodimerzes with G-box binding factorss (GBFs) which was not observed with TGA1. The fact that STF1 possesses both distinct DNA binding speficities and heterodimerization properties suggest that STF1 belongs to a new family of plant bZIP proteins which recognize the Hex/CRE motif.

• Journal of Photoscience
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• 제7권1호
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• pp.31-34
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• 2000

The heterotrichous ciliate Stentor coeruieus shows a step-up photophobic response to visible light In the previous paper, the existence of GTP-binding proteins was confirmed by using the antisera against the carboxy terminal decapeptide of transducin $\alpha$ subunit. The photoreceptor, stentorin, is localized in the pigment granule. If the immunoreactive G-protein directly interacts with the photoreceptor stentorin, the G-protein expected to be located in the pigment granule rather than plasma membrane. To elucidate the function of the immunoreactive G-protein, the localization of the G-protein in Stentor coeruleus was studied. The results suggest that this G-protein is located in the myoneme involved in the contraction and extension of the cell rather than in the pigment granule.

• Bulletin of the Korean Chemical Society
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• 제33권3호
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• pp.971-974
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• 2012

The facilitated diffusion effect on protein-DNA binding is studied. A rigorous theoretical approach is presented to deal with the coupling between one-dimensional and three-dimensional diffusive motions. For a simplified model, the present approach can provide numerically exact results, which are confirmed by the lattice-based Monte Carlo simulations.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2001년도 학술 발표회 진행표 및 논문초록
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• pp.43-43
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• 2001

In cells of the eukaryotic microorganism Dictyostelium discoideum, at least eight small, four-EF hand calcium-binding proteins respectively are expressed at specific stages during development. One of these proteins, calcium-binding protein 3 (CBP3), first appears just prior to cell aggregation and then maintains relatively constant levels throughout development.(omitted)

• Plant Biotechnology Reports
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• 제3권4호
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• pp.293-299
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• 2009

Auxin-binding protein 57 ($ABP_{57}$), a soluble auxin-binding protein, acts as a receptor to activate plasma membrane (PM) $H^+-ATPase$. Here, we report the cloning of abp57 and the biochemical characterization of its protein expressed in E. coli. The analysis of internal amino acid sequences of $ABP_{57}$ purified from rice shoots enabled us to search for the corresponding gene in protein DB of NCBI. Further BLAST analysis showed that rice has four abp57-like genes and maize has at least one homolog. Interestingly, Arabidopsis seems to have no homolog. Recombinant $ABP_{57}$ expressed in E. coli caused the activation of PM $H^+-ATPase$ regardless of the existence of IAA. Scatchard analysis showed that the recombinant protein has relatively low affinity to IAA as compared to natural $ABP_{57}$. These results collectively support the notion that the cloned gene is responsible for $ABP_{57}$.

• Archives of Pharmacal Research
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• 제22권2호
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• pp.130-136
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• 1999

Mouse guanylate-binding protein 3 (mGBP3) is a 71-kDa GTPase which belongs to GTP-binding protein family. The present study showed that the expression of mGBP3 transcript was readily induced in a dose dependent fashion in the macrophage cell line RAW264.7 treated with either $interferon-{\gamma} (IFN-\gamma)$ or lipopolysaccaride (LPS). The expression of mGBP3 protein was also apparent by 4 and 6 h after the treatment of cells with IFN-\gamma (100 U/ml) or LPS ($1{\mu}g/ml$) , and remained at palteau for at least 24 h. Cycloheximide ($10{\mu}g/ml$) had no effect on the $IFN-\gamma-$ or LPS-induced mGBP3 expression, suggesting that the mGBP3 induction did not require further protein synthesis. Interestingly, a protein kinase C (PKC) inhibitor staurosporine (50 nM) abolished the induction of mGBP3 expression by LPS, but not by $IFN-{\gamma}$. These findings suggest that mGBP3 may be involved in the macrophage activation process and both IFN-\gamma and LS induce the mGBP3 expression through distinct signal transduction pathways.

• 대한수의학회지
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• 제37권4호
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• pp.875-882
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• 1997

To produce the recombinant fibronectin-binding protein(FnBP) for development of subunit vaccine against Staphylococcus aureus. The fnbp gene was amplified from the chromosomal DNA of S aureus KNU 196 strain using the polymerase chain reaction, and cloned into pGEX-4T-2. Then, the recombinant FnBP fused with glutathione-S-transferase was produced in E coli, purified by affinity chromatography, and identified its antigenicity and immunogenicity by Western blot. The recombinant FnBP produced in this study is considered to have the same property of native FnBP purified from S aureus, and is expected to be useful as a candidate for S aureus subunit vaccine.

• BMB Reports
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• 제33권2호
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• pp.188-192
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• 2000

Recombinant protein G has been utilized in the purification of antibodies from various mammalian species based on the interaction of antibodies with protein G. The interaction between immunoglobulin and protein G may not be restricted to the Fc protion of antibodies, as many different $F(ab)_2$ or Fab fragments can also bind to protein G. I found both FAb $F(ab)_2$ of 145-2C11, a hamster anti-mouse $CD3{\varepsilon}$ antibody, bound to the protein G-sepharose. Interestingly, Fab and $F(ab)_2$ of 145-2C11 did not bind to the protein A-sepharose. The binding of Fab and $F(ab)_2$ of 145-2C11 to protein G provided a useful method to remove proteases, chopped fragments of the Fc region, and other contaminating proteins. The remaining intact antibody in the protease reaction mixture can be removed by using a protein A-sepharose, because the Fab and $F(ab)_2$ portions of 145-2C11 did not bind to protein A-sepharose. The specific binding of Fab and $F(ab)_2$ portions of 145-sC11 to a protein G-sepharose (though not to a protein A-sepharose) and binding of intact 145-2C11 to both protein A- and G-sepharose will be useful in developing an effective purification protocol for Fab and $F(ab)_2$ portions of 145-2C11.

• Reproductive and Developmental Biology
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• 제30권1호
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• pp.13-19
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• 2006

생물학적 자극통제 수단으로 활용하기 위한 돼지 웅성 페르몬성 분자를 탐색하고자 일련의 냄새 분자로서 2-(cyclo-hexyloxy) tetrahydrofurane 유도체들의 정량적인 구조와 수용체인 porcine odorant binding protein (pOBP)간의 결합 친화력 상수$(p(Od)_{50})$에 대한 비교 분자장 분석(CoMFA)을 실행하였다. 가장 양호한 CoMFA 모델 AIV $(r^2_{cv}.(q^2)=0.886$ 및 $r^2_{ncv}.=0.984$)은 기질 분자 내 입체 중심(chiral center)의 절대 배열이 $C_1(R),C_2(S)$인 분자를 atom based fit 방법으로 배열하였을 경우의 standard field와 indicator field가 조합된 CoMFA장의 조건에서 유도되었다. 이 CoMFA 모델은 입체장 40.8% 정전기장 14.6%및 소수성장 44.6%가 결합 친화력 상수에 영향을 미치는 요소임을 나타내었다. 등고도의 분석 결과로부터 효과적인 결합 친화력 냄새 분자를 수식하는 데 몇 가지 가치 있는 정보를 얻을 수 있었다.

• 한국자기공명학회논문지
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• 제20권4호
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• pp.138-142
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• 2016

Replication Protein A (RPA) is the eukaryotic single-stranded DNA binding protein. It involves in DNA replication, repair, and damage response. Among three subunits, RPA70 has a protein-protein binding domain (RPA70N) at the N-terminal. It has known that the domain recruits several damage response proteins to the damaged site. Also, it is suggested that there are more candidates that interact with RPA70N. Even though several studies performed on the structural aspects of RPA70N and its ligand binding, the backbone assignments of RPA70N is not available in public. In this study, we present the backbone assignments of RPA70N.