• Development and Reproduction
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• v.23 no.3
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• pp.285-295
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• 2019

Junction-mediating and regulatory protein (JMY) is a regulator of both transcription and actin filament assembly. The actin-regulatory activity of JMY is based on a cluster of three actin-binding Wiskott-Aldrich syndrome protein homology 2 (WH2) domains that nucleate actin filaments directly and promote nucleation of the Arp2/3 complex. In addition to these activities, we examined the activity of JMY generation in early embryo of mice carrying mutations in the JMY gene by CRISPR/Cas9 mediated genome engineering. We demonstrated that JMY protein shuttled expression between the cytoplasm and the nucleus. Knockout of exon 2, CA (central domain and Arp2/3-binding acidic domain) and NLS-2 (nuclear localization signal domain) on the JMY gene by CRISPR/Cas9 system was effective and markedly impeded embryonic development. Additionally, it impaired transcription and zygotic genome activation (ZGA)-related genes. These results suggest that JMY acts as a transcription factor, which is essential for the early embryonic development in mice.

• Journal of Korean Port Research
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• v.9 no.2
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• pp.25-38
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• 1995

The wind generated circulation model describes the phenomenon based on the following physical assumptions: a) As the horizontal dimension of the flow domain is several orders of magnitude larger than vertical dimension, nearly horizontal flow is realistic. b) The time taken for circulation to develop may effect on the flow domain of the earth's rotation, the contribution of the Coriolis force. c) A flow domain of large dimension results in quite large Reynolds number and the Reynolds stresses are approximated by the turbulent mean velocity gradient. d) The circulation is forced by the shear stresses on the water surface exercised by the wind. Modification made to the depth average approximation of the convective terms and the bed shear stress terms by adopting a certain distribution of current over the depth and laboratory measurements for the bed shear expression. Modification circulation patterns, energy evolution and surface profile gave the significant differences comparing with the classical model results. The modified model results in higher free surface gradients balancing both the free surface shear and the bed shear and consequently to higher surface profiles along the coast.

• Biodesign
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• v.5 no.3
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• pp.122-125
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• 2017

Receptor for advanced glycation end products (RAGE) is one of the single transmembrane domain containing receptors and causes various inflammatory diseases including diabetes and atherosclerosis. RAGE extracellular domain has three consecutive IgG-like domains (V-C₁-C₂ domain) which interact with various soluble ligands including heparan sulfate or HMGB1. Studies have shown that each ligand induces different oligomeric forms of RAGE which results in a ligand-specific signal transduction. The structure of mouse RAGE bound to heparan sulfate has been previously determined but the electron density map of heparan sulfate was too ambiguous that the exact position of heparin sulfate could not be defined. Furthermore, the complex structure of human RAGE and heparin sulfate still remains elusive. Therefore, to determine the structure, human RAGE was overexpressed using bacterial expression system and crystallized using the sitting drop method in the condition of 0.1 M sodium acetate trihydrate pH 4.6, 8 % (w/v) polyethylene glycol 4,000 at 290 K. The crystal diffracted to 3.6 Å resolution and the space group is C121 with unit cell parameters a= 206.04 Å, b= 68.64 Å, c= 98.73 Å, α= 90.00°, β= 90.62°, γ= 90.00°.

• Proceedings of the KIPE Conference
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• 2001.10a
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• pp.169-173
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• 2001

In this paper, dc link ripple currents for three-phase ac/dc/ac PWM converters are ana lysed in a frequency domain. The expression of the harmonic currents is developed by using switching functions and exponential Fourier series expansion. The dc link ripple currents with regard to power factor and modulation index are investigated. In addition, the effect of the displacement angle between the switching periods of line-side converters and load-side inverters on the dc link ripple current is studied. The result of the dc link current analysis is helpful in specifying the dc link capacitor size and its lifetime estimation.

• International Journal of Oral Biology
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• v.31 no.3
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• pp.81-86
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• 2006

SET (Suppressor of variegation, Enhancer of zeste, and the Trithorax) domain-containing proteins are known to have methyltransferase activity at lysine residues of histone proteins. In this study, we identified a novel SET domain-containing protein from mouse and named Kodo7. Indeed, Kodo7 has methyltransferase activity at K9 residue of the H3 protein as demonstrated by a histone methyl-transferse activity assay using GST-tagged Kodo7. Confocal microscopy showed that Kodo7 is co-localized with histones in the nucleus. Interestingly, ectopic expression of Kodo7 by transient transfection induced cell death and treatment of the transfectants with a caspase-3 inhibitor, Ac-DEVD-AFC decreased Kodo7-induced apoptosis. These results suggest that Kodo7 induces apoptotic cell death through increased methylation of histones leading to transcriptional repression.

• Journal of Mechanical Science and Technology
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• v.16 no.10
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• pp.1320-1326
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• 2002

In a one-dimensional heat conduction domain with heated and insulated walls, an integral approach is proposed to estimate time-dependent boundary heat flux without internal measurements. It is assumed that the expression of the heat flux is not known a priori. Hence, the present inverse heat conduction problem is classified as a function estimation problem. The spatial temperature distribution is approximated as a third-order polynomial of position, whose four coefficients are determined from the heat fluxes and the temperatures at both ends at each measurement. After integrating the heat conduction equation over spatial and time domain, respectively, a simple and non-iterative recursive equation to estimate the time-dependent boundary heat flux is derived. Several examples are introduced to show the effectiveness of the present approach.

• IMMUNE NETWORK
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• v.5 no.3
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• pp.144-149
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• 2005

Background: Fc receptor-mediated phagocytosis is a complex process involving the activation of kinases and phosphatases. FcgammaRIIB has been known to transduces inhibitory signals through an immunoreceptor tyrosine-based inhibitory motif (ITIM) in cytoplasmic domains. In this study, we examined the involvement of inositol-phosphatase in the Fc receptor-mediated phagocytosis. Methods: J774 cells were infected using vaccinia viral vector containing SH2 domain-containing inositol-phosphatase (SHIP) cDNA and stimulated with the sensitized sheep red blood cells. Results: Stimulation of J774 cells induced the tyrosine phosphorylation of SHIP which was maximal at 5 minutes. Phosphatidylinositol-3 (PI-3) kinase inhibitor (wortmannin) inhibits J774 cell phagocytosis of sensitized sheep red blood cells in a dose-dependent manner. Heterologious expression of SHIP in J774 cells inhibits phagocytosis of sensitized sheep red blood cells in a dose-dependency manner, but catalytically dead mutants of SHIP has no effect on phagocytosis. Conclusion: These results strongly suggest that the active signals mediated by PI-3 kinase are opposed by inhibitory signals through SHIP in the regulation of Fc receptor-mediated phagocytosis.

• Journal of Industrial Technology
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• v.29 no.B
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• pp.115-119
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• 2009

Green fluorescent protein (GFPuv) was displayed on the surface of ethanol-producing bacteria Zymomonas mobilis using N-terminal domain of ice nucleation protein (INP) as an anchoring motif. To evaluate the ice nucleation protein as plausible anchor motif in Z. mobilis, GFPuv gene was subcloned into Zymomonas expression vector yielding pBBR1MCS-3/pPDC/INPN/GFPuv plasmid., INP-GFPuv fusion protein was expressed in Z. mobilis and its fluorescence was verified by confocal microscopy. The successful display of GFPuv on Zymomonas mobilis suggest that INP anchor motif could be used for future fusion partner in Z. mobilis strain improvement.

• BMB Reports
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• v.43 no.6
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• pp.407-412
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• 2010

Homeodomain (HD) is a highly conserved DNA-binding domain composed of helix-turn-helix motif. Drosophila Vnd (Ventral nervous system defective) containing HD acts as a regulator to either enhance or suppress gene expression upon binding to its target sequence. In this study, kinetic analysis of Vnd binding to DNA was performed. The result demonstrates that DNA-binding affinity of the recombinant protein containing HD and NK2-specific domain (NK2-SD) was higher than that of the full-length Vnd. To access whether phosphorylation sites within HD and NK2-SD affect the interaction of the protein with the target sequence, alanine substitutions were introduced. The result shows that S631A mutation within NK2-SD does not contribute significantly to the DNA-binding affinity. However, S571A and T600A mutations within HD showed lower affinity for DNA binding. In addition, DNA-binding analysis using embryonic nuclear protein also demonstrates that Vnd interacts with other nuclear proteins, suggesting the existence of Vnd as a complex.

• Proceedings of the Microbiological Society of Korea Conference
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• 2002.10a
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• pp.135-139
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• 2002

Yeast cells respond to condition of amino acid starvation by synthesizing GCN4, a typical eukaryotic transcriptional activator, which regulates the expression of many amino acids biosynthetic genes. By introducing point mutations in the DNA binding domain of GCN4, mutants with normal DNA binding activity but defective in transcriptional activity were isolated to identify unknown proteins that could suppress the mutant phenotype under an amino acid depletion condition. As a result, SSB(Stress-Seventy B) subfamily proteins were identified as suppressors of mutant GCN4. SSB proteins were known as a member of yeast hsp70 family that probably aids passage of nascent chain through ribosomes. Among them, the mechanism of suppression by SSB2 on the defective GCN4 mutant strains is under investigation. Gcn4p directly interacts with Ssb2p through the basic DNA binding domain of GCN4. It suggests the possibility that physical interaction might induce the transcriptional activation of Gcn4p.