• Journal of Life Science
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• v.24 no.1
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• pp.14-19
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• 2014

Kinesin-1 consists of two heavy chains (KHCs), also called KIF5s, and two light chains (KLCs) that form a heterotetrameric complex. Here, we demonstrate the binding of a neuronal KHC, KIF5A, to the carboxyl (C)-terminal tail region of Fig4 (also known as Sac3), a phosphatase that removes the 5-phosphate from phosphatidylinositol-3,5-bisphosphate ($PtdIns(3,5)P_2$). Fig4 bound to the C-terminal region of KIF5A but not to other KHCs (KIF5B and KIF5C) and KLC1 in yeast two-hybrid assays. The interaction was further confirmed in a glutathione S-transferase pull-down assay and by co-immunoprecipitation. Anti-KIF5A antibody co-immunoprecipitated Fig4 with KIF5A from mouse brain extracts. These results suggest that kinesin-1 could transport the Fig4-associated protein complex or cargo in cells.

• Korean Journal of Plant Tissue Culture
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• v.28 no.5
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• pp.283-287
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• 2001

Differential display based on PCR was employed to identify genes expressed during tuber-developing stage of potato (Solanum tuberosum L. cv. Irish Cobbler). An eukaryotic initiation factor 5A (eIF-5A) clone isolated from a cDNA library constructed with developing micro-tuber using a probe of PCR fragment. We isolated three positive clones and ore of them contained open reading frame. This clone revealed high sequence similarity to tomato eIF 5A cDNA. At the DNA level, there is 94.8% identity with the tomato eIF-5A4, whereas at the protein level there is a high identity with 97.5%. The potato eIF 5A clone is 716 bp in length and contains a single open reading frame from 57 to 539 bp, a 56 bp 5'-untranslated region and a 177 bp 3'-untranslated region. The deduced protein composed of 160 amino acid residues, with a predicted molecular mass of 17.4 kD and an estimated pl of 5.5. The sequence of 12 (STSKTGKHGHAK) amino acids among eIF-5A proteins is perfectly conserved from yeast to human. That sequence in potato eIF-5A protein is also conserved at position 46 to 57 amino acid. This region embeds the post-translational modification site of the lysine residue (at the seventh K) to hypusine that is crucial to eIF-5A activity. The northern blot analysis of eIF5A has shown abundant expression, mainly in flower organs (stamen, ovary, petal, sepal), fruit and stolen.

• Korean Journal of Environmental Biology
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• v.21 no.3
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• pp.276-285
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• 2003

To control pythium root rot, Bacillus lentimorbus WJ5a17 with high anti-fungal activity against Pythium ultimum was induced from B. lentimorbus WJ5 by gamma radiation ($^{60}Co$). The biocontrollers of FWJ5 and FWJ5a17 were formulated ($1.0\times 10^{11}$) with B. lentimorbus WJ5 and WJ5a17, respectively, The population density of FWJ5 and FWJ5a17 maintained highly up to $1.0\times 10^{9}$ CFU $g^{-1}$ in nursery and field soils until 30 days after treatment. P. ultimum spores germination were inhibited 71.0% and 81.4% by FWJ5 and FWJ5a17, respectively. Pythium root rot of yea pepper, Chinese cabbage and radish were significantly (p < 0.05) controled by one time treatment of FWJ5 and FWJ5a17.

• Molecules and Cells
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• v.27 no.1
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• pp.99-103
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• 2009

Ribose-5-phosphate isomerase A (RpiA) plays an important role in interconverting between ribose-5-phosphate (R5P) and ribulose-5-phosphate in the pentose phosphate pathway and the Calvin cycle. We have determined the crystal structures of the open form RpiA from Vibrio vulnificus YJ106 (VvRpiA) in complex with the R5P and the closed form with arabinose-5-phosphate (A5P) in parallel with the apo VvRpiA at $2.0{\AA}$ resolution. VvRpiA is highly similar to Escherichia coli RpiA, and the VvRpiA-R5P complex strongly resembles the E. coli RpiA-A5P complex. Interestingly, unlike the E. coli RpiA-A5P complex, the position of A5P in the VvRpiA-A5P complex reveals a different position than the R5P binding mode. VvRpiA-A5P has a sugar ring inside the binding pocket and a phosphate group outside the binding pocket: By contrast, the sugar ring of A5P interacts with the Asp4, Lys7, Ser30, Asp118, and Lys121 residues; the phosphate group of A5P interacts with two water molecules, W51 and W82.

• Bulletin of the Korean Chemical Society
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• v.35 no.5
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• pp.1337-1342
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• 2014

A novel and convenient route for the synthesis of a series of thalidomide derivatives is described. Compound 2 was cyclized with different amines under alkaline condition to obtain 4-nitro substituted phthalimidines 3a-d. Hydroxylactams 4a-d were produced via bromination and hydroxylation. Different acyl chlorides were reacted with hydroxylactams to provide the desired esters 5a-d. All compounds were evaluated by MTT assay for their inhibitory activities against HCT-116, MG-63, MCF-7, HUVEC and HMVEC cell lines in vitro. Most of them showed no obvious cytotoxic effect on normal human cells, compounds 4a-d, $5a_2$, $5a_4$, $5a_5$, $5b_2$, $5c_2$ and $5d_2$ exhibited potent antitumor activities, among which compounds $5a_2$ and $5b_2$ were more effective than 5-FU.

• Journal of the Korean Chemical Society
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• v.45 no.4
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• pp.325-333
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• 2001

The 4-substituted tetrazolo[1,5-a]quinoxalines were synthesized from 4-chlorotetrazolo-[1,5-a]quinoxaline(8) or 4-hydrazinotetrazolo[1,5-a]quinoxaline(9). Refluxing of the tetrazolo[1,5-a]quinoxaline(12) in N,N-dimethylformamide gave the 1,2,4-triazolo[3,4-c]tetrazolo[1,5-a]quinoxaline(13), which was also obtained by the reaction of compound 9 with ethyl chloroformate in N,N-dimethylformamide. The reaction of compound 9 with isothiocyanates in ethanol provided the tetrazolo[1,5-a]quinoxalines(14), whose reaction with dimethyl acetylenedicarboxylate afforded the tetrazolo[1,5-a]quinoxalines(15). The tetrazolo [1,5-a]quinoxalines(18) were obtained by the reaction of compound 9 with alkyl (ethoxymethylene)cyanoacetates. Some of the compounds showed antibacterial, antifungal or algicidal activities against some strains.

• Korean Journal of Materials Research
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• v.2 no.5
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• pp.353-359
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• 1992

Thermal oxidation and plasma enhanced chemical vapor deposition of tantalum oxide thin films on p-type (100) Si substrates were studied to examine the dielectric nature of T$a_2O_5$ as a Al/T$a_2O_5$/p-Si capacitor. Microstructure and dielectric properties of the capacitors were investigated by XRD, AES, high frequency C-V analyzer, I-V meter and TEM. XRD analysis showed that the structure of T$a_2O_5$ films were amorphous, but the films were crystallized to hexagonal $\delta$-T$a_2O_5$ by 65$0^{\circ}C$ thermal oxidation treatment. It was found that the stoichiometry of the films was more or less close to 2 : 5. Leakage current density and relative dielectric constant of thermal oxidation T$a_2O_5$ film at 60$0^{\circ}C$ was 5.0${ imes}10^{-6}$/A/c$m^2 and 31.5, respectively. In the case of PECVD T$a_2O_5$film deposited at 0.47W/c$m^2 they were 2.5${ imes}10^{-5}$/A/$ extrm{cm}^2$ and 24.0, respectively. The morphology of the films and interfaces were investigated by TEM.

• YAKHAK HOEJI
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• v.47 no.5
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• pp.293-299
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• 2003

Structure-activity relationship studies of allylamine type of antimycotics were carried out to evaluate the effect of naphthyl and methyl portion of naftifine. Compounds with 4-fluorophenyl(2a-5a), 2-fluorophenyl(2b-5b), 2,4-dichlorophenyl(2c-5c), 2,6-dichlorophenyl(2d-5d), 4-nitrophenyl(2e-5e), and 2,3-dihydro-benzo[1,4]dioxan-6-yl( 2f-5f) instead of naphthyl group with hydrogen(3a-3f), methyl(4a-4f), and ethyl(5a-5f) in the place of methyl in naftifine were synthesized and tested their in vitro anti-fungal activity against five different fungi. Eight compounds(3a, 5a, 3c, 4c, 4d, 5d, 5e, and 4f) showed significant antifungal activity against T. mentagrophytes. (E)-N-Ethyl-(3-phenyl-2-propenyl)-4-nitro-benzenemethaneamine(5e) displayed moderate antifungal activity against all five different fungi.

• Bulletin of the Korean Chemical Society
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• v.10 no.5
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• pp.426-430
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• 1989

Two crystal structures of iodine sorption complexes of dehydrated partially Co(Ⅱ )-exchanged zeolite A, $Co_{3.5}Na_5-A{\cdot}xI_2$, x = 2.5 and 5.0, have been determined by single crystal X-ray diffraction techniques. Both structures were solved and refined in cubic space group, Pm3m at $21(1)^{\circ}C$. The structures of $Co_{3.5}Na_5-A{\cdot}2.5I_2$(a = 12.173(1) ${\AA}$) and $Co_{3.5}Na_5-A{\cdot}5.0I_2$(a = 12.130(1) ${\AA}$) were refined to the final error indices, $R_1$ = 0.081 and $R_2$ = 0.077 with 261 reflections and $R_1$ = 0.103 and $R_2$ = 0.112 with 225 reflections, respectively, for which I>3${\sigma}$(I). In both structures, 3.5 $Co^{2+}$ ions and 4.5 $Na^+$ ions per unit cell lie at two crystallographically different 6-ring positions. 0.5 $Na^+$ ion lines in an 8-oxygen ring plane. Dehydrated $Co_{3.5}Na_5$-A sorbs 2.5 iodine molecules per unit cell at $70^{\circ}C$ (vapor pressure of $I_2$ is ca. 8.3 torr) within 30 minutes and 5 iodine molecules per unit cell at $80^{\circ}C$ (vapor pressure of $I_2$ is ca. 14.3 torr) within 24 hours. Each iodine molecule makes a close approach, along its axis to framework oxygen atom with I-I-O = $175^{\circ}$.

• Journal of Life Science
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• v.20 no.8
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• pp.1166-1172
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• 2010

Kinesin-I exists as a tetramer of two heavy chains (KHCs, also called KIF5s), which contain the amino (N)-terminal motor domain and carboxyl (C)-terminal domain, as well as two light chains (KLCs), which bind to the KIF5s (KIF5A, KIF5B and KIF5C) stalk region. To identify the interaction proteins for KIF5A, yeast two-hybrid screening was performed and a specific interaction with the ${\beta}$ subunit of heterotrimeric G proteins ($G{\beta}$) was found. $G{\beta}$ bound to the amino acid residues between 808 and 935 of KIF5A and to other KIF5 members in the yeast two-hybrid assay. The WD40 repeat motif of $G{\beta}$ was essential for interaction with KIF5A. In addition, these proteins showed specific interactions in the glutathione S-transferase (GST) pull-down assay. An antibody to KIF5s specifically co-immunoprecipitated KIF5s associated with heterotrimeric G proteins from mouse brain extracts. These results suggest that kinesin-I motor protein transports heteroterimeric G protein attachment vesicles along microtubules in the cell.