• Journal of Life Science
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• v.17 no.12
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• pp.1610-1615
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• 2007

Genus Sorbus is a long lived woody species that is primarily distributed throughout Asia and Europe. This species is regarded as very important herbal medicines in Korea and China. Sorbus commixta is primarily distributed throughout Europe. We evaluated a representative sample of the four taxa with nuclear ribosomal DNA internal transcribed spacer sequences (ITS) to estimate genetic relationships within genus. Aligned nucleotide sequences of the length of ITS1 were nearly constant within genus Sorbus varying from 219 in S. aucuparia to 218 in the rest species. Especially, the 5.8S subunit of all taxa of Sorbus was found to constant of 165 bp nucleotides. However, aligned nucleotide sequences of the length of ITS2 vary from 240 in S. sambucifolia var. pseudogrcilisto 245 in S. aucuparia. Total alignment length is 629 positions, of which 35 are parsimony-informative, 32 variable but parsimony-uninformative, and 552 constant characters. The base furtherance showed the difference to the by a total taxon: an average A and T are 17.7% and G and C are 30.4%, 34.2%, respectively. All the four taxa beginning with conserved base paired triplets emerging from single strand regions (domain I). Noteworthy, in the RNA secondary structure proposed for the three Korean Sorbus taxa RNA transcript ITS2, which shows a remarkedly well-conserved folding (domain II). When compared to the European Sorbus (S. aucuparia) of ITS2. ITS analysis may be useful in germ-plasm classification several taxa of genus Sorbus.

• Journal of Life Science
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• v.17 no.3 s.83
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• pp.318-327
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• 2007

This study presents the molecular phylogenetic analysis of Korean Aurelia aurita Linnaeus collected from Yeosu in the southern waters of Korea using nuclear ITS1 region and mitochondrial COI gene sequences. The use of oligonucleotide primers F5 (forward) and R5 (reverse) targeted to ITS1 and LCO1490 (forward) and HCO2198 (reverse) targeted to COI amplified 267 bp and 643 bp fragments, respectively. The shortest genetic distance towards the ITS1 region is estimated at 0.023 when comparing Korean A. aurita to Aurelia sp. collected from California, USA. In particular, Korean and American/Swedish A. aurita were located far away in terms of genetic distance, ranging from 0.393 to 0.395. On the other hand, the genetic distance between Korean and English/Turkish/Swedish/American A. aurita regarding the mitochondrial DNA COI gene ranged from 0.201 to 0.205. However, a sister-ship with Korean and American A. aurita showed an extremely high bootstrap value (100%). The predicted secondary RNA structure of the mitochondrial DNA COI gene showed many different folding structures with a similar energy between Korean and American A. aurita. These results suggest that ITS1 and the mitochondrial DNA COI gene could be used as genetic markers for identification of the biogeographic populations.

• Journal of Life Science
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• v.33 no.10
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• pp.828-834
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• 2023

The cDNA that encodes transmembrane protein 258 (Tmem258) was cloned from Gryllus bimaculatus and named GbTmem258. This protein comprises 80 amino acids, has no N-glycosylation site, and contains five potential phosphorylation sites at two serines, two threonines, and one tyrosine. The predicted molecular mass of GbTmem258 is 9.06 kDa, and its theoretical isoelectric point is 5.5. The tertiary structure of GbTmem258 was predicted using the available secondary structure information, which suggests the presence of alpha helices (52.5%), random coils (22.5%), extended strands (16.25%), and beta turns (8.75%). Homology analysis revealed that GbTmem258 exhibits high similarity at the amino-acid level to Tmem258 found in other species. The effect of starvation and refeeding on GbTmem258 mRNA expression was also examined in this study. It was found that GbTmem258 mRNA expression in the hindgut progressively increased throughout the starvation period, peaking at almost 1.5 times the control level after six days of starvation. However, refeeding for one to two days after the six-day starvation period restored GbTmem258 mRNA expression to the control level. In fat body, GbTmem258 mRNA expression was almost 3-fold higher during starvation compared to the control level. Refeeding for one to two days after the six-day fast resulted in a decline in the expression to about a 2.5-fold increase over the control level. Throughout the starving and refeeding periods, no other tissues showed any discernible alterations in GbTmem258 mRNA expression.

• Proceedings of the Korean Society of Plant Pathology Conference
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• 2003.10a
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• pp.81.2-82
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• 2003

Plants have evolved along with pathogens, and they have developed sophisticated defense systems against specific microorganisms to survive. G-protons are considered one of the upstream signaling components working as a key for the defense signal transduction pathway. For activation and inactivation of G-protein, GTP-biding proteins are involved. GTP -binding proteins are found in all organisms. Small GTP-binding proteins, having masses of 21 to 30kD, belong to a superfamily, often named the Ras supefamily because the founding members are encoded by human Ras genes initially discovered as cellular homologs of the viral ras oncogene. Members of this supefamily share several common structural features, including several guanine nucleotide binding domains and an effector binding domain. However, exhibiting a remarkable diversity in both structure and function. They are important molecular switches that cycle between the GDP-bound inactive form into the GTP-bound active form through GDP/GTP replacement. In addition, most GTP-binding proteins cycle between membrane-bound and cytosolic forms. such as the RAC family are cytosolic signal transduction proteins that often are involved in processing of extracellular stimuli. Plant RAC proteins are implicated in regulation of plant cell architecture secondary wall formation, meristem signaling, and defense against pathogens. But their molecular mechanisms and functions are not well known. We isolated a RacB homolog from rice to study its role of defense against pathogens. We introduced the constitutively active and the dominant negative forms of the GTP-hinging protein OsRacB into the wild type rice. The dominant negative foms are using two forms (full-sequence and specific RNA interference with RacB). Employing southern, and protein analysis, we examine to different things between the wild type and the transformed plant. And analyzing biolistic bombardment of onion epidermal cell with GFP-RacB fusion protein revealed association with the nucle.

• International Journal of Industrial Entomology and Biomaterials
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• v.31 no.1
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• pp.14-19
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• 2015

In a previous report, we identified several candidate antimicrobial peptides through de novo RNA sequencing of the centipede Scolopendra subspinipes mutilans. Here, we identify and characterize one of these peptides, Scolopendrasin I. We identified the centipede antimicrobial peptide Cecropin from the centipede transcriptome using an SVM algorithm, and subsequently analyzed the amino acid sequence for predicted secondary structure using a GOR algorithm. We identified an alpha helical region of Cecropin and named it Scolopendrasin I. We then assessed antimicrobial and hemolytic activity of Scolopendrasin I. Scolopendrasin I showed antimicrobial activity against various microbes, including antibiotic-resistant Gram-negative bacteria, in a radial diffusion assay. Scolopendrasin I had potent antibacterial activity against acne-associated microbes in a colony count assay and showed no hemolytic activity in a hemolysis assay. In addition, we confirmed that Scolopendrasin I bound to the surface of bacteria via a specific interaction with lipoteichoic acid and lipopolysaccharide, two components of bacterial cell membranes. In conclusion, the results presented here provide evidence that this is an efficient strategy for antimicrobial peptide candidate identification and that Scolopendrasin I has potential for successful antibiotic development.

• Journal of Microbiology and Biotechnology
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• v.26 no.12
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• pp.2019-2029
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• 2016

Zinc finger proteins are among the most extensively applied metalloproteins in the field of biotechnology owing to their unique structural and functional aspects as transcriptional and translational regulators. The classical zinc fingers are the largest family of zinc proteins and they provide critical roles in physiological systems from prokaryotes to eukaryotes. Two cysteine and two histidine residues ($Cys_2His_2$) coordinate to the zinc ion for the structural functions to generate a ${\beta}{\beta}{\alpha}$ fold, and this secondary structure supports specific interactions with their binding partners, including DNA, RNA, lipids, proteins, and small molecules. In this account, the structural similarity and differences of well-known $Cys_2His_2$-type zinc fingers such as zinc interaction factor 268 (ZIF268), transcription factor IIIA (TFIIIA), GAGA, and Ros will be explained. These proteins perform their specific roles in species from archaea to eukaryotes and they show significant structural similarity; however, their aligned amino acids present low sequence homology. These zinc finger proteins have different numbers of domains for their structural roles to maintain biological progress through transcriptional regulations from exogenous stresses. The superimposed structures of these finger domains provide interesting details when these fingers are applied to specific gene binding and editing. The structural information in this study will aid in the selection of unique types of zinc finger applications in vivo and in vitro approaches, because biophysical backgrounds including complex structures and binding affinities aid in the protein design area.

• Journal of Life Science
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• v.31 no.7
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• pp.671-676
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• 2021

A cDNA encoding the protein lethal (2) essential for life [l(2)efl] was cloned from Gryllus bimaculatus and named GBl(2)efl. This protein is composed of 189 amino acids, including an N-glycosylation site and 15 phosphorylation sites. Its predicted molecular mass is 21.19 kDa, with a theoretical isoelectric point of 6.2. The secondary structure of GBl(2)efl was predicted from the identification of random coils (56.08%), alpha helices (22.22%), extended strands (17.99%), and beta turns (3.7%) through sequence analyses. A homology analysis revealed that GBl(2)efl exhibited a high similarity with other species at the amino acid level, ranging from 52% to 69%. While GBl(2)efl mRNA expression was higher in the dorsal longitudinal flight muscle following a three-day starvation and in the Malpighian tubules following a one-day starvation, no changes in expression were detected in other tissues. Furthermore, tunicamycin-induced endoplasmic reticulum (ER) stress resulted in an approximately 1.8-fold higher expression in the fat body compared with the wild type.

• Journal of Microbiology and Biotechnology
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• v.22 no.2
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• pp.176-183
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• 2012

Eukaryotic translation termination is governed by eRF1 and eRF3. eRF1 recognizes the stop codons and then hydrolyzes peptidyl-tRNA. eRF3, which facilitates the termination process, belongs to the GTPase superfamily. In this study, the effect of the MC domain of eRF1a (eRF1aMC) on the GTPase activity of eRF3 was analyzed using fluorescence spectra and high-performance liquid chromatography. The results indicated eRF1aMC promotes the GTPase activity of eRF3, which is similar to the role of eRF1a. Furthermore, the increased affinity of eRF3 for GTP induced by eRF1aMC was dependent on the concentration of $Mg^{2+}$. Changes in the secondary structure of eRF3C after binding GTP/GDP were detected by CD spectroscopy. The results revealed changes of conformation during formation of the eRF3C GTP complex that were detected in the presence of eRF1a or eRF1aMC. The conformations of the eRF3C eRF1a GTP and eRF3C eRF1aMC GTP complexes were further altered upon the addition of $Mg^{2+}$. By contrast, there was no change in the conformation of GTP bound to free eRF3C or the eRF3C eRF1aN complex. These results suggest that alterations in the conformation of GTP bound to eRF3 is dependent on eRF1a and $Mg^{2+}$, whereas the MC domain of eRF1a is responsible for the change in the conformation of GTP bound to eRF3 in Euplotes octocarinatus.