• Molecules and Cells
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• v.37 no.5
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• pp.357-364
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• 2014

Medulloblastoma, the most common malignant brain tumor in children, is a disease whose mechanisms are now beginning to be uncovered by high-throughput studies of somatic mutations, mRNA expression patterns, and epigenetic profiles of patient tumors. One emerging theme from studies that sequenced the tumor genomes of large cohorts of medulloblastoma patients is frequent mutation of RNA binding proteins. Proteins which bind multiple RNA targets can act as master regulators of gene expression at the post-transcriptional level to co-ordinate cellular processes and alter the phenotype of the cell. Identification of the target genes of RNA binding proteins may highlight essential pathways of medulloblastomagenesis that cannot be detected by study of transcriptomics alone. Furthermore, a subset of RNA binding proteins are attractive drug targets. For example, compounds that are under development as anti-viral targets due to their ability to inhibit RNA helicases could also be tested in novel approaches to medulloblastoma therapy by targeting key RNA binding proteins. In this review, we discuss a number of RNA binding proteins, including Musashi1 (MSI1), DEAD (Asp-Glu-Ala-Asp) box helicase 3 X-linked (DDX3X), DDX31, and cell division cycle and apoptosis regulator 1 (CCAR1), which play potentially critical roles in the growth and/or maintenance of medulloblastoma.

• Parasites, Hosts and Diseases
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• v.53 no.5
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• pp.583-595
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• 2015

DEAD/DExH-box RNA helicases catalyze the folding and remodeling of RNA molecules in prokaryotic and eukaryotic cells, as well as in many viruses. They are characterized by the presence of the helicase domain with conserved motifs that are essential for ATP binding and hydrolysis, RNA interaction, and unwinding activities. Large families of DEAD/DExH-box proteins have been described in different organisms, and their role in all molecular processes involving RNA, from transcriptional regulation to mRNA decay, have been described. This review aims to summarize the current knowledge about DEAD/DExH-box proteins in selected protozoan and nematode parasites of medical importance worldwide, such as Plasmodium falciparum, Leishmania spp., Trypanosoma spp., Giardia lamblia, Entamoeba histolytica, and Brugia malayi. We discuss the functional characterization of several proteins in an attempt to understand better the molecular mechanisms involving RNA in these pathogens. The current data also highlight that DEAD/DExH-box RNA helicases might represent feasible drug targets due to their vital role in parasite growth and development.

• Korean Journal of Microbiology
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• v.46 no.3
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• pp.233-239
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• 2010

Four genes (yqfR, yfmL, ydbR, deaD) were identified as putative DEAD-box RNA helicase genes in the genomic sequence of Bacillus subtilis by homology search. To understand the function of these genes, each of the genes was deleted and the constructed strains were tested for their growth charateristics at different temperatures. The growth rate of ydbR deletion mutant ($T_d$=53 min) was a little bit reduced at $37^{\circ}C$ as compared to that of wild type strain (CU1065). But the growth rate of other three (yqfR, yfmL, deaD) deletion mutants ($T_d$=30-40 min) is nearly equal to the growth rate of wild type ($T_d$=32 min). On the other hands, the growth rate of deletion mutants were reduced at $22^{\circ}C$ in order of yqfR ($T_d$=151 min), yfmL ($T_d$=214 min), ydbR ($T_d$=343 min), which showed cold-sensitive phenotype. The deletion mutant of deaD ($T_d$=109 min) grew equally as compared to the growth rate ($T_d$=102 min) of the wild type at $22^{\circ}C$ and did not show cold-sensitive growth. Double, triple and quadruple deletion mutants of these genes were constructed, and growth rate of these mutants were measured at various temperature conditions ($22^{\circ}C$, $37^{\circ}C$, $42^{\circ}C$) using LB broth. Multiple deletion mutations showed more severe cold-sensitive growth than single deletion mutations, and double deletion of ydbR and yfmL ($T_d$=984 min) showed most cold-sensitive growth than any other double mutants. Such a cold-sensitive growth of these mutations is quite similar to the result of csdA or srmB deletion in E. coli and suggested that physiological role of ydbR and yfmL is related with ribosome assembly.

• Korean Journal of Microbiology
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• v.50 no.2
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• pp.95-100
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• 2014

Hrq1 is a novel member of RecQ helicase family, found in fungal genomes by bioinformatics analyses. It is most homologous to human RECQL4 and recent genetic and biochemical studies suggested that it may play roles in the maintenance of genome stability. In this study, we investigated yeast two-hybrid interactions between Hrq1 and the yeast genes homologous to the human genes that are known to interact with RECQL4. Among the 11 genes tested, Rad14, a nucleotide excision repair (NER) factor, was found to interact with Hrq1. In addition, pull-down assay with the purified proteins revealed direct protein-protein interaction between Hrq1 and Rad14. The yeast two-hybrid interaction was enhanced by the DNA damage induced by 4-nitroquinoline-1-oxide, which was dependent on the presence of Rad4, a key NER factor. These results suggest that Hrq1 may function in NER through interaction with Rad14.

• Journal of the Korea Organic Resources Recycling Association
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• v.23 no.1
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• pp.70-81
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• 2015

Helicases are known to be a proteins that use the chemical energy of NTP binding and hydrolyze to separate the complementary strands of double-stranded nucleic acids to single-stranded nucleic acids. They participate in various cellular metabolism in many organisms. DEAD-box proteins are ATP-dependent RNA helicase that participate in all biochemical steps involving RNA. DEAD-box3 (DDX3) gene is belonging to the DEAD-box family and plays an important role in germ cell development in many organisms including not only vertebrate, but also invertebrate during asexual and sexual reproduction and participates in stem cell differentiation during regeneration. In this study, in order to identify and characterize DDX3 gene in the earthworm, Perionyx excavatus having a powerful regeneration capacity, total RNA was isolated from adult head containing clitellum. Full length of DDX3 gene from P. excavatus, Pe-DDX3, was identified by RT-PCR using the total RNA from head as a template. Pe-DDX3 encoded a putative protein of 607 amino acids and it also has the nine conserved motifs of DEAD-box family, which is characteristic of DEAD-box protein family. It was confirmed that Pe-DDX3 has the nine conserved motifs by the comparison of entire amino acids sequence of Pe-DDX3 with other species of different taxa. Phylogenetic analysis revealed that Pe-DDX3 belongs to a DDX3 (PL10) subgroup of DEAD-box protein family. And it displayed a high homology with PL10a, b from P. dumerilii.

• Journal of Life Science
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• v.15 no.1 s.68
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• pp.124-131
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• 2005

The regulation of gene expression plays an important rolet in cell cycle controls. In this study, a novel $mas3^+$ (mitosis associated protein) gene, a homolog of human SMARCADl, was isolated and characterized from a fission yeast Schizosaccharomyces pombe. The overall homology between the helicase proteins of the two species is $87\%$. This DEAD/H box-containing molecule has seven highly conserved sequence regions that allow us to place it in the SNF2 family of the helicase superfamily. Knock-out cell of $mas3^+$ gene was constructed using kanMX6 as a selection marker. Survival of mas3 null mutant exposed to UV or MMS was similar to those of wild type cells. $mas3^+$ expression was lowest at $G_2$ and gradually increased. Cytokinesis of mas3 null mutant was abnormal at $26^{\circ}C\;and\;35^{\circ}C$ and a large number of multi-septate cells were produced. These results indicate that the $mas3^+$ is involved in cytokinesis and cell shape control.

• Journal of Life Science
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• v.6 no.3
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• pp.185-192
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• 1996

Bacteriophage T7 gene 2.5 protein, a single-stranded DNA binding protein, is required for T7 DNA replication, recombination, and repair. T7 gene 2.5 protein has two distinctive domains, DNA binding and C-terminal domain, directly involved in protein-protein interaction. Gene 2.5 protein participates in the DNA replication of Bacteriophage T7, which makes this protein essential for the T7 growth and DNA replication. What gene 2.5 protein makes important at T7 growth and DNA replication is its binding affinity to single-stranded DNA and the protein-protein important at T7 DNA replication proteins which are essential for the T7 DNA synthesis. We have constructed pGST2.5(WT) encoding the wild-type gene 2.5 protein and pGST2.5$\Delta $21C lacking C-terminal 21 amino acid residues. The purified GST-fusion proteins, GST2.5(WT) and GST2.5(WT)$\Delta$21C, were used for whether the carboxyl-terminal domain participates in the protein-protein interactions or not. GST2.5(WT) and GST2.5$\Delta$21C showed the difference in the protein-protein interaction. GST2.5(WT) interacted with T7 DNA polymerase and gene 4 protein, but GST2.5$\Delta$21C did not interact with either protein. Secondly, GST2.5(WT) interacts with gene 4 proteins (helicase/primase) but not GST2.5$\Delta$21C. these results proved the involvement of the carboxyl-terminal domain of gene 2.5 protein in the protein-protein interaction. We clearly conclude that carboxy-terminal domain of gene 2.5 protein is firmly involved in protein-protein interactions in T7 replication proteins.

• Proceedings of the Korean Biophysical Society Conference
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• 1996.07a
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• pp.24-24
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• 1996

SecA protein of E. coli is essential for the translocation of various precursor proteins across the plasma membrane. Along with it, SecA protein interacts with precursor proteins, SecY/E, SecB and is an ATPase which has multiple ATP binding sites. There is little known about the regulation mechanism of the protein translocation machinery. (omitted)

• Proceedings of the Microbiological Society of Korea Conference
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• 1998.04a
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• pp.52.2-52.2
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• 1998

• Journal of Life Science
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• v.21 no.5
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• pp.626-630
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• 2011

In October 2008, a pair of Crested ibis Nipponia nippon, an endangered avian species in the world, was donated to Korea from China. They have since been the subject of a successful program to incubate chicks for the first time in South Korea. This study was carried out to determine the sex of chicks from the Crested ibis through polymerase chain reaction (PCR) using the sex-related gene and the chromodomain helicase DNA binding protein (CHD) gene. The result of the CHD gene, which was used with a single set of primers and a restriction enzyme treatment after the PCR process, was more accurate in identifying the gender of the Crested ibis. In addition, we compared the CHD gene sequences with the previously reported sequences and found 1~2 different bases between females (CI2, CI4, CI5, and CI6) than in studies previously reporting female sequences.