• Development and Reproduction
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• v.16 no.4
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• pp.371-378
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• 2012

Notch signaling plays fundamental roles in various animal development. It has been suggested that Hr-Notch, a Notch homologue in the ascidian Halocynthia roretzi, is involved in the formation of peripheral neurons by suppressing the neural fates and promoting the epidermal differentiation. However, roles of Notch signaling remain controversial in the formation of nervous system in ascidian embryos. To precisely investigate functions of Notch signaling, we have isolated and characterized Hr-Numb, a Numb homologue which is a negative regulator of Notch signaling, in H. roretzi. Maternal expression of Hr-Numb mRNAs was detected in egg cytoplasm and the transcripts were inherited by the animal blastomeres. Its zygotic expression became evident by the early neurula stage and the transcripts were detected in dorsal neural precursor cells. Suppression of Hr-Numb function by an antisense morpholino oligonucleotide resulted in larvae with defect in brain vesicle and palps formation. Similar results have been obtained by overexpression of the constitutively activated Hr-Notch forms. Therefore, these results suggest that Hr-Numb is involved in Notch signaling during ascidian embryogenesis.

• Journal of fish pathology
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• v.20 no.3
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• pp.299-306
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• 2007

Cysteine-cysteine chemokine receptor 9 (CCR9) homologue cDNA was isolated from olive flounder leukocyte cDNA library. Olive flounder CCR9 homologue consisted of 1709 bp encoding 367amino acid residues. When compared with other known CCR peptide sequences, the most conserved region of the olive flounder CCR9 peptide is the seven transmembranes. A phylogenetic analysis based on the deduced amino acid sequence showed the homologous relationship between the olive flounder CCR9 sequence and that of Mouse CCR9. The olive flounder CCR9 gene was predominantly expressed in the Peripheral blood leukocytes (PBLs), kidney, spleen, and gills.

• International Journal of Industrial Entomology and Biomaterials
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• v.11 no.2
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• pp.113-117
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• 2005

A chymotrpsin gene homologue was cloned from the mulberry longicorn beetle, Apriona germari. The A. germari chymotrypsin cDNA contains an ORF of 950 nucleotides capable of encoding a 283 amino acid polypeptide with a predicted molecular mass of 29151 Da and pI of 9.38. The A. germari chymotrypsin has conserved six cysteine residues and active triad formed by His, Asp and Ser. The deduced amino acid sequence of the A. germari chymotrypsin cDNA was closest in structure to the Anthonomus grandis chymotrypsin. Northern blot analysis revealed that A. germari chymotrypsin showed the midgut-specific expression.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.04a
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• pp.67-67
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• 2003

The NAD$^{+}$-dependent 15-hydroxyprostagladin dehydrogenase (15-PGDH) is a key catabolic enzyme responsible for the control of the biological activities of prostagladins. So far the gene has been found in a diverse organism including three insect dipteran species and one lepidopteran species. In this study, a cDNA encoding the 15-PGDH gene homologue was isolated from the cDNA library of the mole cricket, Gryllotalpa orientalis. (omitted)d)

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.04a
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• pp.68-68
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• 2003

The glutathione-S-transferases (GSTs) are enzymes responsible for the protection of cells from chemical toxicants and oxidative stress. In insects, GSTs have been particularly known to be implicated in the resistance to insecticides. In this study, a cDNA encoding the GST gene homologue was isolated from the cDNA library of the mole cricket, Gryllotalpa orientalis. (omitted)

• Proceedings of the Korean Biophysical Society Conference
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• 1996.07a
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• pp.26-26
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• 1996

The methionine-rich segments of the Fifty four homologue (Ffh) protein of Escherichia coli and its eukaryotic counterpart SRP54 are thought to bind signal sequences of secretory proteins. The structure of a chemically synthesized 25-residue-long peptide corresponding to one of the proposed methionine rich amphiphilic helices of Ffh was determined in water and in aqueous trifluroethanol (TFE) solution using CD ard NMR. (omitted)

• Proceedings of the Microbiological Society of Korea Conference
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• 2009.05a
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• pp.123-124
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• 2009

• BMB Reports
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• v.39 no.6
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• pp.686-695
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• 2006

Interleukin-2 enhancer binding factor 2 (ILF2) was reported to regulate transcription of interleukin-2 (IL-2), a central cytokine in the regulation of T-cell responses. This property of ILF2 was well characterized in human and mammals, but little is known in bony fish. In this paper, an ILF2 homologue was cloned and well characterized from Tetraodon nigrovirid is for the further investigation of the function of ILF2 in bony fish. The full-length Tetraodon ILF2 cDNA was 1380 bp in size and contained an open reading frame (ORF) of 1164 bp that translates into a 387 amino-acid peptide with a molecular weight of 42.9 kDa, a 5' untranslated region (UTR) of 57 bp, and a 3' UTR of 159 bp containing a poly A tail. The deduced peptide of Tetraodon ILF2 shared an overall identity of 58%~93% with other known ILF2 sequences, and contained two N-glycosylation sites, two N-myristoylation sites, one RGD cell attachment sequence, six protein kinase C phosphorylation sites, one amino-terminal RGG-rich single-stranded RNA-binding domain, and a DZF zinc-finger nucleic acid binding domain, most of which were highly conserved through species compared. Constitutive expression of Tetraodon ILF2 was observed in all tissues examined, including gill, gut, head kidney, spleen, liver, brain and heart. The highest expression was detected in heart, followed by liver, head kidney and brain. Stimulation with LPS did not significantly alter the expression of Tetraodon ILF2. Gene organization analysis showed that the Tetraodon ILF2 gene have fifteen exons, one more than other known ILF2 genes in human and mouse. Genes up- and down-stream from the Tetraodon ILF2 were Rpa12, Peroxin-11b, Smad4, Snapap and Txnip homologue, which were different from that in human and mouse.

• Bulletin of the Korean Chemical Society
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• v.29 no.2
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• pp.381-388
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• 2008

An X-linked skeletal disorder, SEDT (spondyloepiphyseal dysplasia tarda) is a genetic disease characterized by a disproportionately short trunk and short stature caused by mutations in the SEDL gene. This gene is evolutionarily conserved from yeast to human. The yeast SEDL protein ortholog, Trs20p, has been isolated as a member of a large multi-protein complex called the transport protein particle (TRAPP), which is involved in endoplasmic reticulum (ER)-to-Golgi transport. The interaction between SEDL and partner proteins is important in order to understand the molecular mechanism of SEDL functions. We isolated several SEDL-binding proteins derived from rat cells by an immobilized GST-fusion method. Furthermore, the SEDL-homologue proteins were identified using motif based methods. Common motifs between SEDL-binding proteins and SEDL-homologue proteins were classified into seven types and 78 common motifs were revealed. Sequence similarities were contracted to seven types using phylogenetic trees. In general, types I-III and VI were classified as having the function of acetyl-CoA carboxylase, glycogen phosphorylase, isocitrate dehydrogenase, and enolase, respectively, and type IV was found to be functionally related to the GST protein. Types V and VII were found to contribute to TRAPP vesicle trafficking.

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2001.11a
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• pp.129-129
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• 2001