• International Journal of Industrial Entomology and Biomaterials
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• v.6 no.2
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• pp.157-162
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• 2003

The glutathione S-transferase (GSTs) are enzymes responsible for the protection of cells from chemical toxicants and oxidative stress. We describe here the cDNA sequence and mRNA expression of a putative GST from the mole cricket, Gryllotalpa orientalis. The G. orientalis GST cDNA sequences comprised of 621 bp encoding 207 amino acid residues. The multiple sequence alignment of G. orientalis GST gene with other known insect GSTs showed several conserved residues that may be essential for the enzymatic activity of the protein. Phylogenetic analysis of the deduced amino acid sequences of G. orientalis GST gene with other insect GST sequences revealed that the G. orientalis GST gene belongs to class I GST, forming a strong monophyletic group (100% bootstrap value) exclusively for class I GSTs from a diverse insect species. Northern blot analysis confirmed midgut-specific expression at transcriptional level, evidencing the midgut as a site for GST synthesis.

• ALGAE
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• v.27 no.1
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• pp.55-62
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• 2012

A novel lectin specific to N-acetyl-D-galactosamine as well as N-acetyl-D-glucosamine was isolated from Bryopsis plumosa and named as BPL-4. Sodium dodecyl sulfate polyacrylamide gel electrophorese (SDS-PAGE) and matrix-assisted laser desorption / ionization-time of flight (MALDI-TOF) mass spectrometry data showed that this lectin was a monomeric protein with molecular weight 12.9 kDa. The N-terminal amino acid sequences of the lectin were determined by Edman degradation and the full cDNA sequence encoding this lectin was obtained using the degenerate primers designed from the amino acid sequence. The size of the cDNA was 414 bp containing single open reading frame (ORF) encoding the lectin precursor. The homology analysis showed that this lectin might belong to H lectin group. BPL-4 showed high sequence similarity (60.6%) to BPL-3, which is a previously reported lectin from the same species. The comparative analysis on the lectin's primary structure showed two conserved domains including one possible active domain of H lectin group.

• Journal of fish pathology
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• v.22 no.3
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• pp.343-352
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• 2009

Natural-killer-cell-enhancing factor (NKEF) belongs to the newly defined peroxiredoxin (Prx) family. It was originally isolated from human erythroid cells. The black rockfish NKEF cDNA was identified through the expressed sequence tag (EST) analysis of PBLs libraries. The full-length NKEF cDNA was 1433 bp long and contained an open reading frame (ORF) of 594 bp that encoded 198 amino-acid residues. The 5' UTR had a length of 39 bp, and the 3’UTR 800 bp. The deduced amino-acid sequence of the black rockfish had a density 93.4, 92.9, 87.8, 85.8, 84.8, 83.8, 80.3, 79.7, 77.2, and 75.2% that of the pufferfish, olive flounder, channel catfish, zebrafish, chicken, common carp, Myotis lucifugus, cattle, human PrxI, rat PrxI, human NKEF-A, and Xenopus tropicalis, respectively. The NKEF gene was expressed in all the tissues of the black rockfish. The RT-PCR indicated that the NKEF transcripts were predominantly in the spleen and gill, less dominantly in the PBLs, head kidney, trunk kidney, and liver, and least in the intestine and muscles. This is the first report on the existence of the NKEF-A gene in black rockfish.

• Journal of Microbiology and Biotechnology
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• v.22 no.5
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• pp.642-648
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• 2012

We determined the nucleotide sequence of the URA3 gene encoding orotidine-5'-phosphate decarboxylase (OMPDCase) of the erythritol-producing osmotolerant yeast Candida magnoliae by degenerate polymerase chain reaction and genome walking. Sequence analysis revealed the presence of an uninterrupted open-reading frame of 795 bp, encoding a 264 amino acid residue protein with the highest identity to the OMPDCase of the yeast Kluyveromyces marxianus. Phylogenetic analysis of the deduced amino acid sequence revealed that it shared a high degree of identity with other yeast OMPDCase homologs. The cloned URA3 gene successfully complemented the ura3 null mutation in Saccharomyces cerevisiae, revealing that it encodes a functional OMPDCase in C. magnoliae. An enzyme activity assay and reverse transcription polymerase chain reaction indicated that the expression level of the C. magnoliae URA3 gene in S. cerevisiae was not as high as that of the S. cerevisiae URA3 gene. The GenBank accession number for C. magnoliae URA3 is JF521441.

• Journal of Microbiology and Biotechnology
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• v.24 no.11
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• pp.1525-1535
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• 2014

The xynC gene, which encodes high molecular weight xylanase from Paenibacillus sp. DG-22, was cloned and expressed in Escherichia coli, and its nucleotide sequence was determined. The xynC gene comprised a 4,419bp open reading frame encoding 1,472 amino acid residues, including a 27 amino acid signal sequence. Sequence analysis indicated that XynC is a multidomain enzyme composed of two family 4_9 carbohydrate-binding modules (CBMs), a catalytic domain of family 10 glycosyl hydrolases, a family 9 CBM, and three S-layer homologous domains. Recombinant XynC was purified to homogeneity by heat treatment, followed by Avicel affinity chromatography. SDS-PAGE and zymogram analysis of the purified enzyme identified three active truncated xylanase species. Protein sequencing of these truncated proteins showed that all had identical N-terminal sequences. In the protein characterization, recombinant XynC exhibited optimal activity at pH 6.5 and $65^{\circ}C$ and remained stable at neutral to alkaline pH (pH 6.0-10.0). The xylanase activity of recombinant XynC was strongly inhibited by 1 mM $Cu^{2+}$ and $Hg^{2+}$, whereas it was noticeably enhanced by 10 mM dithiothreitol. The enzyme exhibited strong activity towards xylans, including beechwood xylan and arabinoxylan, whereas it showed no cellulase activity. The hydrolyzed product patterns of birchwood xylan and xylooligosaccharides by thin-layer chromatography confirmed XynC as an endoxylanase.

• The Journal of the Institute of Internet, Broadcasting and Communication
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• v.11 no.4
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• pp.113-118
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• 2011

Sequence homology analysis in the substances in the phenomenon of life is to create database by sorting and indexing and to demonstrate the usefulness of informatics. In this paper, Markov models are used in GenScan program to convert the pattern of complex eukaryotic protein sequences. It becomes impossible to navigate the minimum distance, complexity increases exponentially as the exact calculation. It is used scorecard in amino acid substitutions between similar amino acid substitutions to have a differential effect score, and is applied the Markov models sophisticated concealment of the transition probability model. As providing superior method to translate sequences homologous sequences in analysis using blast p, Markov models. is secreted protein structure of sequence translations.

• 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.

• Journal of Microbiology and Biotechnology
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• v.22 no.10
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• pp.1441-1445
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• 2012

The entire nucleotide sequence of the HIS3 gene encoding imidazoleglycerol phosphate dehydratase (IGPD) in yeast Candida milleri CBS 8195 was determined. Sequence analysis revealed an open-reading frame of C. milleri HIS3 that spans 678 bp, encodes 226 amino acids, and shares 80.5% amino acid identity to Torulaspora delbrueckii IGPD, followed by that to Saccharomyces cerevisiae (79.6%). The cloned HIS3 gene complemented a his3 mutation in S. cerevisiae, suggesting that it encodes a functional IGPD in C. milleri CBS 8195. A new auxotrophic marker is now available for acid-tolerant yeast C. milleri.

• Proceedings of the Microbiological Society of Korea Conference
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• 2006.05a
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• pp.129-131
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• 2006

Through molecular phylogenetic analysis using the nef gene sequences of HIV-l isolated from Korean registered in the NCBI GenBank together with 41 reference strains and 94 foreign isolates, we verified that most (${\sim}80%$) of Korean isolates belonged to subtype B and 78% of subtype B were clustered together exclusively of foreign isolates, and this cluster was named Korean clade subtype B ($K_cB$). Similarity study suggested that the $K_cB$ cluster was more homogeneous than and clearly distinctive from the non-Korean subtype B ($NK_cB$). Comparison of the consensus amino acid sequences of the $K_cB\;or\;NK_cB$ revealed characteristic $K_cB$ signature amino acid pattern comprised of 13 amino acid residues. The $K_cB$ signature amino acid residues were critical in separating the $K_cB$ ftom the $NK_cB$, since substitution of the $NK_cB$ sequences with $K_cB$ signature amino acids relocated them to the Koran clade, and vice versa. Synonymous and nonsynonymous substitution rate study suggested positive selection event for the $K_cB$.