• Plant Resources
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• v.8 no.1
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• pp.52-59
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• 2005

A cDNA, PSOD1, encoding cytosolic copper/zinc superoxide dismutase (CuZn-SOD) was cloned and characterized from a full length cDNA library prepared from Populus alba${\times}$Populus glandulosa cultured in vitro. A PSOD1, is 725 nucleotides long and has an open reading frame of 459 bp with 152 amino acid residues (pI 5.43). The deduced amino acid sequence of PSOD1 perfect matched to the previously reported CuZn-SOD (CAC33845.1). Consensus amino acid residues (His-45, -47, -62, -70, -79, -119) were involved in Cu-, Cu/Zn-, and Zn- binding ligands. The deduced amino acid sequence of PSOD1 exhibited the high level of similarity from 100 to $85\%$ among previously registered SOD genes. The expression of PSOD1 in poplar increased at the 1 mM $H_{2}O_2$ and drought stress during 30 min and 60 min, but the ozone treated poplar increased at 30 min in the early time and then decreased at 60 min.

• Journal of Microbiology and Biotechnology
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• v.10 no.5
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• pp.670-676
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• 2000

Several clones obtained from Serratia marcescens stimulated E. coli TP2139 (${\Delta}lac, \;{\Delta} crp$) cells to use maltose as a carbon source. The crp gene clone, pCKB12, was confirmed to stimulate the $\beta$-galactosidase activity, by Southern hybridization [31]. The nucleotide sequence of the crp region consisting of 1,979 bp was determined. The sequencing of the fragment led to the identification of two open reading frames: One of these, the crp gene, encoded 210 amino acid and the other encoded a truncated protein. The S. marcescens and E. coli crp genes showed a higher degree of divergence in their nucleotide sequence with 120 changes, however, the corresponding amino acid sequences showed only two amino acid differences. Yet, an analysis of the amino acid divergence revealed that the catabolite gene activator protein, the crp gene product, was the most conserved protein observed so far. Using a crp-lac protein fusion, it was demonstrated that S. marcescens CRP could repress its own expression, probably via a mechanism similar to that previously described for the E. coli crp gene.

• Journal of KIISE:Software and Applications
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• v.37 no.1
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• pp.74-79
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• 2010

The amino acid composition of a protein provides basic information for solving many problems in bioinformatics. We propose a new method that uses biologically relevant similarity between amino acids to determine the amino acid composition, where the BOLOSUM matrix is exploited to define a similarity measure between amino acids. Futhermore, to extract more information from a protein sequence than conventional methods for determining amino acid composition, we exploit the concepts of spectral analysis of signals such as radar and speech signals-the concepts of time-dependent analysis, time resolution, and frequency resolution. The proposed method was applied to predict subcellular localization of proteins, and showed significantly improved performance over previous methods for amino acid composition estimation.

• The Plant Pathology Journal
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• v.18 no.5
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• pp.251-258
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• 2002

A potyvirus was isolated from cultivated Iris plants showing leaf streak mosaic symptom. Reverse transcription and polymerase chain reaction (RT-PCR) product of 1 kb long which encoded partial nuclear inclusion B and N-terminal region of viral coat protein (CP) genes for potyviruses was successfully amplified with a set of potyvirus-specific degenerate primers with viral RNA samples from the infected leaves: The RT-PCR product was cloned into the plasmid vector and its nucleotide sequences were determined. The nucleotide sequence of a CDNA clone revealed that the virus was an isolate of Ornithogalum moseic virus (OrMV) based on BLAST search analysis and was denoted as OrMV Korean isolate (OrMV-Ky). To further characterize the CP gene of the virus, a pair of OrMV-specific primers was designed and used for amplification of the entire CP gene of OrMV-Kr, The virus was easily and reliably detected from virus-infected Iris leaves by using the RT-PCR with the set of virus-specific primers. The RT-PCR product of the CP gene of the virus was cloned and its sequences were determined from selected recombinant CDNA clones. Sequence analysis revealed that the CP of OrMV-Kr consisted of 762 nucleotides, which encoded 253 amino acid residues. The CP of OrMV-Ky has 94.1-98.0% amino acid sequence identities (20 amino acid alterations) with that of other three isolates of OrMV, Two NT rich potential N-glycosylation motif sequences, NCTS and NWTM, and a DAC triple box responsible for aphid transmission were conserved in CPs of all the strains of OrMV. The virus has 58.5-86.2% amino acid sequence identities with that of other 16 potyviruses, indicating OrMV to be a distinct species of the genus. OrMV-Ky was the most related with Pterostylia virus Yin the phylogenetic tree analysis of CP at the amino acid level. This is the first report on the occurrence of OrMV in Iris plants in Korea. Data in this study indicate that OrMV is found in cultivated Iris plants, and may have mixed infection of OrMV and Iris severe mosaic virus in Korea.

• Mycobiology
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• v.28 no.4
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• pp.171-176
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• 2000

We have cloned a ${\alpha}-COP$ homolog, ancop, from Aspergillus nidulans by colony hybridization of chromosome specific library using ${\alpha}-COP$ homologous fragment as a probe. The probe DNA was amplified with degenerated primers designed by comparison of conserved region of the amino acid sequences of Saccharomyces cerevisiae ${\alpha}-COP$, Homo sapiens HEP-COP, and Drosophila melanogaster ${\alpha}-COP$. Full length cDNA clone was also amplified by RT-PCR. Comparison of genomic DNA sequence with cDNA sequence obtained by RT-PCR revealed 7 introns. Amino acid sequence similarity search of the anCop with other ${\alpha}-COPs$ gave an overall identity of 52% with S. cerevisiae, 47% with human and bovine, 45% with Drosophila and Arabidopsis. In upstream region from the transcription start site, a putative TATA and CAAT motif were also identified.

• Journal of Applied Biological Chemistry
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• v.48 no.4
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• pp.218-221
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• 2005

Nucleotide sequence of Brevibacterium flavum ptsG gene capable of complementing Escherichia coli ZSC113 mutations defective to glucose permease activity of phosphotransferase system was completely determined, and the gene product was compared with other glucose-specific enzyme II ($EII^{Glc}$). A ptsG gene of B. flavum consisted of open reading frame of 2,025 nucleotides putatively encoding polypeptide of 675 amino acid residues and TAA stop codon. Deduced amino acid sequence of B. flavum ($EII^{Glc}$) had high homology with ($EIIs^{Glc}$) of Corynebacterium glutamicum, C. efficiens, and B. lactofermentum. Arrangement of structural domains, IIBCA, of B. flanum ($EII^{Glc}$) protein was identical to that of EIIs belonging to glucose-phosphotransferase system.

• Proceedings of the Plant Resources Society of Korea Conference
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• 2002.11b
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• pp.54-54
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• 2002

The nucleotide sequence of a Korea isolate of broad bean wilt favavirus from Rehmannia glutinosa Lib., designated BBWV-RE, was determined. Direct amino acid sequencing of the virus coat proteins suggests that a comparison of several favaviruses in terms of nucleotide sequence and amino acid sequences showed that BBWV-2 isolates display high sequence identity. The small coat protein genes of RNA-2 were also determined for three other Japanese isolates(E, L, and 1-2) and two ATCC isolates(PV132 and PV176) of BBWV. the CP sequence suggested distinct evolution lineages. Serotype 2 favaviruses are more prevalent in Asia, Australia and North America, Wheres serotype 1 is more prevalent in europe.(중략)

• The Korean Journal of Food And Nutrition
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• v.4 no.2
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• pp.161-166
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• 1991

The blocked N-terminus and N-terminal sequence of soybean B-amylase were aetermined by analyzing the acidic peptides derived on peptic digestion of the enzyme. The acidic peptides were separated from the digest on a Dowex 50$\times$2 column(1X5cm) and purified by reversed phase-high performance liquid chromatography(RP-HPLC). The major acidic peptide, PEP-1, was a heptapeptlde. The N-terminal 7 amino acid sequence of soybean B-amylase was deduced to be acetyl-Ala-Thf-Ser-Asp-Ser-Asn-Met- from the results of sequence analysis of PEP-1 and amino acid analysis of other acidic peptides.

• Korean Journal of Veterinary Research
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• v.42 no.1
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• pp.89-100
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• 2002

The nonstructural glycoprotein NSP4, encoded by the 10th gene of rotavirus, has been known to play important roles in viral assembly and pathogenesis. The NSP4 genes of human rotavirus Korean isolates, designated as CBNU/HR-1, CBNU/HR-2, CBNU/HR-3, and CBNU/HR-4, were cloned, sequenced and characterized. Also, the NSP4 gene of the CBNU/HR-1 was expressed in a baculovirus-insect cell system. The sequence data indicated that the NSP4 genes of human rotavirus Korean isolates were 750 or 751 bases in length and encoded one open reading frame of 175 amino acids. Two glycosylation sites were recognized in the NSP4 gene of human rotavirus isolates tested. The NSP4 of CBNU/HR-1, CBNU/HR-3, and CBNU/HR-4 exhibited a high degree of amino acid sequence homology with that of NSP4 genotype B viruses, but a low degree of amino acid sequence homology with that of NSP4 genotype A viruses. However, the NSP4 of CBNU/HR-2 exhibited a high degree of amino acid sequence homology with that of NSP4 genotype A viruses, but a low degree of amino acid sequence homology with that of NSP4 genotype B viruses. The Sf9 cells infected with recombinant baculovirus, inserted with NSP4 gene of CBNU/HR-1, produced specific cytopathic effects and the expressed NSP4 was detected by immunofluorescence staining using NSP4-specific monoclonal antibody(MAb). The expressed NSP4 migrated at 16-26 kDa on SDS-PAGE and reacted with NSP4-specific MAb by Western blotting.

• Preventive Nutrition and Food Science
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• v.1 no.2
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• pp.244-251
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• 1996

Molecular weight and partial amino acid sequence of the cis, 9-cis, 12-octadecadienoate isomerase(linoleate isomerase) of Butyrivibrio fibrisovens A-38 were determined. Linoleate isomerase was isolated from the bac-teria cultured anaerobically and purified by ultracentrifugation in conjunction with Sepharose 6B column chro-matography, Phenyl sepharose 4B column chromatography and fast performance liquid chromatography (EPLC). The isomerase was single polypeptide with 19KD of molecular weight, when determined by SDS-PAGE. Fourteen amino acids sequence of N-terminal of the linoleate isomerase was N-GEIDKYPRIIKQQ determined by Edman method.