• Journal of Microbiology
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• v.44 no.6
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• pp.617-621
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• 2006

Coprinellus congregatus secreted a laccase isozyme when the culture was transferred to an acidic liquid medium (pH 4.1). The laccase cDNA gene (clac2) was used as a probe for cloning of the genomic laccase gene (lac2) including the promoter (Plac2). The open reading frame (ORF) of lac2 had 526 deduced amino acids and four conserved copper binding domains as other fungal laccases. Recombinant plasmid (pRSlac2p-cDNA) of lac2 cDNA with its own promoter was transformed in Saccharomyces cerevisiae. Expression of the transformed lac2 gene was induced by oxidative stress ($H_2O_2$) in yeast and the survival rate of the transformed yeast strain was greatly increased when compared with that of the control strain transformed with pRS316 yeast vector.

• Journal of Microbiology and Biotechnology
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• v.8 no.5
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• pp.531-535
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• 1998

The gene encoding alginate lyase was isolated from a library constructed with the vector, pUC19, and expressed in Escherichia coli. The nucleotide sequence of the cloned alginate lyase gene (ALY) from Pseudomonas sp. W7 was determined. The nucleotide sequence revealed a 1,035 bp open reading frame (ORF), encoding 345 amino acid residues with a calculated molecular mass of 37,478 Da. The N-terminal amino acid sequences (15 residues) of purified alginate lyase corresponded to that of the deduced amino acid sequence.

• Journal of Microbiology and Biotechnology
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• v.3 no.2
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• pp.73-77
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• 1993

The nucleotide sequence of Bacillus sp. bacteriolytic enzyme gene, lytP and its flanking regions were determined. A unique open reading frame for a protein of Mw. 27, 000, and a putative terminator sequence, were found behind a concensus ribosome binding site located 8 nt upstream from ATG start codon. The primary amino acid sequence deduced from nucleotide sequence revealed a putative protein of 255 amino acid residues with an Mw. of 27, 420. No significant homology could be found between the amino acid sequence of Bacillus sp. bacteriolytic enzyme and that of other cell wall hydrolases.

• Journal of Microbiology and Biotechnology
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• v.3 no.2
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• pp.91-94
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• 1993

A 3-isopropylmalate dehydrogenase (3-IPMD) gene was cloned from Kluyveromyces fragilis. pJK104 could complement Escherichia coli leuB and Saccharomyces cerevisiae leu2 auxotrophs. The coding region was subcloned and the nucleotide sequence was determined. A 1.8 Kb EcoRI/SphI fragment of pJK104 subcloned in pUC18 could still complement the leuB mutation. An open reading frame of 1164 bp that corresponds to a polypeptide of 387 amino acids was found in the cloned fragment. The homology between the 3-isopropylmalate dehydrogenase of S. cerevisiae and that of K. fragilis was 68.13％ in nucleotides.

• Journal of Microbiology and Biotechnology
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• v.27 no.4
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• pp.834-837
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• 2017

A distinct double-stranded RNA (dsRNA) cryptic virus, named spinach cryptic virus 1 (SpCV1), was identified from spinach transcriptome datasets. The SpCV1 genome has two dsRNA genome segments. The larger dsRNA1 has an open reading frame for a conserved RNA-dependent RNA polymerase (RdRp). The smaller dsRNA2 encodes a putative coat protein (CP). The sequence identity of SpCV1 RdRp and CP to the closest cryptic virus is 81% and 60%, respectively. Phylogenetic analysis indicates that SpCV1 is a novel member of the genus Alphapartitivirus (family Partitiviridae).

• 한국생물공학회:학술대회논문집
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• 2003.10a
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• pp.536-539
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• 2003

A strong constitutive $P_{JH}$ promoter from Bacillus sp. was applied to overexpress the endoxylanase gene in Bacillus subtilis. The expression plasmid, pJHKJ4, was designed to contain the $P_{JH}$ promoter and open reading frame of endoxylanase including its own promoter. The plasmid was introduced into B. subtilis DB431 and the resulting transformant was grown on LB glucose medium. The endoxylanase activity in the culture supernatant reached about 140 unit/ml. The enzyme in the supernatant was efficiently concentrated to 70% by two-step treatments of ammonium sulfate saturation and ultrafiltration. The stabilization of concentrated enzyme solution at different storage temperatures was examined with various stabilizers such as NaCl, $CaCl_2$, sucrose, sorbitol, polyethylene glycol, and Tween-80.

• 한국생물공학회:학술대회논문집
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• 2005.04a
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• pp.396-397
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• 2005

The polyene antibiotics are a family of most promising antifungal polyketide compounds, typically produced by actinomycetes species. Using the polyene CYP-specific PCR screening with served actinomycetes genomic DNAs, Pseudonocardia autotrophica strain was identified to contain a unique polyene-specific CYP gene. The genomic DNA library screening using the polyene-specific CYP gene probe revealed the positive cosmid clone containing an approximately 34.5 kb DNA fragment revealed a total of seven complete and two incomplete open reading frame (ORFs), which are highly homologous but unique to previously-known polyene biosynthetic genes. These results suggest that the polyene-specific screening approach should be an efficient way of isolating potectially-valuable cryptic polyene biosynthetic gene cluster from various rare actinomycetes.

• Korean Journal of Medicinal Crop Science
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• v.13 no.5
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• pp.293-297
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• 2005

A thoredoxin (CTRX) gene was cloned and characterized from a full length cDNA library prepared from taproot of three-year old Codonopsis lanceolata. A CTRX was 666 nucleotides long and has an open reading frame of 372 bp with 124 amino acid residues (pI = 4.92). The deduced amino acid sequence of the CTRX matched to the previously reported plant thioredoxin h genes. The deduced amino acid sequence of CTRX exhibited the similarity of 33-67% among previously registered thioredoxin genes. The expression of CTRX in leaves of Codonopsis lanceolata was increased by wounding and 1 mM $H_2O_2$, but decreased by 0.1 mM cadmium.

• Korean Journal of Medicinal Crop Science
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• v.13 no.5
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• pp.288-292
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• 2005

A class I type 2 metallothionein (CMet2) cDNA from taproot of Codonopsis lanceolata was isolated and characterized. A CMet2 cDNA was 572 nucleotides long and had an open reading frame of 234 bp with a deduced amino acid sequence of 78 residues (pI = 4.99). The deduced amino acid sequence of CMet2 matched to the previously reported type 2 metallothionein-like protein genes and showed 74% identity with that of G. max (BAD18377) and C. arietinum (CAA65009). Expression of CMet2 by the RT-PCR was increased at 1 hr after cadmium and hydrogen peroxide treatment, respectively.

• Biotechnology and Bioprocess Engineering:BBE
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• v.11 no.4
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• pp.337-343
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• 2006

Trimethylamine dehydrogenase (TMADH, EC 1.5.99.7), an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde, was purified from Methylophaga sp. strain SK1. The active TMADH was purified 12.3-fold through three purification steps. The optimal pH and temperature for enzyme activity was determined to be 8.5 and $55^{\circ}C$, respectively. The $V_{max}\;and\;K_m$ values were 7.9 nmol/min/mg protein and 1.5 mM. A genomic DNA of 2,983 bp from Methylophaga sp. strain SK1 was cloned, and DNA sequencing revealed the open reading frame (ORF) of the gene coding for TMADH. The ORF contained 728 amino acids with extensive identity (82%) to that of Methylophilus methylotrophus $W_3A_1$.