• Journal of Microbiology and Biotechnology
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• v.12 no.1
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• pp.172-175
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• 2002

The complete nucleotide sequence of the nahC gene from Pseudomonas fluorescens, the structural gene for 1,2-dihydroxynaphthalene (1,2-DHN) dioxygenase, was determined. The 1,2-DHN dioxygenase is an extradiol ring-cleavage enzyme that cleaves the first ring of 1,2-dihydroxynaphthalene. The amino acid sequence of the dioxygenase deduced from the nucleotide sequence suggested that the holoenzyme consists of eight identical subunits with a molecular weight of approximately 34,200. The amino acid sequence of 1,2-DHN dioxygenase showed more than $90\%$ homology with those of the dioxygenases of other Pseudomonas strains. However, sequence similarity with those of the Sphingomonas species was less than $60\%$. The nahC gene of P. fluorescens was moderately expressed in E. coli NM522, as determined by enzymatic activity.

• Korean Journal of Plant Resources
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• v.16 no.3
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• pp.238-244
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• 2003

During the life cycle, plants have to suffer from various environmental stresses. A common element in response to many environmental stresses is cellular dehydration. Dehydrins are a family of proteins commonly induced by environmental stresses associated with low temperature or dehydration and during seed maturation drying. For the study in the defense mechanism against various stresses, a cDNA clone encoding a dehydrin gene was isolated from a cDNA library prepared from tab root mRNAs of Codonopsis lanceolata. The cDNA, designated ClDhn1, is 893 nucleotides long and has an open reading frame of 480 bp with a deduced amino acid sequence of 159 residues. The ClDhn1 amino acid sequence is highly hydrophilic and possesses two conserved repeats of characterized lysine­rich K­segment (KIKEKLPG), and a 7­serine residue stretch prior to the first lysine­rich repeat that is common to many dehydrins. The DEYGNP conserved motif is, however, modified in the sequence of ClDhn1 gene. The deduced amino acid sequence of ClDhn1 was compared with other plant dehydrinls and showed high homology with Solanum commersonii

• The Plant Pathology Journal
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• v.19 no.3
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• pp.171-176
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• 2003

The complete nucleotide sequences of the genomic RNAs of Soybean mosaic virus strains GS (SMV-G5) and G7H (SMV-G7H) were determined and compared with sequences of other SMV strains. Each viral RNA was determined to be 9588 nucleotides in length excluding the poly (A) tail and contained an open reading frame to encode a polyprotein subsequently processed into up to ten proteins by proteolytic cleavage. Com-parison of the amino acid sequences with those of other SMV strains showed high percentage of amino acid sequence homology with the same genome organization. The nucleotide and the deduced amino acid sequences between SMV-G5 and SMV-G7H were greater than 99% identity. When compared with those of other SMV strains in a phylogenetic analysis of the nucleotide and deduced amino acid sequences, they formed a distinct virus clade showing over 97％ amino acid identity, but were more distantly related to the other potyvirus (44.1-69.6% identity). Interestingly, SMV G7H strain caused a severe mosaic or necrosis symptom in soybean cultivars including Jinpum-1, Jinpum-2, and Sodam, whereas, no symptom was observed in SMV-G5 inoculation. Complete nucleotide sequences of these strains will give clues for determining symptom determinant(s) in future research.

• Korean Journal of Microbiology
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• v.41 no.1
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• pp.13-17
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• 2005

The aim of this work was to investigate the N-terminal amino acid sequence of catechol 2,3-dioxygenase isolated from Delftia sp. JK-2, which could utilize aniline as sole carbon, nitrogen and energy source. Molecular weight of the enzyme was determined to approximately 35 kDa by SDS-PAGE. N-terminal amino acid sequence of C2,3O from strain JK-2 was $^1MGVMRIGHASLKVMDMDAAVRHYENV^{26}$, and exhibited high sequence similarity with that of C2,3O from Pseudomonas sp., Comamonas sp. JS765, Comamonas test-osteroni, or Burkholderia sp. RP007. Approximately 950-bp C2,3O was obtained through PCR using the primers derived from N-terminal amino acid sequence. Analysis of the DNA sequence revealed that the deduced 296 amino acid sequences were determined, and it showed $100\%$ identity with C2,3O from Pseudomonas sp. AW-2 and $97\%$ similarity with Comamonas sp. JS765.

• Fisheries and Aquatic Sciences
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• v.6 no.2
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• pp.101-104
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• 2003

A cDNA clone for the olive flounder (Paralichthys olivaceus) transferrin receptor (fTfR) was isolated from a leukocytes cDNA library. The fTfR gene consisted of 2,319 bp encoding 773 amino acid residues. The amino acid sequence alignment of the fTfR showed that their size and hydrophobic profile are similar. In addition, the Tyr-Thr-Arg-Phe (YTRF) motif that is the recognition signal for high-efficiency endocytosis, is conserved very well. This motif is important for functional properties of TfR. The deduced amino acid sequence had $42.4-42.9\%$ identities with the previously reported TfRs of vertebrates. The fTfR was expressed in the blood, kidney, spleen, and liver of healthy olive flounder by the Northern blot hybridization.

• Journal of Photoscience
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• v.4 no.3
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• pp.141-145
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• 1997

Polymerase chain reaction(PCR) was conducted with a pea cDNA library using two primers synthesized from homology analysis of amino acid sequences for animal and plant cytosolic FBPases. A PCR product with 650 bp long was cloned into pGEM-T vector and sequenced. The deduced amino acid sequence of the cDNA fragment was 98, 91, and 85% homologous with those of cytosolic FBPases from spinach, sugarbeet, and sugarcane, respectively. It was 51% homologous with amino acid sequence of FBPase from pea chloroplasts. Northern blot analysis was proceeded with the cDNA clone resulting that 1.2 kb transcript was highly expressed in light-grown pea leaves but almost not expressed in dark-grown etiolated pea seedlings. When peas grown in the light for 10 days were transferred to darkness, the transcript was gradually decreased with dark treatment, indicating that the expression of the enzyme was induced by continuous white light but suppressed by dark treatment. Pea cytosolic FBPase was highly expressed in leaves with trace amounts in stems. but almost not expressed in roots.

• Journal of Microbiology and Biotechnology
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• v.5 no.5
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• pp.305-308
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• 1995

From the plasmid library made from Sstl and San-digested genomic DNA of Streptomyces fradiae NRRL 2702, four positive clones were selected using an oligodeoxynucleotide probe from the N-terminal amino acid sequence of purified threonine dehydratase. The cloned gene for threonine dehydratase was a 2.0 kilo-base pair DNA fragment. The deduced amino acid sequence of PCR product (PCR245) was matched to that of the N-terminal part of threonine dehydratase from S. fradiae and this showed a high similarity to the threonine dehydratases of other organisms. This indicated that amino acid sequences of threonine dehydratases were highly conserved and the polypeptide product of the PCR245 was likely to be involved in the deamination of threonine.

• BMB Reports
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• v.32 no.4
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• pp.399-404
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• 1999

2,3-Dihydroxybiphenyl 1,2-dioxygenase (2,3-DHBD), which catalyzes the ring meta-cleavage of 2,3-dihydroxybiphenyl, is encoded by the phnQ gene of biphenyl- and phenanthrene-degrading Pseudomonas sp. strain DJ77. We determined the nucleotide sequence of a DNA fragment of 1497 base pairs which included the phnQ gene. The fragment lncluded an open reading frame of 903 base pairs to accommodate the enzyme. The predicted amino acid sequence of the enzyme subunit consisted of 300 residues. In front of the gene, a sequence resembling an E. coli promoter was identified, which led to constitutive expression of the cloned gene in E. coli. The deduced amino acid sequence of the PhnQ enzyme exhibited 85.6% identity with that of the corresponding enzyme in Sphingomonas yanoikuyae Q1 (formerly S. paucimobilis Q1) and 22.1% identity with that of catechol 1,2,3-dioxygenase from the same DJ77 strain. PhnQ showed broader substrate preference than previously-cloned PhnE, catechol 2,3-dioxygenase. Ten amino acid residues, considered to be important for the role of extradiol dioxygenases, were conserved.

• Journal of Microbiology and Biotechnology
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• v.10 no.2
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• pp.244-250
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• 2000

An ${\alpha}-glucosidase$ gene (aglA) from thermophilic Bacillus sp. DG0303 was cloned, sequenced, and expressed in Escherichia coli. The aglA was localized to the 2.1-kb PvuI-XmnI region within the 5.9-kb DNA insert of the gybrid plasmid pAG1. The gene consisted of an open reading frame of 1,686 bp with an unusual GTG initiation codon and TGA termination codon. The amino acid sequence deduced from the nucleotide sequence predicted a protein of 562 amino acid residues with a M, of 66,551 dalton. A comparative amino acid sequence analysis revealed that DG0303 ${\alpha}-glucosidase$ is related to bacillary oligo-1, 6-glucosidases. The Bacillus sp. DG0303 ${\alpha}-glucosidase$ showed a high sequence identity (36-59%) to the B. flavocaldarius, B. cereus, and B. thermoglucosidasius oligo-1, 6-glucosidases. The number of prolines in theses four ${\alpha}-glucosidases. was observed to increase with increasing thermostability of these enzymes. The cloned ${\alpha}-glucosidase was purified from E. coli $DH5{\alpha}$ bearing pAG1 and characterized. The recombinant enzyme was identical with the native enzyme in its optimum pH and in its molecular mass, estimated by sodium dodecy1 sulfate-polyacrylamide gel electrophoresis. The temperature optimum of the cloned ${\alpha}-glucosidase$ was lower than that of the native enzyme.

• Journal of Microbiology and Biotechnology
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• v.20 no.4
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• pp.670-677
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• 2010

An alkaline pectate lyase, Bsp165PelA, was purified to homogeneity from the culture broth of alkaliphilic Bacillus sp. N16-5. The enzyme showed a specific activity as high as 1,000 U/mg and had optimum activity at pH 11.5 and $50^{\circ}C$. It was composed of a single polypeptide chain with a molecular mass of 42 kDa deduced from SDS-PAGE, and its isoelectric point was around pH 6.0. It could efficiently depolymerize polygalacturonate and pectin. Characterization of product formation revealed unsaturated digalacturonate and trigalacturonate as the main products. The pectate lyase gene (pelA) contained an open reading frame (ORF) of 1,089 bp, encoding a 36-amino acids signal peptide and a mature protein of 326 amino acids with a calculated molecular mass of 35.943 Da. The deduced amino acid sequence from the pelA ORF exhibited significant homology to those of known pectate lyases in polysaccharide lyase family 1. Some conserved active-site amino acids were found in the deduced amino acid sequence of Bsp165PelA. $Ca^{2+}$ was not required for activity on pectic substrates.