• 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.

• Korean Journal of Microbiology
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• v.31 no.1
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• pp.44-47
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• 1993

A replication initiation gene was identified and its nucleotide sequence has been determined from a 3.8 kb, chloramphenicol acethyltransferase conferring R-plasmid pSBK203 of Staphylococcus aures. Location of the replication related region of pSBK 203 was determined by interuption with pUC 119 at XBaI and MspI sites which resulted in inactivation of replication in Bacilius subtilis. Base sequence of this region revealed on open reading frame of 942 base pairs, which encoded a 314 amino acid protein. Base sequence homology with other rep of pT181 family plasmids such as pT181, pC221, pC223, pS194, pU112, and pCW7 was ranged from 78% to 97% and the predicted amino acid sequence homology was from 72% to 95%.

• Journal of Microbiology and Biotechnology
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• v.6 no.6
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• pp.369-374
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• 1996

The ${\beta}$-lactamase inhibitory protein (BLIP) produced by Streptomyces exfoliatus SMF19 was purified(33 kDa) and the N-terminal amino acid sequence was determined as NH2-ATSVVAWGGNND. Genomic DNA library of S. exfoliatus SMF19 was constructed in pWE15 and recombinants harbouring the corresponding gene were selected by colony hybridization to the mixture of 36-mer oligonucleotide designed from the N-terminal amino acid sequence. The corresponding gene (bliX) was isolated on a 4-kb ApaI fragment of S. exfoliatus SMF19 chromosomal DNA and then sequenced. The bliX consisting of 1, 119bp encoded a mature protein with a deduced amino acid sequence of 342 residues and also encoded a 40-amino-acid signal sequence. No significant sequence similarity to bliX was found by pairwise comparison using various protein and nucleotide sequences.

• Journal of fish pathology
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• v.8 no.1
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• pp.37-46
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• 1995

The amino acid analysis of polyhedrin protein and nucleotide sequence of polyhedrin gene in H. cunea nuclear polyhedrosis virus (HcNPV) genome have been studied. Polyhedrin had three polypeptide bands in SDS - polyactylamide gel electrophoresis. The major polypeptide had a molecular weight of 25 kd. The polyhedrin was composed of 17 different amino acids. HcNPV DNA was digested with EcoRI restriction enzyme and hybridized with ($\alpha^{32}P$) -labelled AcNPV polyhedrin gene cDNA. The polyhedrin gene was located on the fragment of EcoRI-H. The EcoRI - H fragment containing polyhedrin gene was cloned into the EcoRI site of pUC8 vector which was confirmed with southern blotting, and the recombinant plasmid containg polyhedrin gene was designated as hPE-H. The promoter region of polyhedrin genomic DNA was sequenced. The sequences identified as the TATA box was found at the 5' flanking region of the polyhedrin genomic DNA approximately -79 bp upstream from the transcriptional start site. But CAAT-like box was not shown near the TATA-like box in the polyhedrin gene. Four tandem repeats with the sequence 5' -CTAATAT-3' and 5'-TAAATAA-3' were found between -141 and -108 or -83 upstream and -52 bp downstream from the translation start site. About -141 bp region upstream from the translational start site was highly AT (78%) rich. The coding region for the polyhedrin starts and ends with ATG and TAA, respectively.

• Journal of Microbiology and Biotechnology
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• v.11 no.1
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• pp.106-111
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• 2001

A ${\beta}-galactosidase$ gene of Bifidobacterium adolescentis Int57 (INT57) was cloned using the shotgun method. The sequence of the ${\beta}-galactosidase$ gene existing in the sequenced 3,260-bp fragment showed higher than 40% homology with other bacterial ${\beta}-galactosidase$ genes. The expression in Escherichia coli suggested that the ${\beta}-galactosidase$ might have a monomeric, dimeric, or tetrameric protein structure. This is probably the first peer-reviewed sequence analysis of the ${\beta}-galactosidase$ gene of the genus Bifidobacterium.

• Microbiology and Biotechnology Letters
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• v.21 no.6
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• pp.534-541
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• 1993

The relationship between Schwanniomyces occidentalis CBS 2863 (formerly castellii) and CBS 1153 (formerly alluvius), and their variety persoonii was examined at alpha-amylase gene level. Using Sch. occidentalis alpha-amylase gene as probe, Sch. occidentalis alpha-amylase gene homologues were obtained from Sch. occidentalis CBS 1153 and Sch. occidentalis var. persoonii. The restriction analysis of these homologues showed that the restriction enzyme sites between Sch. occidentalis CBS 2863 and CBS 1153 was identical but different between these strains and Sch. occidentalis var. persoonii.

• Journal of Veterinary Science
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• v.24 no.3
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• pp.40.1-40.6
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• 2023

Analysis of the VP1 gene sequence of the foot and mouth disease virus (FMDV) is critical to understanding viral evolution and disease epidemiology. A standard set of primers have been used for the detection and sequence analysis of the VP1 gene of FMDV directly from suspected clinical samples with limited success. The study validated VP1-specific degenerate primer-based reverse transcription polymerase chain reaction (RT-PCR) for the qualitative detection and sequencing of serotype O FMDV lineages circulating in India. The novel degenerate primer-based RT-PCR amplifying the VP1 gene can circumvent the genetic heterogeneity observed in viruses after cell culture adaptation and facilitate precise viral gene sequence analysis from clinical samples.

• The Journal of Korean Society of Virology
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• v.26 no.1
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• pp.131-137
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• 1996

The sequences of p10 gene its promoter of Hyphantria cunea NPV were determined. According to the sequence analysis, the putative p10 gene ORF has 285 bp. The 5'-non-coding leader sequence of the p10 gene promoter contained the TATA box and the putative transcription initiation site TAAG motif. Poly (A) tail signals, AATAAA sequence was at site 65 base upstream from the 3' terminus. The deduced amino acid sequence of p10 protein was 95 with a predicted molecular weight of 10.26 kDa. In the p10 protein sequence, a hydrophobic region was present at the N-terminus of the protein, whereas the C-terminus was highly hydrophilic. The p10 protein of H. cunea NPV did not contain cysteine, histidine, trytophan, tryptophane, tyrosine, glutamine and asparagine residues.

• Microbiology and Biotechnology Letters
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• v.18 no.3
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• pp.309-316
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• 1990

The sequence of a 1795 bp restriction fragment containing the B. circulans F-2 gene for NaC1- dependent $\alpha$-amylase (CI-amylase) is reported. The probable coding region of the gene is 1005 base pairs (335 amino acida) long. The NaC1-dependent $\alpha$-amylase (el-amy) sequence shows an open reading frame (ORF) with the translated molecular weight of about 38, 006, which correspond to a molecular weight of about 35, 000 (Mi). The gene is preceded by the sequence resembling promoter for the vegetative B, subtitis RNA polymerases. These are followed by the sequences resembling a B. subtilis ribosome binding site 5 nucleotides before the first codon of the gene. Homologous regions with other amylases were found. The N-terminal sequences of the mature proteins expressed in E. eoli were identical to the N-terminal sequences which are anaIysed.

• BMB Reports
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• v.30 no.1
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• pp.41-45
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• 1997

The present study was performed to analyze the molecular mechanism which dictates the transcription regulation of the $O^6$-methylguanine-DNA methyltransferase (MGMT) gene in Saccharomyces cerevisiae. Previously we identified one possible upstream repressing sequence (URS) in MGMT promoter by promoter deletion and competition analysis. In this paper we report another regulatory element (UAS: upstream activating sequence. -213 to -136) which affects the transcription activity of MGMT promoter. Gel mobility shift assay and Southwestern blot analysis using UAS probe showed several specific proteins which were able to bind to this sequence.