• Korean Journal of Microbiology
• /
• v.42 no.1
• /
• pp.67-72
• /
• 2006

The nucleotide sequence of the cloned cellulolytic xylanase gene (bglBC2) from B. circulans ATCC21367 was determined. bglBC2 consists of an 1,224 bp open reading frame (ORF) coding for a polypeptide of 407 amino acids with a deduced molecular weight of 45 kDa. The Shine-Dalgarno (SD) sequence (5'-AAAGGAG-3') was found 9 bp upstream of the initiation codon, ATG. A promoter region corresponding closely to the B. subtilis consensus sequence (-35: TTGACA,-10: TATAAT) was detected, the putative -35 and -10 sequences of which were TTTACA and TATACT, respectively. The deduced amino acid sequence of the cellulolytic xylanase showed 97% homology with that of the alkaline $endo-\beta-1,4-glucanase$ from B. circulans KSM-N257, 75% homology with that of the $endo-\beta-1,3-1,4-glucanase$ from B. circulans WL-12, and 45% homology with that of the $endo-\beta-1,4-glucanase$ (cellulase) from Bacillus sp. KSM-330. The bglBC2 sequence was deposited in Gen-Bank under the accession number AY269256.

• Proceedings of the Microbiological Society of Korea Conference
• /
• 2001.11a
• /
• pp.138-145
• /
• 2001

The hydrophobic spores of Streptomyces sp. AA8321 isolated from the Antarctic coast displayed demulsification ability. The aerial spores demulsified an emulsion of kerosene/$0.2\%$ Triton X-100 (2:1, v/v) to $50\%$ and $95\%$ within 1 min contact at the concentrations of $5.0{\times}10^7$ and $1.0{\times}10^8$ spores/ml, respectively. A cold shock protein (csp) gene was cloned from the hydrophobic spore- producing Streptomyces sp. AA8321 using PCR. It encoded a low molecular protein with 68 amino acids showing very low homology with previously reported csp genes. Only the sequence of the first six amino acids was just the same and yet others were different. RNA blot analysis indicated that the csp gene was induced by cold shock, i.e., transferring from $30^{\circ}C$ to $10^{\circ}C$, and this cold shock response proposed that the isolated gene be a new type of csp gene.

• Korean Journal of Microbiology
• /
• v.31 no.3
• /
• pp.189-196
• /
• 1993

Nucleotide sequences of nodD and nodA from Bradyrhizobium sp. SNUOOI were determined. The open reading frame (ORF) of nodD was 942 bp in length and encoded 314 amino acids. while ORF of nodA, sequence of which is the first one among legume symbionts Bradyrhizobium, was 630 bp and encoded 210 amino acids. The nucleotide sequence of nodD showed 99.4% homology with nodDI of B. japonicum USDAllO. while that of nodA showed 81.5% with B. sp. (Parasponial. At the 5' of nodYAB operon and nodD, consensus nod box sequences composed of 9 bp unit repeated four times and two times respectively were found. Also an A.T-rich sequence was found at 5' of nodD.

• Korean Journal of Microbiology
• /
• v.35 no.1
• /
• pp.18-24
• /
• 1999

Kinesin has been discovered in Saccharomyces cerevisiae, Aspergillus nidulans, and Drosophila melanogaster and it has major roles in the movemenl of chromosomes and separation of spindle poles. In this study, a gene encoding kinesin heavy chain in Schizosaccharo~n)~ces pombe was cloned by using the polymerase chain reaction with degenerated primcrs corresponding to highly conserved regions of the kinesin heavy chain motor domain. The kinesin gene in S pombe contains an open reading frame of 2496 base pairs and encodes a kinesin prolein of 832 amino acids with a molecular weight of 96 kd. From thc comparison of the predictcd amino acids of the newly cloned kinesin, the kinesin in S. pornbe belongs to the C-terminal motor subfamily of kincsin-related protein.

• Journal of Microbiology and Biotechnology
• /
• v.5 no.3
• /
• pp.125-131
• /
• 1995

A 3, 346 bp of the cdd upstream region in Bacillus subtilis was sequenced from the pSO1 (Song BH and J Neuhard. 1989. Mol. Gen. Genet 216: 462-468) and sequence homology was searched to the known genes in Genbank and European Molecular Biology Laboratory databanks. Five complete and one truncated putative coding sequences deduced from the nucleotide sequence were found through the ORF searching by Genetyx and Macvector software, and one of them was identified as the dgk (diacylglycerol kinase) gene and another, a truncated one, as the phoH (phosphate starvation-inducible gene) gene. The B. subtilis dgk gene, having a role for response to several environmental stress signals, revealed an open reading frame of 134 amino acids with 43.1% of sequence identity to the Streptococcus mutans dgk gene. The carboxy terminal 59 residues of the truncated phoH gene showed 52.7% and 34.5% of sequence identity in amino acids with the corresponding genes of Mycobacterium leprae and Escherichia coli. The four remaining coding sequences consisting of 115, 421, 91, and 91 residues were thought to be unknown ORFs because they have no significant similarity to known genes.

• Journal of the Korean Magnetic Resonance Society
• /
• v.13 no.2
• /
• pp.143-153
• /
• 2009

Luteinizing Hormone Releasing Hormone (LHRH) is composed of 10 amino acids, and is best known as a neurotransmitter. Because of the 80% homology in animals, much more concerns have focused on the substances that have similar functions or can control LHRH. Ni, Cu-LHRH complexes were synthesized. The degree of complexation was monitored by $^1H,\;^{13}C$-NMR chemical shifts, and final products were identified by ESI-Mass spectrum. Solution-state structure determination of Ni-LHRH complex was accomplished by using NMR results and NMR-based distance geometry (DG). Interproton distances from nuclear Overhauser effect spectroscopy (NOESY) were utilized for the molecular structure determination. Results were compared with previous structures obtained from energy minimization and other spectroscopic methods. Structure obtained in this study has a cyclic conformation which is similar to that of energy minimized, and exhibits a specific a-helical turn with residue numbers (2~7) out of 10 amino acids. Comparison of chemical shifts and EPR studies of Ni, Cu-LHRH complexes exhibit that Ni-LHRH complex has same binding sites with the 4-coordination mode as in Zn-LHRH complex.

• Animal cells and systems
• /
• v.2 no.1
• /
• pp.113-116
• /
• 1998

A cDNA clone coding for ribosomal protein 46 (rp46) which is a component of 60S ribosomal large subunit has been identified from Drosophila melanogaster. A cDNA clone encoding S. cerevisiae rp46 was used as a probe to screen a Drosophila larvae cDNA library. The DNA sequence analysis revealed that the cDNA coding for Drosophils rp46 contains a complete reading frame of 153 nucleotides coding for 51 amino acids. The deduced amino acid sequence showed 71-75% homology with those of other eukaryotic organisms. Northern blot analysis showed that about 1-kb rp46 transcripts are abundant throughout fly development. Whole mount embryonic mRNA in situ hybridization also showed no preferential distribution of the transcripts to any specific region. The chromosomal in situ hybridization revealed that the identified gene is localized at position 60C on the right arm of the second polytene chromosome with a possibility of single copy.

• Journal of Plant Biology
• /
• v.37 no.2
• /
• pp.167-173
• /
• 1994

Poly(A)+ RNA was selected from Canavalia lineata root nodule RNA through oligo(dT) cellulose column and used for construction of a cDNA library using λgt10-EcoRI arms. The size of the library was 7.2$\times$105 pfu/mL. A full length leghemoglobin (Lb) cDNA clone, pCILb1(687 bp) isolated with soybean Lb probe, contained one open reading frame (ORF) of 447 bp with 54 bp plus 186 bp at 5' and 3' untranslated region, respectively. A consensus sequence of plant translation start region (AAAATGGG) was found at 5' untranslated region, and two polyadenylation-related sequence (AATAAA, AATAAG) and a conserved motif between them (gACTTGTT) were found upstream of poly(A)+ tail consisted of 13 (A)s at 3' untranslated region. The ORF encoded a polypeptide consisted of 149 amino acids with a molecular weight of 16.2 kD. Deduced amino acid sequences showed high degree of homology values with those of other Lbs ranging from 66% (Casuarina glauca) to 85% (Glycine max).

• Journal of Microbiology and Biotechnology
• /
• v.5 no.5
• /
• pp.250-256
• /
• 1995

The ddh gene encoding meso-diaminopimelate (meso-DAP)-dehydrogenase (DDH) in Brevibacterium lactofermentum was isolated by complementation of the Escherichia coli dapD mutation. It was supposed from subcloning experiments and complementation tests that the evidence for DDH activity appeared in about 2.5 kb Xhol fragmented genome. The 2.5 kb Xhol fragment containing the ddh gene was sequenced, and an open reading frame of 960 bp encoding a polypeptide comprising 320 amino acids was found. Computer analysis indicated that the deduced amino acid of the B. lactofermentum ddh gene showed a high homology with that of the Corynebacterium glutamicum ddh gene.

• Proceedings of the Korean Biophysical Society Conference
• /
• 2002.06b
• /
• pp.32-32
• /
• 2002

To understand the functional roles of the neuron-specific $\beta$-subunit of large-conductance calcium-activated potassium ($BK_{Ca}$) channel, we isolate the full-length complementary DNA of $\beta$4-subunit from rat brain library and investigated its effects on the function of $\alpha$-subunit (Slo). The deduced amino acid sequence of rat $\beta$4 (r$\beta$4), 210 amino acids in length, was closely related to those of $\beta$4 subunits in other mammalian species but showed only a limited sequence homology to the other $\beta$-subunits, $\beta$1 to $\beta$3.(omitted)d)