• BMB Reports
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• v.38 no.2
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• pp.206-210
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• 2005

Gonadogenesis is a complicated process which involves multi-gene interactions. A rainbow trout (Oncorhynchus mykiss) gene spermatogenesis associated 4 (SPATA4) was cloned and characterized from adult rainbow trout testis. The cDNA sequence of rainbow trout SPATA4 contains an open reading frame of 1, 081 nucleatides encoding a putative protein of 259 amino acids. The putative protein from rainbow trout shares a 76.8% homology with zebrafish SPATA4. No trans-membrane regions or signal peptide were detected using bioinformatics methods. Subcellular localization analysis revealed that rainbow trout SPATA4 was a nuclear protein with highest possibility (39.1%). Multi-tissue reverse transcriptase PCR (RT-PCR) was performed to examine the distribution of rainbow trout SPATA4 in eleven organs of adult rainbow trout. The result demonstrated that this gene express specifically in testis and slight amount of expression was detected in ovary. Further analysis of SPATA4 characterization and function in rainbow trout may provide insight into the understanding of gonadogenesis process.

• Applied Biological Chemistry
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• v.32 no.1
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• pp.64-72
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• 1989

Near full length cDNA clones encoding the rice seed storage protein, prolamine, were isolated and divided into two homology classes based on cross-hybridization and DNA sequencing analysis. These cDNA clones contain a single open reading frame encoding a putative rice prolamine precursor(M.W.=17,200) possessing atypical 14 amino acid signal peptide. Clones of these two homology classes diverge mainly by insertions/deletions of short nucleotide stretches and point mutations. The deduced primary structures of both types of prolamine polypeptides are devoid of any major tandem repetitive sequences, a feature prevalent in other cereal prolamines. No significant homology teas detected between the rice prolamine and other cereal prolamines, indicating that the rice gene evolved from a different ancestor that gave rise to other cereal prolamine genes. Developing wheat and rice endosperms were examined using ultrathin sections prepared from tissues harvested at various days after flowering. By immunocytochemical localization techniques, wheat prolamines are localized within vesicles from Golgi apparatus and in homogeneous regions of protein bodies. The involvement of the goli apparatus in the packaging of wheat prolamines into protein bodies indicates a pathway which differs from the mode of other cereal prolamines and resembles the mechanism employed for the storage of rice glutelin and legume globulins.

• International Journal of Industrial Entomology and Biomaterials
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• v.21 no.1
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• pp.127-132
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• 2010

We have characterized full-length cDNA encoding Gall-6-tox protein, which was cloned from the fat body of the immunized Galleria mellonella larvae. The cloned cDNA of Gall-6-tox consists of 1301 nucleotides and contained an open reading frame of 891 nucleotides corresponding to a protein of 296 residues that includes a putative 16-residue signal sequence and a 280-residue mature peptide with a calculated mass of 30,707.73 Da. The deduced mature peptide contains conserved tandem repeats of six cysteine-stabilized alpha beta ($Cs{\alpha}{\beta}$) motifs, which was detected in scorpion toxins and insect defensins. In the sequence homology search, mature Gall-6-tox showed 34% and 28% amino acid sequence homology with Bomb-6-tox from Bombyx mori and Spod-11-tox from Spodoptera frugiperda, respectively. Gall-6-tox orthologs were only found in Lepidopteran species, indicating that this new immune-related gene family is specific to this insect order. RT-PCR analysis revealed that Gall-6-tox was expressed primarily in the larval fat bodies, hemocytes, and midgut against invading bacteria into hemocoel. Moreover, the expression time course of Gall-6-tox was examined up to 24 h in the fat bodies and midgut after injection of E. coli. Altogether, these results suggest that Gall-6-tox is derived from defensins and Gall-6-tox may play a critical role in Lepidoptera immune system.

• Journal of Microbiology and Biotechnology
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• v.3 no.3
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• pp.139-145
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• 1993

The nucleotide sequence of the xylanase gene (xynS) from alkali-tolerant Bacillus sp. YA.14 was determined and analyzed. A 639 base pairs open reading frame for xynS gene was observed and encoded for a protein of 213 amino acids with a molecular weight of 23, 339. S1 nuclease mapping showed that the transcription initiation site of the xynS gene did not exist in the cloned DNA. Ribosome binding site sequence with the free energy of -18.8 Kcal/mol was observed 8 base pairs upstream from the initiation codon, ATG. The proposed signal sequence consisted of 28 amino acids, of which 3 were basic amino acid residues and 21 were hydrophobic amino acid residues. When the amino acid sequences of xylanases were compared, Bacillus sp. YA-14 xylanase showed 48% homology with Bacillus sp. YC-335 xylanase and 96% homology with xylanases from B. subtilis and B. circulans.

• Journal of rehabilitation welfare engineering & assistive technology
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• v.5 no.1
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• pp.111-115
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• 2011

In this paper, we present a novel time-synchronization method for distributed systems to measure the body motion. The distributed system scheme is considered because human data acquisition systems tend to have a centralized controller with sensors connected with a long range of electric wires running through the subject's body, which results in inconvenience. Utilizing simple key switches and digital input ports for reading the key, the proposed method requires a very simple hardware structure, which means less power consumption compared with the well-known ubiquitous sensor network. After measuring the motion data as well as the synchronization pulses, the proposed method compensates, in offline, the difference of the sampling instance between the two systems by scaling the time difference. The paper presents experimental results to show the validity of the proposed method.

• The Plant Pathology Journal
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• v.16 no.1
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• pp.9-18
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• 2000

Using differential display techniques, a new acidic pathogenesis-related (PR) protein-1 cDNA (GMPRla) gene was isolated from a cDNA library of soybean (Glycinemax L.Merr, cultivar Jangyup) hypocotyls infected by Phytophthora sojae f. sp. glycines. The 741 bp of fulllength GMPRla clone contains an open reading frame of 525 nucleotides encoding 174 amino acid residues (pI 4.23) with a putative signal peptide of 27 amino acids in the N-terminus. Predicted molecular weight of the protein is 18,767 Da. The deduced amino acid sequence of GMPRla has a high level of identity with PR-1 proteins from Brassica napus, Nicotiana tabacum, and Sambucus nigra. The GMPRla mRNA was more strongly expressed in the incompatible than the compatible interaction. The transcript accumulation was induced in the soybbean hypocotyls by treatment with ethephon or DL-$\beta$-amino-n-butyric acid, but not by wounding. In situ hybridization data showed that GMPRIa mRNAs were usually localized in the vascular bundle of hypocotyl tissues, especially phloem tissue. Differences between compatible and incompatible interactions in the timing of GMPRla mRNA accumulation were remarkable, but the spatial distribution of GMPRla mRNA was similar in both interactions. However, more GMPRla mRNA was accumulated in soybean hypocotyls at 6 and 24 h after inoculation.

• Fisheries and Aquatic Sciences
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• v.6 no.3
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• pp.116-124
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• 2003

Isolation and cloning of seven-band grouper (Epinephelus septemfasciatus) growth hormone cDNA from pituitary gland revealed an open reading frame of 612 bp coding for a pre-growth hormone of 204 amino acids with a 17 amino acid putative signal peptide. Deduced amino acid sequence showed that there was one possible N-glycosylation site at $Asn^{l84}$ and four cysteine residues $(Cys^{52},\;Cys^{160},\;Cys^{177},\;Cys^{185})$ on t e same positions as in some other species where they were involved in the stabilization of the tertiary structure. The seven-band grouper growth hormone (sbgGH) presented a $99.5\%$ amino acid sequence identity with the growth hormone of Epinephelus coioides and contained the conserved hormone domain region. Comparison of growth hormone sequences from evolutionarily diverse species revealed 25 amino acid residues conserved in jawless fishes to modern mammals. It also revealed an evolutionary trend to retain the same polypeptide sequence even in the distantly related animals while allowing alterations to occur in polypeptides of the closely related species. In order to create a recombinant system to produce high levels of the growth hormone, it was expressed in Escherichia coli (BL21) cells. The gel analysis revealed theoretically expected molecular weights for both mature and pre-sbgGHs.

• Asian-Australasian Journal of Animal Sciences
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• v.26 no.8
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• pp.1057-1064
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• 2013

p70 ribosomal S6 kinase (p70S6K) can integrate nutrient and growth factor signals to promote cell growth and survival. We report our molecular characterization of the complementary DNA (cDNA) that encodes the goat p70S6K gene 40S ribosomal S6 kinase 1 (S6K1) (GenBank accession GU144017) and its 3' noncoding sequence in Inner Mongolia Cashmere goats (Capra hircus). Goat S6K1 cDNA was 2,272 bp and include an open reading frame (ORF) of 1,578 bp, corresponding to a polypeptide of 525 amino acids, and a 694-residue 3' noncoding sequence with a polyadenylation signal at nucleotides 2,218 to 2,223. The relative abundance of S6K1 mRNA was measured by real-time PCR in 6 tissues, and p70S6K expression was examined by immunohistochemistry in heart and testis. The phosphorylation of p70S6K is regulated by mitogen-activated protein kinase (MAPK) signaling in fetal fibroblasts.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.655-659
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• 2000

A 11.5-kb DNA fragment containing an endo-inulinase gene was cloned from Xanthomonas oryzae #5. It contained a single open reading frame of 3,999bp, encoding a polypeptide composed of signal peptide of 32 amino acids and mature protein of 1,301 amino acids. From the comparison of amino acids sequences with fructan hydrolases, inulinase, levanase and CFTase, the sequence of the endo-inulinase had highly homology of 72% with CFTase of B. circulans, and six highly conserved regions including the ${\beta}-fructosidase$ motif were found.

• Journal of Microbiology and Biotechnology
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• v.3 no.4
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• pp.224-231
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• 1993

The nucleotide sequence of the xylanase gene (xynY) from alkalophilic Bacillus sp. YC-335 was determined and analyzed. An open reading frame of 1, 062 base pairs for xynY gene was observed and encoded for a protein of 354 amino acids with a molecular weight of 38, 915. S1 nuclease mapping showed that the transcription initiation sites of the xynY gene were different in Bacillus sp. YC-335 and Escherichia coli HB101 (pYS55). S1 mapping also showed that -10 region of the xynY gene recognized by RNA polymerases of E. coli and Bacillus sp. YC-335 were TACAGT and TATGAT , respectively. A ribosome binding site sequence with the free energy of -17.0 Kcal/mol was observed 9 base pairs upstream from the unusual initiation codon, TTG. The proposed signal sequence consisted of 27 amino acids, 2 of which were basic amino acid residues and 21 were hydrophobic amino acid residues. When the amino acid sequences of xylanases were compared, Bacillus sp. YC-335 xylanase showed more than 50% homology with xylanases from B. pumilus, B. subtilis, and B. circulans.