• Korean Journal of Microbiology
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• v.24 no.4
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• pp.394-399
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• 1986

From the lysates of the 7 selected strains of Pseulomonas utilizing 2-methyl-4-chlorophenoxyactate as a sole source of carbon and energy, several MCPA plasmids, which encodes genes for the degradation of 2-methyl-4-chlorophenoxyacetate, were isolated, and measured their molecular weight as well as genetic characters such as resistance to antibiotics and degradative ability of other chlorinated herbicides. Transmissibility of the MCPA plasmids, pKU1, pKU15, and pKU17 was tested by conjugation or transformation and the restriction pattern of pKU15 for Pvu II, Hind III, EcoR I, Xho I, Bgl II, and Ava II was analyzed.

• Korean Journal Plant Pathology
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• v.12 no.2
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• pp.156-161
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• 1996

세계적으로 구리약제에 대해서 저항성을 나타내는 균주들이 발견되있으며, 이들은 구리약제의 방제효과를 감소시켰다. 국내에서도, 구리 저항성 균주 Xanthomonas campestris. pv. vesicatoria HN94-2, -3, -4, -5, -6 들이 천안지역의 고추재배지에서 처음으로 분리되었으며, 이들 균주들의 nutrient agar에서 황산구리(CuSo\ulcorner)에 대한 최소억제농도(minimum inhibitory concentration, MIC)는 1.4~1.6 mM이었다. 이들은 모두 황산아연(ZnSO\ulcorner)에 대해서는 감수성을 보여, 구리저항성 균주에 대한 방제약제로서 아연 함유 약제를 사용할 수 있을 것이다. 분리된 균주중 HN94-2와 HN94-6을 이용하여 접합(conjugation)을 통해 구리저항성의 전파를 실험한 결과, 이들 두 균주 모두 구리감수성 균주에게 4.3$\times$10\ulcorner에서 1.0$\times$10\ulcorner(transconjugant/donor)의 정도로 구리 저항성이 전이되었다. 이들 HN94-2와 HN94-6 균주의 구리정항성 유전자들은 약 200 kb 정도의 커다란 플라스미드(plasmid)에 존재하며, 이들은 각각 pXVK9402와 pXVK9406이라 명명되었다.

• Journal of Life Science
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• v.13 no.5
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• pp.712-717
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• 2003

In order to establish yeast cells that produce leucocin A, a bacteriocin, the 117 bp leucocin A gene with start and stop codons was synthesized and cloned in pAUR123, a yeast vector. Transformed yeast cells showed antibacterial activity against Bacillus subtilis. The leucocin A gene was confirmed by means of PCR methods with plasmid prepared from transformed yeast cells as template and two leucocin A-specific primers. In this results, yeast cells that produce mass amounts of bacteriocin to use as food preservative or antibiotics were established.

• YAKHAK HOEJI
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• v.36 no.3
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• pp.255-258
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• 1992

The clinical isolate Staphylococcus aureus SA8 was resistant to tetracycline(Tc) and harboured a plasmid pKH1(24.82 kb). pKH1 was shown by curing and by transformation to specify resistance to Tc. The cleavage map of a pKH1 was determined by restricction enzyme mapping techniques. Cleavage map is given for BglII, EcoRI, HpaII, PvuII and SalI. Restriction endonuclease BamHI, BglI, BstEII, HpaI, PstI, and XhoI have no sites on this plasmid. HaeIII, XbaI, and HindIII have 5, 6, 14 sites, respectively.

• The Journal of Natural Sciences
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• v.15 no.1
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• pp.89-95
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• 2005

JSRV, which causes sheep lung cancer, is known to have the transforming activity of NIH3T3 cells. Especially Envelope protein of this virus has the transforming activity to NIH3T3. To know the effects on the transcriptional activity of transcription factors by this viral protein transient transfection was performed by using the luciferase reporter system. The result showed that JSRV Envelope protein increased the transcriptional activity of NF-kB and AP-1.

• YAKHAK HOEJI
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• v.37 no.6
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• pp.621-624
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• 1993

The clirical isolate Staphylococcus aureus SA2 had four kinds of plasmids and was resistant to ampicillin, chloroamphenicol, clindamycin. erythromycin, gentamicin, kanamycin, methicillin, streptomycin, tetracycline and tobramycin. Transformation experiment demonstrated that 4.14kb plasmid(pKH7) encoded resistance to chloramphenicol. The cleavage map of pKH7 was determined by restriction enzyme mapping techniques. The cleavage map is given for BstEll, Hindlll, Hpall, and Xbal. The above restriction endonucleases have a single site, but nucleases BamHl, Bgll, BglII, EcoRl, EcoRV, HaeIII, Hpal, Kpnl, Pstl, PvnII, Sall, Smal, and XhoI have no site on this plasmid.

• Microbiology and Biotechnology Letters
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• v.24 no.4
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• pp.423-426
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• 1996

The complete nucleotide sequence of pKH6, a tetracycline-resistance (Tc$^{r}$) plasmid isolated from multi-drug resistant Staphylococcus aureus SA2, has been determined and compared with that of the staphylococcal Tc$^{r}$ plasmid pTl8l. The nucleotide sequences of the two plasmids are in agreement except for 7 nucleotides. All differences are caused by base pair substitutions. Among 6 substitutions, 3 occurred in coding regions. However, only two base substitutions in coding regions resulted in changes of amino acid sequences in two different ORFs of repC and Pre proteins.

• YAKHAK HOEJI
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• v.36 no.5
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• pp.486-490
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• 1992

The clinical isolate Staphylococcus aureus SA2 was resistant to ampicillin, Chloramphenicol, clindamycin, erythromycin, gentamicin, kanamycin, methicillin, streptomycin, and tobramycin and harboured more than two kinds of plasmids. Transformation experiment demonstrated that 40.98-kb plasmid(pKH2) encoded resistance to ampicillin, clindamycin, erythromycin, kanamycin, and streptomycin. The cleavage map of a pKH2 was determined by restriction enzyme mapping techniques. Cleavage map is given for BamHI, BglI, BstEII, SalI and XhoI.

• YAKHAK HOEJI
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• v.52 no.2
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• pp.147-150
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• 2008

Previously, we reported on the antibiotic resistance patterns of 50 strains of Staphylococcus aureus which were isolated from a hospital in Busan, Korea from July 2005 to December 2006. We have isolated small plasmids and classified plasmid types by agarose gel electrophoresis. We have selected 5 plasmids and determined complete nucleotide sequences of those plasmids. The aim of this paper is to report on the characteristics of cadmium, erythromycin, lincomycin resistance plasmids and a cryptic plasmid based on the sequence analysis obtained by using the BLAST program.

• YAKHAK HOEJI
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• v.39 no.6
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• pp.676-680
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• 1995

The nucleotide sequence of Xbal-Mbol fragment of pKH7, a chloramphenicol-resistant($Cm^{r}$) plasmid isolated from multidrug-resistant S. aureus SA2, has been determined. Xbal-Mbol fragment of pKH7 was found to contain two ORFs. One ORF encoded Rap and the other encoded CAT protein. The deduced amino acid sequences of Rep and CAT of pKH7 were compared to those of pUB112 and pC221. Comparisons revealed that there was one amino acid difference in CAT between pKH7 and pUB112. CAT of pKH7 exhibited 98.6% amino acid identity to that of pC221. In case of Rep proteins, a slightly lower homology of 96.4% and 86.7% in amino acid sequences was observed between pKH7 and pUB112 and between pKH7 and pC221, respectively.