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Ha, Kwon-Soo,Leem, Sun-Hee,Choi, Jong-Soon,Kim, Seung Il 東亞大學校附設遺傳工學硏究所 1999 遺傳工學硏究 Vol.- No.6
Previously, we have reported that two clustered cat genes from Acenitobacter lwoffii K24 had different arrangements, catB₁C₁A₁ and catB₂A₂C₂ (Kim, S.I., S.-H. Leem, J.-S. Choi,Y.H.Chung, S.Kim,Y.-M.Park, Y.K.Park, Y.N.Lee, and K.-S.Ha.1997,J.Bacteriol.179,5226-5231). By further analysis of the organization of the cat1 gene ciuster, we obtained a complete sequence of the catB₁ gene, which encoded 40.8-kDa polypeptide containing 379 amino acids, and found a open reading frame (ORF) coding a putative regulatory protein in upstream region of catB₁ on plasmid pCD1-1. This ORF encoded 34.2-kDa polypeptide containing 379 amino acids and had more than 40% identity with catR, LysR family regulatory protein of Pseudomonas putida. RT-PCR, Northern blot analysis and primer extension assay for transcriptional analysis of the cat1 gene cluster revealed that the catB₁C₁ genes were cotranscribed and the catA₁ gene was independently transcribed.
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Phospholipase D Is Not Involved in Rho A-Mediated Activation of Stress Fiber Formation
Ha, Kwon-Soo,Kim, Seung-Il,Kim, Jae-Hong,Shin, Incheol,Leem, Sun-Hee,Kweon, Soo-Mi 東亞大學校附設遺傳工學硏究所 1999 遺傳工學硏究 Vol.- No.6
In order to investigate the role of a small GTP-binding protein RhoA in lysophosphatidic acid (LPA)-induced stress fiber formation. C3 ADP-ribosyltransferase was prepared by expressing in E. coli and then applied to Rat-2 fibroblasts. C3 transferase isolated from E.coli was as effective as the toxin from Clostridium botulinum in ADP-ribosylation of RhoA. Incubation of the cells with C3 transferase for 2 days induced ADP-ribosylation of RhoA by a dose-dependent manner, with a sub-maximal induction at 25 ug/ml. As expected, LPA-induced stress fiber formation was completely blocked by pre-incubation with C3 transferase for 2 days. However, exogenously added C3 transferase had no significant effect on the formation of phosphatidylethanol by LPA. These results suggested that phospholipase D was not activated by RhoA in the LPA-induced stress fiber formation.
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Cloning and Characterization of Two catA Genes in Acinetobacter lwoffii K24
CHUNG, YOUNG HO,HA, KWON-SOO,LEE, YUNG NOK,KIM, SEUNG IL,PARK, YOUNG-MOK,KIM, SOOHYUN,CHOI, JONG SOON,LEEM, SUN HEE,PARK, YONG KEUN 東亞大學校附設遺傳工學硏究所 1997 遺傳工學硏究 Vol.- No.6
Two novel type I catechol 1,2-dioxygenases inducible on aniline media were isolated from Acinetobacter lwoffii K24. Although the two purified enzymes, CDI₁and CDI₂, had similar intradiol cleavage activities, they showed different substrate specificities for catechol analogs, physicochemical properties, and amino acid sequences. Two catA genes, catA₁and catA₂, encoding by CDI₁ and CD I₂, respectively, were isolated from the A. lwoffii K24 genomic library by using colony hybridization and PCR. Two DNA fragments containing the catA1 and catA₂ genes were located on separate regions of the chromosome. They contained open reading frames encoding 33.4-and 30.4-kDa proteins. The amino acid sequences of the two proteins matched well with previously determined sequences. Interestingly, further analysis of the two DNA fragments revealed the locations of the catB and catC genes as well. Moreover, the DNA fragment containing catA₁ had a cluster of genes in the order catB₁-catC₁-catA₁ while the catB₂-catA₂-catC₂ arrangement was found in the catA₂ DNA fragment. These results may provide an explanation of the different substrate specificities and physicochemical properties of CDI₁ and CDI₂.
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Proteomic applications of surface plasmon resonancebiosensors: analysis of protein arrays
육종설,하권수 생화학분자생물학회 2005 Experimental and molecular medicine Vol.37 No.1
Proteomics is one of the most important issues in the post-genomic area, because it can greatly contribute to identifying protein biomarkers for disease diagnosis and drug screning. Protein array is a key technology for proteome research-es and has been analyzed by various methods including fluorescence, mass spectrometry, atom-ic force microscopy and surface plasmon re-sonance (SPR). SPR biosensor is a promising technology in proteomics, since it has various advantages including real-time measurement of biomolecular interactions without labeling and the simple optical system for the device. SPR biosensors have a strong potential for analyzing proteomes by SPR imaging and SPR spectro-scopic imaging, even though the challenge is to produce proteins on a proteomic scale.
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