- Physiological Relevance of Salt Environment for in vitro recA System
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Kim , Jong Il
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J. Microbiol. 1999;37(2):59-65.
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RecA protein can promote strand assimilation, homologous pairing, and strand exchange. All these reactions require DNA-dependent ATP hydrolysis by recA protein, and the activities of recA protein are affected by the ionic environment. In this experiment, DNA-dependent ATPase activity showed different sensitivity to anionic species. ATP hydrolysis and strand exchange were relatively sensitive to salt in the reactions with NaCl, strongly inhibited at 100 mM NaCl. However, the inhibition by sodium acetate or sodium glutamate was not observed at 50∼100 mM concentration. Addition of sodium glutamate to the standard reaction condition increased the apparent efficiency of ATP hydrolysis during strand exchange. The condition including 50∼100 mM sodium-glutamate might be similar to the physiological condition.
- The Schizosaccharomyces pombe Proteins that Bind to the Human HnRNPA1 Winner RNA
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Kim , Jeong Kook
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J. Microbiol. 1997;35(4):327-333.
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Although extensively characterized in human cells, no heterogeneous nuclear ribonucleoprotein(hnRNP) has been found in the fission yeast Schizosaccharomyces pombe which is amenable to genetic studies and more similar to mammals than Saccharomyces cerevisiae is in terms of RNA processing. As a first step to characterize hnRNPs from S. pombe, attempt was made to find human hnRNP A1 homologs from S. pombe. The RNA molecule (A1 winner) containing the consensus high-affinity hnRNP A1 binding site (UAGGGA/U) was synthesized in vitro and used in an ultraviolet(UV) light-induced protein-RNA cross-linking assay. A number of S, pombe proteins bound to the A1 winner RNA. An approximately 50-kDa protein(p50) cross-linked more efficiently to the A1 winner RNA than other proteins. The p50 protein did not cross-link to a nonspecific RNA, but rather to the A1-5’ SS RNA in which the consensus 5’ splice junction sites of S. pombe introns were abolished. This suggests that the p50 protein, however, did not bind to the single-stranded DNA to shich the human hnRNP A1 could bind and be eluted with 0.5M NaCl. Further analysis should reveal more features of this RNA-binding protein.
- Immunofluorescence localization of schizosacharomjyces pombe cdc103^+ gene product
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Kim , Hyong Bai
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J. Microbiol. 1996;34(3):248-254.
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Abstract
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cdc103^+ gene in Schizosaccharomyces pombe which is similar to the CDC3 gene in Saccharomyces cerevisiae was cloned and sequenced. Comparison of the predicted amino acid sequences of cdc103^+ and CDC3 revealed that they share significant similarity (43% identity and 56% identity or similarity) to each other. The gene product of CDC3 S. cerevisiae is known to be a highly ordered ring of filaments that lies just inside the cytoplasmic membrane in the region of the mother-bud neck. In order to characterize the gene product of cdc103^+ in Schizosaccharomyces pombe, fusion proteins were used to generate the polyclonal antibodies specific for the gene product (cdc103p). In immunofluorescence experiments, these antibodies decorate the region of the septum formation as a double ring structure late in the cell division cycle.
- Adsorption of Pb^2+ in the components of bacterial cell membrane
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Kim , Mal Nam
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J. Microbiol. 1995;33(4):278-282.
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S. epidermidis cell was fractionated into cell wall, cell membrane and cytoplasm. The cell membrane adsorbed the most abundant Pb^2+ per unit dry weight of the three fractions tested. Adsorption behavior of Pb^2+ in lipid and protein, which are the main components of the cell membrane, indicated that phosphatidylethanolamine and phosphatidylinositol having phosphoryl group and gangliosides containing carboxyl groups adsorbed much more Pb^2+ than triglycerides lacking any chargeable functional groups. Protein purified from cell membrane adsorbed larger amount of Pb^2+ than total native cell membrane or cell membrane lipid.
- Sequence analysis of the schizosaccharomycs pombe homologue of the CDC3 gene in saccharomyces cerevisiae
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Kim , Hyong Bai
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J. Microbiol. 1995;33(4):350-354.
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Saccharomyces cervisiae has a highly ordered ring of filaments that lies just inside the cytoplasmic membrane in the region of the mother-bud neck. Mutants defective in any one of the our cell division cycle genes (CDC3, CDC10, CDC11, CDC12) fail to form these filaments and exhibit a pleiotropic phenotype that includes failure to complete cytokinesis and abnormal bud growth. However, the role of the filament is not clear. In order to find out the role of filament, the similar gene in S pombe (called cdc103^+) to the CDC3 was cloned and sequenced. Here I report the sequence analysis of the cdc103^+) to the CDC3 was cloned and sequenced. Here I report the sequence analysis of the cdc103^+. Comparison of the predicted amino acid sequences of cdc103^+ and CDC3 revealed that they share significant similarity (43% identity and 56% identity or similarity) to each other.
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