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REFERENCE LINKING PLATFORM OF KOREA S&T JOURNALS
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The Korean Journal of Microbiology
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Journal DOI :
The Microbiological Society of Korea
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Volume & Issues
Volume 32, Issue 4 - Jan 1994
Volume 32, Issue 3 - Jan 1994
Volume 32, Issue 2 - Jan 1994
Volume 32, Issue 1 - Jan 1994
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Phylogeny of Ganoderma Based on the Restriction Enzyme Analysis of Mitochondrial DNA
Hong, Soon-Gyu ; Jung, Hack-Sung ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 245~251
Ten strains of 7 species from the genus Ganoderma, G. lucidum ATCC 64251, FP-103561-T, and ES70701, G. applanatum ATCC 44053 and FP-57035-T. G. lobatum ATCC 42985, G. resinaceum ATCC 52416, G. subamboinense var. laevisporum ATCC 52420, G. meredithae ATCC 64492, and G. microsporum ATCC 76024, were studied to discuss their phylogenetic relationships by utilizing restriction fragment length polymorphisms (RFLPs) of mitochondrial DNAs (mtDNAs). Six restriction enzymes, BamHI, BglII, EcoRI, HindIII, PvuII, and XbaI which digested mtDNAs into adequate numbers of restriction fragments for cluster analysis, were used in this study. Restriction profiles of strains for each restriction enzyme were treated as analysis characters to calculate similarity coefficients, which were converted into nucleotide sequence divergence values whose mean values were then arranged in a matrix table. This table was utilized for a phylogenetic analysis using the Neighborjoining method of the PHYLIP package to construct phylogenetic tree. Three strains of G. lucidum and two strains of G. applanatum exhibited different lineages each but one of G. applanatum strains showed a close relationship with G. lobatum, which reflected the species complexity of these species whose strains were phenotypically indistinguishable but genetically distinct. The present results suggest that the natural classification of Ganoderma needs to be considered from the viewpoints of molecular biology-based systematics as well as morphological classifications and cultural identifications for better phylogenetic conclusions.
Isolation and Characterization of a New Hydrogen Sulfide-Oxidizing Bacterium Thiobacillus Sp.
Cha, Jin-Myeong ; Lee, In-Hwa ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 252~257
A new hydrogen sulfide-oxidation bacterium, Thiobacillus sp. was isolated from waste coal mine water around Hawsun in Chunnam province. The isolate was motile gram-negative rod shape, formed spore and grew up to be aerobically facultative chemolithotroph by using energy released from the oxidation of reduced inorganic sulfur compounds. It could assimilate various kinds of organic compounds and grew well upon thiosulfate-supplemented basal medium. To the lelvel of 32 mM in thiosulfate concentration, thiosulfate in itself was utilized as energy source for growth. However, from those of the higher concentration than 32 mM, thiosulfate functioned specifically as the substrate inhibitor rather than as the energy source. It was found that the optimum thiosulfate concentration for growth was 32 mM. The G+C content of the DNA was 65.0 mol%. The isolate had 16 : 1 + 17
, 16 : 0 as their major non-hydroxylated cellular fatty acids, 3-OH 12 : 0 as a hydroxylated fatty acid and also contained unidentified
branched fatty acid. The ubiquinone system in the respiratory chain was Q-9. Based on the physiological and biochemical characteristics, the isolate was assigned to a novel species of the genus Thiobacillus sp. iw.
Molecular Cloning of nifH, D from Frankia EuIK1 Strain, A Symbiont of Elaeagnus umbellata Root Nodules
Kim, Ho-Bang ; Kim, Chun-Ho ; Song, Seun-Dal ; An, Chung-Sun ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 258~263
Genomic Southern hybridization of Frankia EuIKl strain, a nitrogen fixing symbiont of Elaeagnus umbellate root nodules, with nifH,D of K. pneumoniae as a probe, showed that 3.2 Kb and 5.5 Kb of BamHI fragments and 15 Kb PstI fragment were strongly hybridized with the probe, indicating nifH,D are located on these fragments. Using the same probe, one clone(pEuNIF) was isolated from the genomic library constructed into pWE15 cosmid vector by colony hybridization. The 3.2 Kb and 5.5 Kb BamHI fragments of this clone were hybridized with the same probe and this result corresponds to the genomic Southern hybridization data. However, using nifH of Frankia FaCl strain as a probe, only the 3.2 Kb BamHI fragment showed hybridization signal. Amino acid sequence deduced from nucleotide sequence of 3' terminus of the 3.2 Kb and 5' terminus of the 5.5 Kb fragments showed that the former was highly homologous with that of ArI3 nifD from 182nd to 240th amino acids, while the latter was from 241st to 282nd amino acids. These results show that nifH and partial nifD sequences are located on the 3.2 Kb fragment and residual sequences of nifH on the 5.5 Kb fragment which is contiguous to the 3.2 Kb fragment.
Cloning of hadA-like Sigma Factor Gene from Streptomyces coelicolor A3(2)
Hahn, Ji-Sook ; Cho, Eun-Jung ; Roe, Jung-Hye ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 264~270
A gene coding for a novel putative
factor of RNA polymerase has been identified from Streptomyces coelicolor A3(2) using Escherichia coli rpoS gene fragment as a probe. The 486 bp rpoS gene fragment was amplified from E. coli genomic DNA by PCR with two synthetic oligonucleotides, the sequences of which were deduced from the amino acid sequences in the regions 2.3 and 4.2 conserved among various bacterial factors. When E. coli genomic DNA fragments were hybridized with cloned rpoS probe, only one band corresponding to rpoS gene (3.2 kb PvuII fragment or 2.3 kb KpnI fragment) was detected. In S. coelicolor, however, two bands were detected both in PvuII digested DNA and SalI digested DNA. 3.5 kb PvuII fragment which binds the rpoS gene probe was cloned (pMS1) from the sublibrary, and the nucleotide sequences of 1.0 kb BamH'/HincII subclone (pBH2) was partially determined. The nucleotide sequences revealed extensive similarity to other
factor genes of S. coelicolor (hrdA, hrdB, hrdC, hrdD), S. aureofaciens (hrdA, hrdB, hrdC, hrdD), Synechococcus species, Pseudomonas aeruginosa, Stigmatella aurantiaca, and Anabaena species. The nucleotide sequences in regions 1.2 and 4 were compared with the corresponding regions of 5 known
factor genes of S. coelicolor by multiple alignment. It turned out that the cloned gene is most closely related to hrdA showing 88% amino acid similarity in region 1.2 and 75% in region 4.
Mitotic Stability of Heterologous
-Amylase Gene in Starch-Fermenting Yeast
Kim, Jung-Hee ; Kim, Keun ; Choi, Yong-Keel ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 271~279
To develop a yeast strain which stably secretes both
-amylase and glucoamylase and therefore is able to convert starch directly to ethanol, a mouse salivary
-amylase cDNA gene with a yeast alcohol dehydrogenase I promoter has been introduced into the cell of a Saccharomyces diactaticus hybrid strain secreting only glucoamylase. To secrete both enzymes more stably without loss of the
-amylase gene during a cell-multiplication, an integrating plasmid vector containing
-amylase gene was constructed and introduced into the yeast cell. The results showed that the linearized form of the integrating vector was superior in the transformation efficiency and the rate of the expression of the
-amylase gene than the circular type of the vector. The yeast transformant having a linearized plasmid vector exhibited higher mitotic stability than the yeast transformant habouring episomat plasmid vector. The transformant containing the linearized vector producing both
-amylase and glucoamylase exhibited 2-3 times more amylolytic activity than the original untransformed strain secreting only glucoamylase.
A possible role of lipopolysaccharides in the prevention of lysosome0symbiosome fusion as studied by microinjection of an anti-LPS monoclonal antibody
Choi, Eui-Yul ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 280~284
Lack of lysosomal fusion with symbiosomes in symbiont-bearing Amoeba proteus may be due either to the presence of a component in the symbiosome membrane or to the absence of a component needed in the fusion process. Using monoclonal antibody as a probe, lipopolysaccharides were identified as symbiosome-membrane components contributed by symbionts and were found to be exposed on the cytoplasmic side of the membrane. In order to test whether lipopolysaccharides may play a role in the prevention of lysosome-symbiosome fusion, the antilipopolysaccharides antibody was microinjected and processed for double immunostaining in conjuction with anti-lysosome antibody as a lysosome-fusion indicator. Microinjection of the anti-LPS antibody caused symbiosomes to fuse with lysosomes, suggesting that X-bacterial lipopolysaccharides could be 'fusion-preventing' factors.
Characterization of a Restriction Endonuclease AspJI from Alcaligenes sp. J-482
Lee, Jeong-Taek ; ; Lim, Jai-Yun ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 285~290
About 500 bacterial and fungal strains from a wide variety of natural habitats were screened for a new type II restriction endonuclease. Among the 500 species, we selected one species that produced a new restriction endonuclease. This strain has an optimum temperature of
for growth. Morphological, cultural, and physiological characteristics were examined for identification of the isolated strain J-482. This strain was found to belong to the genus Alcaligenes. The restriction endonuclease was named as AspJI and partially purified from Alcaligenes sp. J-482 by DEAE-Sephadex A-50 column chromatography and gel filtration. Most of other nucleases were removed by the purification steps. The AspJI has a substrate specificity to
DNA, pBR322 and Adenovirus-2 DNA. For its maximal activity, the isolated enzyme requires
, which should be at least 12.5 mM and it does not need any other cofactors. It is maximally active in the absence of NaCl and is completely inactivated at 100 mM NaCl. The pH and temperature optima for activity were pH 7.5 and
, respectively. The DNA fragments generated by digesting
DNA, pBR322, and Adenovirus-2 DNA with AspJI were the same as that produced by AatII. This suggests that AspJI is an isoschizomer of AatII.
Properties of Protease from Aeromonas hydrophila AM-28 Isolated from Soil
Kim, In-Sook ; Kim, Hyung-Kwoun ; Lee, Jung-Kee ; Bae, Kyung-Sook ; Oh, Tae-Kwang ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 291~296
A bacterial strain NO. AM-28, showing proteolytic activity against defatted soybean was isolated from domestic soil. The isolated strain was identified as Aeromonas hydrophila by both the biochemical tests using API kit and the analysis of cellular fatty acid profile with MIDI system. The protease production from A. hydrophila AM-28 was highly enhanced when it was cultivated in the medium containing glycerol as a carbon source, tryptone or
as a nitrogen source, and
as a mineral source. The optimal pH and temperature for the enzyme was 8.0 and
, respectively. The enzyme was stable up to
and at pH values ranging from 7.0 to 13.0. The enzyme activity was inhibited by phenylmethylsulfonyl fluoride and EDTA, indicating that serine residue and metal ions be involved in enzyme activity.
Purification of Festriction Endonuclease,SdiI, from Streptomyces diastatochromogenes
Bae, Mu ; Song, Eun-Suk ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 297~300
About thirty bacterial strains of actinomycete isolated from the soil were examined for the presence of restriction endonuclease activity. Streptomyces diastatochromogenes, which was identified previously, was found to contain restriction endonuclease activity. The purification of this enzyme, SdiI, was carried out via streptomycin sulfate precipitation and ammonium sulfate fractionation followed by hydroxylapatite column chromatography. Sephacryl S-200 HR column chromatography and second hydroxylapatite column chromatography. SDS-polyacrylamide gel electrophoresis of the active protein (purified from various column chromatography) resulted in 35,000 Da protein.
Characterization of a Restriction Endonuclease, SdiI from Streptomyces diastatochromogenes
Bae, Moo ; Song, Eun-Sook ; Hwang, Hye-Yeon ; Yim, Jeong-Bin ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 301~305
In catalytic properties of the restriction enonuclease, SdiI, which was purified from Streptomyces diastatochromogenes, this enzyme was active at wide range between pH 7.0 and 12.5, and up to
and 500 mM of NaCl concentration. It was stable between
, and essentially requires
for endonuclease activity. The restriction map of lambda DNA which was obtained by double digestion with various enzymes suggested SdiI to be an isoschizomer of XhoI. From the determination of restriction site based on DNA sequencing method, recognition and cleavage specificity of SdiI was concluded as: 5‘-C
TCGA G-3' 3'-G AGCT
Mode of action anf active site of xylanase II from Trichoderma koningii ATCC 26113
Kim, Hyun-Ju ; Kang, Sa-Ouk ; Hah, Yung-Chil ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 306~314
The action mode of xylanase II from Trichoderma koningii ATCC 26113 on xylan and related oligosaccharides (xylotriose, xylotetraose, and arabinoxylotriose) indicated that xylanase II is an endo-enzyme and also has trans-xylosidase activity. The
-NMR studies of the reaction products formed by xylanase II revealed that all the hydrolysis products of xylooligosaccharides by the enzyme have only
-1,4-xylosidic linkage(s). Chemical modification of the enzyme with iodoacetamide showed that two cysteine residues per molecule of the enzyme was essential for the activity. Modification of the enzyme with N-bromosuccinimide demonstrated that four of the eight tryptophan residues were involved in its active site.
Purification and Characterization of Glyoxalase I from Pleurotus ostreatus
Kim, Seong-Tae ; Yang, Kap-Seok ; Seok, Yeong-Jae ; Huh, Won-Ki ; Kang, Sa-Ouk ;
The Korean Journal of Microbiology, volume 32, issue 4, 1994, Pages 315~321
Glyoxalase I was purified 2,294-fold from Pleurotus ostreatus by S-hexylglutathione affinity chromatography, Sephadex G-150 gel filtration chromatography and DEAE-sepharose A-50 CL-6B ion exchange chromatography with an overall yield of 21.7%. The molecular mass determined by gel filtration was found to be approx. 34 kDa. SDS-PAGE revealed that the enzyme consists of two identical subunits with a molecular mass of approx. 17 kDa. The K sub(m) values of this enzyme for methylglyoxal and phenylglyoxal were 0.39 mM and 0.22 mM, respectively. And this enzyme had a strong affinity for L-xylosone and hydroxypyruvaldehyde. The enzyme showed its optimal activity at pH 6.5-7.5 and at
-NMR spectroscopic analysis of enzymic reaction showed that this enzyme catalyzes intramolecular proton transfer.