- Factors affecting pheromone induction of schizosaccharomyces pomba and isolation of pheromone induction mutants
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Jun, Jai Hyun , Kim, Young Min , Lee, Joo Hun , Chung, In Kwon , Kim, Dae Myung
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J. Microbiol. 1998;36(3):196-202.
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The mating pheromones of Schizosaccharomyces pombe are induced by nutritional starvation. However, this nutritional signaling pathway is largely unknown. For a complete understanding of pheromone induction, we examined the environmental factors affecting the induction afer cells were transferred to a nitrogen-starved medium. It appeared that the induction of mfm2 transcription was affected by the general environmental stress including incubation time, incubation temperature, and the growth phase of the cells. We identified 7 pheromone induction mutants by screening temperature sensitive mutant bank. Three of these mutants showed elongated cell shapes and one mutant exhibited swollen cell morphology in permissive culture, suggesting that their cell cycles were also impaired. Characterization of the pheromone induction mutants may elucidate the components required in nutritional signaling pathway leading to pheromone induction.
- Effect of Polyamines on Cellular Differintiation of N. gruberi: Inhibition of Translation of Tubulin mRNA
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Yoo, Jin Uk , Kwon, Kyung Soon , Cho, Hyun Il , Kim, Dae Myung , Chung, In Kwon , Kim, Young Min , Lee, Tae HO , Lee, Joo Hun
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J. Microbiol. 1997;35(4):315-322.
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The effects of a polyamine, spermine, on the differentiation of Naegleria gruberi amebas into flagellates were tested. Addition of spermine at early stages of differentiation (until 40 min after the initiation of differentiation) completely inhibited the differentiation. To understand the inhibition mechanism, we examined the effect of spermine treatment on the transcription and translation of differentiation-specific genes during differentiation. Addition of spermine at early stages did not inhibit the accumulation of two differentiation-specific mRNAs, α-tubulin and Class I mRNA, significantly, but rather prevented the rapid degradation of the mRNAs in later overall protein synthesis partially and gradually. However, translation of the α-tubulin mRNA was completely inhibited. These data suggest that the inhibition of differentiation of N. gruberi by spermine treatment did not result from the inhibition of transcription of differentiation-specific genes but from the specific inhibition of translation of the mRNAs during the differentiation.
- Kinetic and spectral investigations on Ca^2+ and Sr^2+ containing methanol dehydrogenases
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Kim, Si Wouk , Kim, Chung, Sung , Lee, Jung Sup , Koh, Moon Joo , Yang, Song Suk , Duine, Johannis A. , Kim, Young Min
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J. Microbiol. 1997;35(3):200-205.
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Both Ca^2+ and Sr^2+ containing methanol dehydrogenases (MDH) were purified to homogeneity with yields of 48% and 42%, respectively, from Methylabacillus methanolovorus sp. strain SK5. Most of the biochemical and structural properties were similar to each other. However, some differences were found: (1) although the overall shape of the absorption spectrum of Sr^2+ MDH was very similar to that of Ca^2+ MDH, the absorption intensity originating from the cofactor in Sr^2+. MDH was higher than that in Ca^2+-MDH. Small blue shift of the maximum was also observed. These are probably due to a difference in redox state of the cofactors in Ca^2+ and Sr^2+ -MDH; (2)Sr^2+ -MDH was more heat-stable than Ca^2+-MDH above 56℃; (3) the V_max values for the methanol-dependent activities of Sr^2+ Ca^2+ -MDH in the presence of 3 mM KCN were 2.038 and 808 nmol/mg protein/min, respectively. In addition, the K_m values of Sr^2+ and Ca^2+ MDH for methanol were 12 and 21 uM, respectively; (4) the endogenous activity of Ca^2+ -MDH was more sensitive than that of Sr^2+ -MDH in the presence of cyanide; (5) Diethyl pyrocarbonate treatment increased the enzyme activities of Ca^2+ and Sr^2+ MDH 4.2 and 1.4 folds, respectively. These results indicate that Sr^2+ stabilizes the structural conformation and enhances the activity of MDH more than Ca^2+.
- Growth on methanol of a carboxydobacterium, acinetobacter sp. strain JC1 DSM 3803
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Ro, Young Tae , Seo, Jae Goo , Lee, Joo Hun , Kim, Dae Myung , Chung, In Kwon , Kim, Tae Ue , Kim, Young Min
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J. Microbiol. 1997;35(1):30-39.
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Acinetobacter sp. strain JC1 DSM 3803, a carboxydobacterium, was found to grow methylotrophically at the expense of methanol and methlamine, but not of methane, formaldehyde, formate, dimethylamine, or trimethylamine, as the sole source of carbon and energy. The doubling times of the bacterium growing on methanol (0.5% v/v) and methylamine (0.5% w/v) at 30℃ and pH 6.8 were 4.8 h and 5.7 h respectively. Cells grown on methanol, however, failed to show typical methanol dehydrogenase and oxidase activities. The cell was found to contain no c-type cytochromes. Cells grown on methanol exhibited higher catalase activity than those grown on pyruvate or glucose. The catalase present in the cells also exhibited peroxidase activity. The catalase activity, growth on methanol of the cell, and oxygen consumption by methanol-grown maldehyde dehydrogenase, formaldehyde reductase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase activities were detected from cells grown on methanol.
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