• KSBB Journal
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• v.13 no.1
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• pp.6-12
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• 1998

In order to produce xylitol from hemicellulose hydrolysate which is widely used as a substrate, the development of strain such as catabolite derepressed mutant is required. After treatment of Candida sp. with EMS, GM-17 and PM-34 as catabolite derepressed mutant were isolated from Candida guilliermondii and Candida parapsilosis, respectively. Mutant GM-17 and PM-34 simultaneously assimilated xylose and glucose during the fermentation. The specific xylose reductase and xylitol dehydrogenase activities of mutant strains were also higher than those of wild strains in glucose medium and mixed medium of glucose and xylose. The xylitol productivity and yield of mutant GM-17 and PM-34 were improved as compared to the wild types in the mixed medium. The xylitol productivity and yield of mutant GM-17 were 0.09 g/L·hr and 0.56 g-xylitol/g-xylose, and those of mutant PM-34 were 0.21 g/L·hr and 0.52 g-xylitol/g-xylose in the mixed medium, respectively.

• KSBB Journal
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• v.24 no.1
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• pp.25-29
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• 2009

Ceramide is important not only for the maintenance of the barrier function of the skin but also for the water-binding capacity of the stratum corneum. Though the effectiveness of ceramide is not understood fully, ceramide has become a widely used ingredient in cosmetic and pharmaceutical industries. However, ceramide production from Saccharomyces cerevisiae has not been widely studied and the quantity are very low. Gene deletion in the cell is used frequently to investigate the function of gene and verification research of drug target. Specially, deletion mutant library is useful for a large amount functional analysis of gene. In this study, deletion mutants of genes on the metabolic pathway of ceramide synthesis in S. cerevisiae were grown in a batch culture and the cellular content of ceramide was measured. The ceramide content was highest in ${\triangle}$ydc1 mutant and 6 mg ceramide/g cell was obtained.

• Microbiology and Biotechnology Letters
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• v.16 no.6
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• pp.463-467
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• 1988

In this study characterization of spontaneous Lac$^-$ mutant of Lactobacillus casei YIT 9018 was investgated. The frequency of occuring the spontaneous Lac$^-$ mutant cells from stok culture strains was approximately 0.5% in MRS Media and 0.29% in 10% nonfat dried milk, ohterwise, that from pure Lac$^+$ colony it was 0.25% in MRS Media and 0.1% in l0% nonfat dried milk. In the physiological deference the spontaneous Lac$^-$ mutants were defective in lactose and/ or galactose-fermenting ability and also needed longer time for coagulation of nonfat dried milk than wild type.

• Proceedings of the Korea Environmental Mutagen Society Conference
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• 2003.10a
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• pp.184-184
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• 2003

• Korean Journal of Fisheries and Aquatic Sciences
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• v.53 no.4
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• pp.524-529
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• 2020

Recently, several mutant laver Pyropia yezoensis strains were developed. In this study, control laver Pyropia yezoensis and its mutant Py500G were compared for their amino acid contents and antioxidative activities. There was no significant difference of total amino acid contents between wild-type and mutant Py500G, but mutant had higher free amino acid contents than wild-type. Also, total phenolic content was higher in mutant Py500G. Phycoerythrin and phycocyanin contents were higher in wild-type. But, antixoidative activities were shown to be higher in mutant Py500G. These results will be useful for the development of new cultivar of Pyropia.

• Animal cells and systems
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• v.14 no.1
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• pp.1-10
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• 2010

Previously we showed that CHIP, a co-chaperone of Hsp70 and E3 ubiquitin ligase, can promote the degradation of mutant SOD1 linked to familial amyotrophic lateral sclerosis (fALS) via a mechanism not involving SOD1 ubiquitylation. Here we present evidence that CHIP functions in the interaction of mutant SOD1 with 26S proteasomes. Bag-1, a coupling factor between molecular chaperones and the proteasomes, formed a complex with SOD1 in an hsp70-dependent manner but had no direct effect on the degradation of mutant SOD1. Instead, Bag-1 stimulated interaction between CHIP and the proteasome-associated protein VCP (p97), which do not associate normally. Over-expressed CHIP interfered with the association between mutant SOD1 and VCP. Conversely, the binding of CHIP to mutant SOD1 was inhibited by VCP, implying that the chaperone complex and proteolytic machinery are competing for the common substrates. Finally we observed that mutant SOD1 strongly associated with the 19S complex of proteasomes and CHIP over-expression specifically reduced the interaction between S6/S6' ATPase subunits and mutant SOD1. These results suggest that CHIP, together with ubiquitin-binding proteins such as Bag-1 and VCP, promotes the degradation of mutant SOD1 by facilitating its translocation from ATPase subunits of 19S complex to the 20S core particle.

• Journal of Microbiology and Biotechnology
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• v.17 no.5
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• pp.721-727
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• 2007

Stability-enhanced mutants, H44, 11-94, 5A2-84, and F8, of L-threonine aldolase(L-TA) from Streptomyces coelicolor A3(2)(SCO1085) were isolated by an error-prone PCR followed by a high-throughput screening. Each of these mutant, had a single amino acid substitution: H177Y in the H44 mutant, A169T in the 11-94 mutant, D104N in the 5A2-84 mutant and F18I in the F8 mutant. The residual L-TA activity of the wild-type L-TA after a heat treatment for 20 min at $60^{\circ}C$ was only 10.6%. However, those in the stability-enhanced mutants were 85.7% for the H44 mutant, 58.6% for the F8 mutant, 62.1% for the 5A2-84 mutant, and 67.6% for the 11-94 mutant. Although the half-life of the wild-type L-TA at $63^{\circ}C$ was 1.3 min, those of the mutant L-TAs were longer: 14.6 min for the H44 mutant, 3.7 min for the 11-94 mutant, 5.8 min for the 5A2-84 mutant, and 5.0 min for the F8 mutant. The specific activity did not change in most of the mutants, but it was decreased by 45% in the case of mutant F8. When the aldol condensation of glycine and 3,4-dihydroxybenzaldehyde was studied by using whole cells of Escherichia coli containing the wild-type L-TA gene, L-threo-3,4-dihydroxyphenylserine(L-threo-DOPS) was successfully synthesized with a yield of 2.0 mg/ml after 20 repeated batch reactions for 100 h. However, the L-threo-DOPS synthesizing activity of the enzyme decreased with increased cycles of the batch reactions. Compared with the wild-type L-TA, H44 L-TA kept its L-threo-DOPS synthesizing activity almost constant during the 20 repeated batch reactions for 100 h, yielding 4.0 mg/ml of L-threo-DOPS. This result showed that H44 L-TA is more effective than the wild-type L-TA for the mass production of L-threo-DOPS.

• Korean Journal of Veterinary Service
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• v.30 no.3
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• pp.291-304
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• 2007

Mutants of an obligate aerobic bacterium, Vitreoscilla, that have deficiency in heat-labile catalase-peroxidase hydroperoxidase I (HPI) were created by EMS treatment. The catalase-peroxidase HPI-deficient mutant showed substantially lower peroxidase activity in exponential and mid-stationary phase compared with the wild type strain. In late stationary phase, the mutant exhibited no peroxidase activity. Peroxidase deficiency in the mutant was revealed by polyacrylamide gels stained for peroxidase activity. Characteristically, catalase levels in the mutant increased about 14- and 8-fold during growth in the exponential and stationary phases, respectively, compared to those in the wild type, suggesting a compensatory effect for protection from $H_2O_2$ toxicity. The mutant showed differences in physiology from the wild type: retardation in growth rate and decrease in oxygen consumption. Both the wild type and the catalase-peroxidase HPI-deficient mutant of Vitreoscilla had lower growth rates in media containing increasing $H_2O_2$ concentrations. However, the mutant exhibited an additionally decreased growth rate after 6 to 8 h of growth compared to the wild type. The wild type was resistent up to 20 mM $H_2O_2$, whereas the mutant was very sensitive to high concentrations of exogenous $H_2O_2$. Although elevated catalase levels would provide protection of the bacteria from the deleterious effect of $H_2O_2$, it did not appear to be complete. Cell-free extracts of the mutant showed decreased NADH oxidation rates and higher accumulation of $H_2O_2$ during this oxidation. These results may account for the impaired growth and earlier onset of death phase by the catalase-peroxidase HPI-deficient mutant of Vitreoscilla.

• KSBB Journal
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• v.31 no.1
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• pp.52-57
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• 2016

Mutant p53 (R280K) is highly expressed in MDA-MB-231 triple-negative human breast cancer cells. Currently, we reported the role of mutant p53-R280K in mediating the survival of MDA-MB-231 cells in vitro. The present study was undertaken to determine whether mutant p53-R280K affects breast cancer cell growth in vivo. To this end, we used small interfering RNA to knockdown the level of mutant p53-R280K in MDA-MB-231 cells. Silencing of mutant p53-R280K in MDA-MB-231 cells causes substantial tumor regression of established xenografts in vivo. In xenograft model for breast cancer, silencing of mutant p53-R280K in MDA-MB-231 cells significantly inhibited the tumor growth. Moreover, TUNEL assay showed more occurrence of apoptotic cells in mutant p53-R280K silenced tumors compared to control. Our data indicate that mutant p53-R280K has an important role in mediating tumor growth of MDA-MB-231 cells in vivo. Taken together, this study suggests that endogenous mutant p53-R280K could be used as a therapeutic target for breast cancer cells harboring this TP53 missense mutation.

• Proceedings of the Korean Society of Toxicology Conference
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• 2003.10b
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• pp.184-184
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• 2003

ENU(ethylnitrosourea) mutagenesis has been carrying out since 1999 in Korea Institute of Toxicology (KIT), Korea Research Institute Chemical of Technology (KRlCT). We have chosen BALB/c and C57BL/6 and screened for dominant and recessive mutants. Four hundred and twenty one males(GO) have been injected with ENU, 150, 200, 250 and 300 mg/kg body weight, twice, one week apart.(omitted)