• Korean Journal of Plant Resources
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• v.20 no.6
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• pp.524-529
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• 2007

We carried out to study the function of ArgE in transgenic rice plants, which were confirmed by PCR analysis and hygromycin selection. Transgenic rice plants were with selectable marker gene(HPT) inserted in genome of the rice. Southern analysis with hpt probe confirmed by two restriction enzymes that copy numbers of the selectable gene was introduced into the plant genome. We displayed that the relationship between drought stress and ArgE gene with the overexpressing rice plants. From this result, we observed that the degree of leaves damage has no difference in control and transgenic lines. The total RNAs were extracted from 6 weeks-seedling in normal condition in order to examine their expression levels with ArgE-overexpressed transgenic rice. In particular, expression patterns of genes encoding enzymes involved in abiotic stress, including drought and salt stresses. OsGF14a and OsSalt were investigated by reverse transcription-PCR(RT-PCR). Expression levels of the OsSalt gene decreased significantly in transgenic rice plants compared to control plant. However, ion leakage measurement did not demonstrate any leaves damage change between control and ArgE transgenic plants exposure to mannitol treatment. These results suggest that expression of the ArgE is not involved in tolerance for drought stress in rice but may playa role of signaling networks for salt-induced genes.

• Journal of Microbiology
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• v.34 no.4
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• pp.355-362
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• 1996

Complementation cloning of the argC, E, B, D, F, and G genes in Corynebacterium glutamicum was done by transforming the genomic DNA library into the corresponding arginine auxotrophs fo Escherichia coli. Recombinant plasmids containing 6.7 kb and 4.8kb fragments complementing the E. coli argB mutant were also able to complement the E. coli argC, E, A, D, and F mutants, indicating the clustered organization of the arginine biosynthetic genes within the cloned DNA fragments. The insert DNA fragments in the recombinant plasmids, named pRB1 AND pRB2, were physically mapped with several restriction enzymes. By further subcloning the entire DNA fragment containing the functions and by complementation analysis, we located the arg genes in the order of ACEBDF on the restriction map. We also determined the DNA nucleotide sequence of the fragment and report here the sequence of the argB gene. When compared to that with the mutant strain, higher enzyme activity of N-acetylglutamate kinase was detected in the extract of the mutant carrying the plasmid containing the putative argB gene, indicating that the plasmid contains a functional argB gene. Deduced amino acid sequence of the argB gene shows 45%, 38%, and 25% identity to that from Bacillus strearothermophilus, Bacillus substilus, and E. coli respectively. Our long term goal is genetically engineering C. glutamicum which produces more arginine than a wild type strain does.

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.326.1-326
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• 1995

No Abstract, See Full Text

• Korean Journal of Plant Resources
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• v.20 no.5
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• pp.437-441
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• 2007

The argE gene of E.coli was introduced into #Ilmibyeo# cultivar of rice by Agrobacterium tumefaciens and a large number of transgenic plants were produced. Embryogenic calli were co-cultivated with A. tumefaciens strain AGL1 carrying the plasmid pCAMBIA1300 containing hygromycin resistance(HygR). Transgenic plants showing in vitro resistance to 50mg/L hygromycin were obtained using a selection procedure. Stable integration of argE and HPT genes into chromosomal DNA was proven by southern blot analysis and PCR analysis of genomic isolated from $T_0$ progenies. The fragments of 650 bp(HPT) were detected in transgenic rice lines. The 230 bp(argE) fragments were showed in agarose gel, and detected fragments were matched with size of argE specific primer. The microscopic feature of leaf on scanning electron microscope(SEM) revealed differences between clear and chalky in shape and arrangement of stoma but did not discriminate.

• Journal of Life Science
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• v.8 no.5
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• pp.486-491
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• 1998

Previously, we have cloned and characterized two ADP-ribosyltransferases (Yac-1 and Yac-2) from mouse Iym-phocyte. Yac-2 transferase contains significant NAD glycohydrolase activity as well as ADP-ribosyltransferase acti-vity. Yac-2 has an arginine at position 221 between two conserved glutamic acids. To investigate the significance of Arg-221 on enzyme activities, Arg-221 was mutagenized to Glu (R221E) and to Ala (R221A). Mutants R221E and R221A were active as wild type for ADP-ribosyltransferase and NAD glycohydrolase activity, suggesting that the arginine 221 in Yac-2 does not play a major role in enzyme activities.

• Asian Pacific Journal of Cancer Prevention
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• v.15 no.7
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• pp.3247-3252
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• 2014

Background: Genetic factors have been shown to play an important role in the development of cancers. However, individual studies may fail to completely demonstrate complicated genetic relationships because of small sample size. Therefore, we performed a meta-analysis to evaluate the association of E-selectin Ser128Arg (S128R) with cancer risk. Materials and Methods: A literature search in PubMed, Embase, Web of Science, Science Direct, SpringerLink, EBSCO, Wanfang, and Chinese National Knowledge Infrastructure databases was carried out to identify studies of the association between E-selectin S128R polymorphism and cancer risk. The odds ratio (OR) with 95% confidence intervals (95%CIs) were used to assess the strength of association. Results: A total of eight studies involving 1,675 cancer cases and 2,285 controls were included in the meta-analysis. In overall populations, S128R polymorphism seemed to be associated with cancer risk (Arg allele vs Ser allele: OR=1.65, 95%CI =1.33-2.04, p<0.01; Arg/Arg+Arg/Ser vs Ser/Ser: OR=1.87, 95%CI =1.48-2.36, p<0.01; Arg/Ser vs Ser/Ser: OR=1.80, 95%CI =1.51-2.14, p<0.01). Similarly, subgroup analysis by ethnicity and source of control also revealed that this polymorphism was related to cancer risk. Conclusions: Our meta-analysis revealed that there was association between the E-selectin S128R polymorphism and the risk of cancer. Further large and well-designed studies are needed to confirm this association.

• Applied Biological Chemistry
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• v.38 no.2
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• pp.118-122
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• 1995

Escherichia Coli ornithine transcarbamylase is the enzyme which catalyzes the L-citrulline biosynthesis from L-ornithine and carbamyl phosphate. To facilitate the purification of enzyme which will be used for many biochemical studies such as structure and function relationships and catalytic mechanisms, the cloning and expression of E. coli argI gene for ornithine transcarbamylase was conducted. argI was amplified from genomic DNA of E. coli strain of $DH5{\alpha}$, by polymerization chain reaction (PCR) method. The amplified argI gene was ligated to the prokaryotic expression vector pKK223-3 and used for transformation of E. coli TB2 which was deficient of ornithine transcarbamylase. The over-produced enzyme by the tnansformant was purified by ammonium sulfate fractionation, heat denaturation and affinity chromatography. The result of SDS denaturation gel electrophoresis for the purified enzyme showed a single band of about 38 kDa of ornithine transcarbamylase. Kinetic data for the expressed enzyme gave almost the s?????? values as those of the wild type enzyme. The $k_{cat}$, of the enzyme was $1.0{\times}10^5min^{-1}$, and $K_ms$ for ornithine and carbamyl phosphate were 0.35 mM and 0.06 mM, respectively.

• Journal of Microbiology and Biotechnology
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• v.13 no.6
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• pp.949-954
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• 2003

The argG gene of Corynebacterium glutamicum encoding argininosuccinate synthetase (EC6345) was cloned and sequenced. The gene was cloned by heterologous complementation of an Escherichia coli arginine auxotrophic mutant (argG/sup -/). The cloned DNA fragment also complements E. coli argD, argF, and argH mutants, suggesting a clustered organization of the genes in the chromosome. The coding region of the argG gene is 1,206 nucleotides long with a deduced molecular weight of about 44 kDa, comparable with the predicted size of the expressed protein on the SDS-PAGE. Computer analysis revealed that the amino acid sequence of the argG gene product had a high similarity to that of Mycobacterium tuberculosis and Streptomyces clavuligerus. Two conserved sequence motifs within the ArgG appear to be ATP-binding sites which correspond to 2 of the 3 conserved regions found in sequences of all known argininosuccinate synthetases.

• Journal of Animal Science and Technology
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• v.64 no.4
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• pp.727-739
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• 2022

Mycotoxin contamination in pig feeds has a negative impact on growth performance, the immune system, and major body organs. Arginine (Arg) plays an important role in animals' body biochemistry and physiology. This study aimed to determine the effect of dietary Arg supplementation on mitigating the negative effects of mycotoxins in growing pigs. A total of 72 growing pigs (Landrace × Large white) with initial mean body weight (BW) = 55 ± 2.5 kg were allotted to four treatment groups with three replicates per group of six pigs per replicate in a completely randomized design. The treatments included a non-toxin diet with 1.2% Arg (NT1.2) and mycotoxin-challenged treatments supplemented with 1.2% Arg (TX1.2), 1.3% Arg (TX1.3), and 1.4% Arg (TX1.4). Statistical analysis of data included the effects of dietary level of Arg. The results indicated a significantly higher BW (p < 0.05), average daily gain (p < 0.05), and gain-to-feed ratio (p < 0.05) in the NT1.2 group than in the TX1.2, TX1.3, and TX1.4 groups. The relative weight of the liver was higher (p < 0.05) in the TX1.2 compared to that of the NT1.2 group, although it was not different from that of TX1.3 and TX1.4. The level of tumor necrosis factor-alpha was significantly up-regulated (p < 0.05) in the liver tissue of the TX1.2 group compared to that of the other treatments. Overall, dietary Arg supplementation remedied liver injury and alleviated the compromised immune system caused by mycotoxin toxicity.

• Biomedical Science Letters
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• v.11 no.4
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• pp.429-434
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• 2005

Apolipoprotein E (apoE) restriction isotyping used oligonucleotides to amplify apoE gene sequences containing amino acid positions 112 and 158. The amplification products were digested with HhaI and subjected to electrophoresis on $4\%$ agarose gel. Each of the isoforms was distinguished by a unique combination of HhaI fragment sizes that enabled unambiguous typing of all homozygotic and heterozygotic combinations. HhaI cleaves at GCGC encoding 112arg (E4) and 158arg (E3, E4), but does not cut at GTGC encoding 112cys (E2, E3) and] 58cys (E2). DNA was isolated from 72 study participants and apoE genotypes were determined utilizing the polymerase chain reaction and restriction isotyping. In the entire group of subjects, $38 (52.8\%)$ had apo E4/4 or E3/4 (Group E4), $28(38.9\%)$ had the apo E3/3 genotype (Group E3) and $6(8.3\%)$ had apo E2/2 or E2/3 (Group E2). This genotypic information may help to identify individuals at increased risk for several diseases.