• Title/Summary/Keyword: diverse pathways

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Oxidative Stress-dependent Structural and Functional Regulation of 2-cysteine Peroxiredoxins In Eukaryotes Including Plant Cells (산화 스트레스에 의존한 식물 및 진핵세포 2-시스테인 퍼록시레독신의 기능 조절)

  • Jang, Ho-Hee;Kim, Sun-Young;Lee, Sang-Yeol
    • Journal of Plant Biotechnology
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    • v.33 no.1
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    • pp.1-9
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    • 2006
  • Peroxiredoxins (Prxs) are ubiquitously distributed and play important functions in diverse cellular signaling systems. The proteins are largely classified into three groups, such as typical 2-Cys Prx, atypical 2-Cys Prx, and 1-Cys Prx, that are distinguished by their catalytic mechanisms and number of Cys residues. From the three classes of Prxs, the typical 2-Cys Prx containing the two-conserved Cys residues at its N-terminus and C-terminus catalyzes $H_2O_2$ with the use of thioredoxin (Trx) as an electron donor. During the catalytic cycle, the N-terminal Cys residue undergoes a peroxide-dependent oxidation to sulfenic acid, which can be further oxidized to sulfinic acid at the presence of high concentrations of $H_2O_2$ and a Trx system containing Trx, Trx reductase, and NADPH. The sulfinic acid form of 2-Cys Prx is reduced by the action of sulfiredoxin which requires ATP as an energy source. Under the strong oxidative or heat shock stress conditions, 2-Cys Prx in eukaryotes rapidly switches its protein structure from low-molecular-weight species to high-molecular-weight protein structures. In accordance with its structural changes, the protein concomitantly triggers functional switching from a peroxidase to a molecular chaperone, which can protect its substrate denaturation from external stress. In addition to its N-terminal active site, the C-terminal domain including 'YF-motif' of 2-Cys Prx plays a critical role in the structural changes. Therefore, the C-terminal truncated 2-Cys Prxs are not able to regulate their protein structures and highly resistant to $H_2O_2$-dependent hyperoxidation, suggesting that the reaction is guided by the peroxidatic Cys residue. Based on the results, it may be concluded that the peroxidatic Cys of 2-Cys Prx acts as an '$H_2O_2$-sensor' in the cells. The oxidative stress-dependent regulation of 2-Cys Prx provides a means of defense systems in cells to adapt stress conditions by activating intracellular defense signaling pathways. Particularly, 2-Cys Prxs in plants are localized in chloroplasts with a dynamic protein structure. The protein undergoes conformational changes again oxidative stress. Depending on a redox-potential of the chloroplasts, the plant 2-Cys Prx forms super-molecular weight protein structures, which attach to the thylakoid membranes in a reversible manner.

Flavonoid Biosynthesis: Biochemistry and Metabolic Engineering (Flavonoid 생합성:생화학과 대사공학적 응용)

  • Park, Jong-Sug;Kim, Jong-Bum;Kim, Kyung-Hwan;Ha, Sun-Hwa;Han, Bum-Soo;Kim, Yong-Hwan
    • Journal of Plant Biotechnology
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    • v.29 no.4
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    • pp.265-275
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    • 2002
  • Flavonoid biosynthesis is one of the most extensively studied areas in the secondary metabolism. Due to the study of flavonoid metabolism in diverse plant system, the pathways become the best characterized secondary metabolites and can be excellent targets for metabolic engineering. These flavonoid-derived secondary metabolites have been considerably divergent functional roles: floral pigment, anticancer, antiviral, antitoxin, and hepatoprotective. Three species have been significant for elucidating the flavonoid metabolism and isolating the genes controlling the flavonoid genes: maize (Zea mays), snapdragon (Antirrhinum majus) and petunia (Prtunia hybrida). Recently, many genes involved in biosynthesis of flavonoid have been isolated and characterized using mutation and recombinant DNA technologies including transposon tagging and T-DNA tagging which are novel approaches for the discovery of uncharacterized genes. Metabolic engineering of flavonoid biosynthesis was approached by sense or antisense manipulation of the genes related with flavonoid pathway, or by modified expression of regulatory genes. So, the use of a variety of experimental tools and metabolic engineering facilitated the characterization of the flavonoid metabolism. Here we review recent progresses in flavonoid metabolism: confirmation of genes, metabolic engineering, and applications in the industrial use.

Degradation Kinetic and Mechanism of Methyl Tert-butyl Ether (MTBE) by the Modified Photo-Fenton Reaction (Modified Photo-Fenton Reaction을 이용한 Methyl Tert-butyl Ether (MTBE)의 분해 Kinetic 및 메커니즘 규명에 관한 연구)

  • Kim, Min-Kyoung;Kong, Sung-Ho
    • Journal of Soil and Groundwater Environment
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    • v.11 no.6
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    • pp.69-75
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    • 2006
  • Improper disposal of petroleum and spills from underground storage tanks have created large areas with highly toxic contamination of the soil and groundwater. Methyl tert-butyl ether (MTBE) is widely used as a fuel additive because of its advantageous properties of increasing the octane value and reducing carbon monoxide and hydrocarbon exhausts. However, MTBE is categorized as a possible human carcinogen. This research investigated the Modified Photo-Fenton system which is based on the Modified Fenton reaction and UV light irradiation. The Modified Fenton reaction is effective for MTBE degradation near a neutral pH, using the ferric ion complex composed of a ferric ion and environmentally friendly organic chelating agents. This research was intended to treat high concentrations of MTBE; thus, 1,000 mg/L MTBE was chosen. The objectives of this research are to find the optimal reaction conditions and to elucidate the kinetic and mechanism of MTBE degradation by the Modified Photo-Fenton reaction. Based on the results of experiments, citrate was chosen among eight chelating agents as the candidate for the Modified Photo-Fenton reaction because it has a relatively higher final pH and MTBE removal efficiency than the others, and it has a relatively low toxicity and is rapidly biodegradable. MTBE degradation was found to follow pseudo-first-order kinetics. Under the optimum conditions, [$Fe^{3+}$] : [Citrate] = 1 mM: 4 mM, 3% $H_2O_2$, 17.4 kWh/L UV dose, and initial pH 6.0, the 1000 ppm MTBE was degraded by 86.75% within 6 hours and 99.99% within 16 hours. The final pH value was 6.02. The degradation mechanism of MTBE by the Modified Photo-Fenton Reaction included two diverse pathways and tert-butyl formate (TBF) was identified to be the major degradation intermediate. Attributed to the high solubility, stability, and reactivity of the ferric-citrate complexes in the near neutral condition, this Modified Photo-Fenton reaction is a promising treatment process for high concentrations of MTBE under or near a neutral pH.

Construction of Gene Network System Associated with Economic Traits in Cattle (소의 경제형질 관련 유전자 네트워크 분석 시스템 구축)

  • Lim, Dajeong;Kim, Hyung-Yong;Cho, Yong-Min;Chai, Han-Ha;Park, Jong-Eun;Lim, Kyu-Sang;Lee, Seung-Su
    • Journal of Life Science
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    • v.26 no.8
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    • pp.904-910
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    • 2016
  • Complex traits are determined by the combined effects of many loci and are affected by gene networks or biological pathways. Systems biology approaches have an important role in the identification of candidate genes related to complex diseases or traits at the system level. The gene network analysis has been performed by diverse types of methods such as gene co-expression, gene regulatory relationships, protein-protein interaction (PPI) and genetic networks. Moreover, the network-based methods were described for predicting gene functions such as graph theoretic method, neighborhood counting based methods and weighted function. However, there are a limited number of researches in livestock. The present study systemically analyzed genes associated with 102 types of economic traits based on the Animal Trait Ontology (ATO) and identified their relationships based on the gene co-expression network and PPI network in cattle. Then, we constructed the two types of gene network databases and network visualization system (http://www.nabc.go.kr/cg). We used a gene co-expression network analysis from the bovine expression value of bovine genes to generate gene co-expression network. PPI network was constructed from Human protein reference database based on the orthologous relationship between human and cattle. Finally, candidate genes and their network relationships were identified in each trait. They were typologically centered with large degree and betweenness centrality (BC) value in the gene network. The ontle program was applied to generate the database and to visualize the gene network results. This information would serve as valuable resources for exploiting genomic functions that influence economically and agriculturally important traits in cattle.

Discovery of UBE2I as a Novel Binding Protein of a Premature Ovarian Failure-Related Protein, FOXL2 (조기 난소 부전증 유발 관련 단백질인 FOXL2의 새로운 결합 단백질 UBE2I의 발견)

  • Park, Mira;Jung, Hyun Sook;Kim, Hyun-Lee;Pisarska, Margareta D.;Ha, Hye-Jeong;Lee, Kangseok;Bae, Jeehyeon;Ko, Jeong-Jae
    • Development and Reproduction
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    • v.12 no.3
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    • pp.289-296
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    • 2008
  • BPES (Blepharophimosis/Ptosis/Epicanthus inversus Syndrome) is an autosomal dominant disorder caused by mutations in FOXL2. Affected individuals have premature ovarian failure (POF) in addition to small palpebral fissures, drooping eyelids, and broad nasal bridge. FOXL2 is a member of the forkhead family transcription factors. In FOXL2-deficient ovaries, granulosa cell differentiation dose not progress, leading to arrest of folliculogenesis and oocytes atresia. Using yeast two-hybrid screening of rat ovarian cDNA library with FOXL2 as bait, we found that small ubiquitin-related modifier (SUMO)-conjugating E2 enzyme UBE2I protein interacted with FOXL2 protein. UBE2I also known as UBC9 is an essential protein for processing SUMO modification. Sumoylation is a form of post-translational modification involved in diverse signaling pathways including the regulation of transcriptional activities of many transcriptional factors. In the present study, we confirmed the protein-protein interaction between FOXL2 and UBE2I in human cells, 293T, by in vivo immunoprecipitation. In addition, we generated truncated FOXL2 mutants and identified the region of FOXL2 required for its association with UBE2I using yeast-two hybrid system. Therefore, the identification of UBE2I as an interacting protein of FOXL2 further suggests a presence of novel regulatory mechanism of FOXL2 by sumoylation.

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