• Title/Summary/Keyword: industrial proteomics

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Genomic Structure of the Cu,Zn Superoxide Dismutase (SOD1) Gene of Paecillomyces tenuipes and Paecilomyces sp.

  • Park Nam Sook;Lee Kwang Sik;Lee Sang Mong;Je Yeon Ho;Park Eunju;Sohn Hung Dae;Jin Byung Rae
    • International Journal of Industrial Entomology and Biomaterials
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    • v.10 no.1
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    • pp.35-43
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    • 2005
  • We describe here the complete nucleotide sequence and the exon-intron structure of the Cu,Zn superoxide dismutase (SOD1) gene of Paecilomyces tenuipes and Paecilomyces sp. The SOD1 gene of P. tenuipes spans 966 bp, and consisted of three introns and four exons coding for 154 amino acid residues. Three unambiguous introns in P. tenuipes separate exons of 13, 332, 97, and 20 bp, all exhibiting exon sizes identical to Cordyceps militaris SOD1 gene. The SOD1 gene of Paecilomyces sp. contains 946 bp and consisted of four introns and five exons coding for 154 amino acid residues. Five exons of Paecilomyces sp. SOD1 are composed of 13, 180, 152, 97, and 20 bp. Interestingly, this result showed that the total length of exons 2 (180 bp) and 3 (152 bp) of Paecilomyces sp. SOD1 is same to exon 2 length (332 bp) of C. militaris SOD1 and P. tenuipes SOD1. The deduced amino acid sequence of the P. tenuipes SOD1 showed $95\%$ identity to C. militaris SOD1 and $78\%$ to Paecilomyces sp. SOD1. Phylogenetic analysis confirmed that the C. militaris SOD1, P. tenuipes SOD1 and Paecilomyces sp. SOD1 are placed together within the ascomycetes group of fungal clade.

Proteomic Approach of the Protein Profiles during Seed Maturation in Common Buckwheat (Fagopyrum esculentum Moench.)

  • Park, Min-Hwa;Shin, Dong-Hoon;Han, Myoung-Hae;Yun, Young-Ho;Bae, Jeong-Sook;Lee, Yun-Sang;Chung, Keun-Yook;Lee, Moon-Soon;Woo, Sun-Hee
    • Korean Journal of Plant Resources
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    • v.22 no.3
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    • pp.227-235
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    • 2009
  • Single seeds of common buckwheat cultivar Suwon No. 1 when subjected to SDS-PAGE revealed very high polymorphism. High variation existed for protein or protein subunits with molecular weight 54-47kDa, 45-25kDa and 16-11kDa. The electrophoregram showed variation for globulin as well as other protein fractions. About 300 proteins were separated by two-dimensional electrophoresis in common buckwheat (Fagopyrum esculentum Moench.) seed. Seed maturation is a dynamic and temporally regulated phase of seed development that determines the composition of storage proteins reserves in mature seeds. Buckwheat seeds from 5, 10, 15, 20, and 25 days after pollination and matured stage were used for the analysis. This led to the establishment of high-resolution proteome reference maps, expression profiles of 48 spots. It was identified 48 proteins from MALDI-TOF/MS analysis of wild buckwheat seed storage proteins. The 48 proteins were found identical or similar to those of proteins reported in buckwheat and other plants; it is belonging to 9 major functional categories including seed storage proteins, stress/defense response, protein synthesis, photosynthesis, allergy proteins, amino acid, enzyme, metabolism, and miscellaneous. It appears that the major allergenic storage protein separated played the important role in buckwheat breeding and biochemical characterization.

Characterization of Proteins in the Muscle of Limanda yokohamae from the Masan Bay, Korea

  • Kim, Soo-Woon;Kim, Sam-Moon;Lee, Dong-Kun;Moon, Hyo-Bang;Choi, Hee-Gu;Kang, Chang-Keun;Choe, Eun-Sang
    • Ocean Science Journal
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    • v.42 no.2
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    • pp.129-134
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    • 2007
  • Increasing industrial development in the Masan Bay area of Korea over the past decades increased the risk for the survival of marine organisms in the bay area by the deterioration of the water quality. Since living organisms have the ability to adapt contamination-associated stimuli by the alteration of gene expression, changes in proteins can be used as an important criterion for assessing the levels of environmental conditions. In this study, therefore, alterations of the expression of proteins in the muscle of Limanda yokohamae from Dukdong and Dotsum in the bay area were surveyed and characterized as compared with Haegumgang, which served as a control site. The results demonstrated that the twenty spots detected from Dukdong and Dotsum were similar to each other. Fifteen proteins were found to be predicted or undefined proteins, while five proteins were identified as heavy polypeptide 11 of myosin, apolipoprotein A-I, fibroblast growth factor 17b precursor, G protein-coupled receptor kinase 1 b and bonnie and clyde. These data suggest that local fish in the bay area have dysfunction in muscle physiology including contraction, lipid metabolism, proliferation and differentiation and nervous system.

A Substrate Serves as a Hydrogen Atom Donor in the Enzyme-Initiated Catalytic Mechanism of Dual Positional Specific Maize Lipoxygenase-1

  • Huon, Thavrak;Jang, Sung-Kuk;Cho, Kyoung-Won;Rakwal, Randeep;Woo, Je-Chang;Kim, Il-Chul;Chi, Seung-Wook;Han, Ok-Soo
    • Bulletin of the Korean Chemical Society
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    • v.30 no.4
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    • pp.917-923
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    • 2009
  • The maize lipoxgyenase-1 is a non-traditional dual positional specific enzyme and the reaction proceeds via enzyme-initiated catalysis. Bioinformatic analysis indicated that the maize lipoxygenase-1 is structurally more similar to soybean LOX1 than pea LOXN2 in that it has an additional external loop (residues 318-351) in the carboxy-terminal catalytic domain. We analyzed the dependence of product distribution on concentration of linoleic acid and monitored the formation of hydroperoxyoctadecadienoic acid as a function of enzyme concentration. Product distribution was strongly influenced by substrate concentration, such that kinetically-controlled regioisomers were enriched and thermodynamically-controlled regioisomers were depleted at high substrate concentration. Kinetic studies indicated that the formation of hydroperoxyoctadecadienoic acid saturated rapidly in an enzyme concentration-dependent manner, which implied that reactivation by reoxidation of inactive Fe(II) failed to occur. Our results support the previously proposed enzyme-initiated catalytic mechanism of the maize lipoxgyenase-1 and reveals that a substrate molecule serves as a hydrogen atom donor in its enzyme-initiated catalysis.

Spatial protein expression of Panax ginseng by in-depth proteomic analysis for ginsenoside biosynthesis and transportation

  • Li, Xiaoying;Cheng, Xianhui;Liao, Baosheng;Xu, Jiang;Han, Xu;Zhang, Jinbo;Lin, Zhiwei;Hu, Lianghai
    • Journal of Ginseng Research
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    • v.45 no.1
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    • pp.58-65
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    • 2021
  • Background: Panax ginseng, as one of the most widely used herbal medicines worldwide, has been studied comprehensively in terms of the chemical components and pharmacology. The proteins from ginseng are also of great importance for both nutrition value and the mechanism of secondary metabolites. However, the proteomic studies are less reported in the absence of the genome information. With the completion of ginseng genome sequencing, the proteome profiling has become available for the functional study of ginseng protein components. Methods: We optimized the protein extraction process systematically by using SDS-PAGE and one-dimensional liquid chromatography mass spectrometry. The extracted proteins were then analyzed by two-dimensional chromatography separation and cutting-edge mass spectrometry technique. Results: A total of 2,732 and 3,608 proteins were identified from ginseng root and cauline leaf, respectively, which was the largest data set reported so far. Only around 50% protein overlapped between the cauline leaf and root tissue parts because of the function assignment for plant growing. Further gene ontology and KEGG pathway revealed the distinguish difference between ginseng root and leaf, which accounts for the photosynthesis and metabolic process. With in-deep analysis of functional proteins related to ginsenoside synthesis, we interestingly found the cytochrome P450 and UDP-glycosyltransferase expression extensively in cauline leaf but not in the root, indicating that the post glucoside synthesis of ginsenosides might be carried out when growing and then transported to the root at withering. Conclusion: The systematically proteome analysis of Panax ginseng will provide us comprehensive understanding of ginsenoside synthesis and guidance for artificial cultivation.

Status of research on the sweetpotato biotechnology and prospects of the molecular breeding on marginal lands (고구마 생명공학연구 현황과 조건 불리지역 분자육종 전망)

  • Kim, Ho Soo;Yoon, Ung-Han;Lee, Chan-Ju;Kim, So-Eun;Ji, Chang Yoon;Kwak, Sang-Soo
    • Journal of Plant Biotechnology
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    • v.45 no.3
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    • pp.196-206
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    • 2018
  • Dramatic increase in global population accompanied by rapid industrialization in developing countries has led to serious environmental, food, energy, and health problems. The Food and Agriculture Organization of the United Nations has estimated world population will increase to 9.7 billion by 2050 and require approximately 1.7 times more food, and more than 3.5 times energy than that of today. Particularly, sweetpotato is easy to cultivate in unfavorable conditions such as heat, drought, high salt, and marginal lands. In this respect, sweetpotato is an industrially valuable starch crop. To replace crops associated with these food and energy problems, it is necessary to develop new crops with improved nutrients and productivity, that can be grown on marginal lands, including desertification areas using plant biotechnology. For this purpose, exploring useful genes and developing genetically modified crops are essential strategies. Currently, sweetpotato [Ipomoea batatas (L.) Lam.] have been re-evaluated as the best health food and industrial crop that produces starch and low molecular weight antioxidants, such as vitamin A, vitamin E, anthocyanins and carotenoids. This review will focus on the current status of research on sweetpotato biotechnology on omics including genome sequencing, transcriptome, proteomics and molecular breeding. In addition, prospects on molecular breeding of sweetpotato on marginal lands for sustainable development were described.

Proteomic changes in leaves of sorghum exposed to copper stress in sorghum

  • Roy, Swapan Kumar;Kwon, Soo Jeong;Cho, Seong-Woo;Kamal, Abu Hena Mostafa;Kim, Sang-Woo;Sarker, Kabita;Jeong, Hae-Ryong;Lee, Moon-Soon;Chung, Keun-Yook;Woo, Sun-Hee
    • Proceedings of the Korean Society of Crop Science Conference
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    • 2017.06a
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    • pp.128-128
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    • 2017
  • Copper (Cu) is very toxic to plant cells due to its inhibitory effects on many physiological and biochemical processes. In spite of its potential physiological and economic significance, molecular characterization after Cu stress has so far been grossly overlooked in sorghum. To explore the molecular alterations that occur in response to copper stress, the present study was executed in ten-day-old Cu-exposed leaves of sorghum seedlings. The growth of shoots was markedly reduced, and ionic alterations were prominently observed in the leaves when the seedlings were exposed to different concentrations (0, 100, and $150{\mu}M$) of $CuSO_4$. Using two-dimensional gels with silver staining, 643 differentially expressed protein spots (${\geq}1.5-fold$) were identified as either significantly increased or reduced in abundance. Of these spots, a total of 24 protein spots (${\geq}1.5-fold$) from Cu-exposed sorghum leaves were successfully analyzed by MALDI-TOF-TOF mass spectrometry. Of the 24 differentially expressed proteins from Cu-exposed sorghum leaves, a total of 13 proteins were up-regulated, and 11 proteins were down-regulated. The abundance of most identified protein species, which function in carbohydrate metabolism, stress defense, and protein translation, was significantly enhanced, while that of another protein species involved in energy metabolism, photosynthesis and growth and development were severely reduced. The resulting differences in protein expression patterns together with related morpho-physiological processes suggested that these results could help to elucidate plant adaptation to Cu stress and provide insights into the molecular mechanisms of Cu responses in $C_4$ plants. The over-expression of GAPDH plays a significant role in assisting Sorghum bicolor to attenuate the adverse effects of oxidative stress caused by Cu, and the proteins involved in resistance to stress helped the sorghum plants to tolerate high levels of Cu.

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Proteomic analysis of serum proteins responsive to styrene exposure (Styrene 노출에 반응을 보이는 혈청 단백질에 대한 프로테오믹스 분석)

  • Kim, Ki-Woong;Heo, Kyung-Hwa;Won, Yong Lim;Jeong, Jin Wook;Kim, Tae Gyun;Park, Injeong
    • Journal of Korean Society of Occupational and Environmental Hygiene
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    • v.17 no.3
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    • pp.235-244
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    • 2007
  • By comparing the proteins from the workers exposed to styrene with the ones from controls, it may be possible to identify proteins that play a role in the occurrence and progress of occupational disease and thus to study the molecular mechanisms of occupational disease. In order to find the biomarkers for assessing the styrene effects early, before clinical symptoms develop and to understand the mechanisms of adverse health effects, we surveyed 134 employees, among whom 52 workers(30 male and 22 female) were chronically exposed to styrene in 10 glass-reinforced plastic boat manufacturing factories in Korea and 82 controls had never been occupationally exposed to hazardous chemicals including styrene. The age and drinking habits and serum biochemistry such as total protein, BUN and serum creatinine in both groups were significantly different. Exposed workers were divided into three groups according to exposure levels of styrene(G1, below 1/2 TLV; G2, 1/2 TLV to TLV; G3, above TLV). The mean concentration of airborne styrene in G1 group was $10.93{\pm}11.33ppm$, and those of urinary mandelic acid(MA) and phenylglyoxylic acid(PGA) were $0.17{\pm}0.21$ and $0.13{\pm}0.11g/g$ creatinine, respectively. The mean concentration of airborne styrene in G2 and G3 groups were $47.54{\pm}22.43$ and $65.33{\pm}33.47ppm$, respectively, and levels of urinary metabolites such as MA and PGA increased considerably as expected with the increase in exposure level of styrene. The airborne styrene concentration were significantly correlated to the urinary concentration of MA(r=0.784, p=0.000) and PGA(r=0.626, p<0.001). In the 2D electrophoresis, the concentration of five proteins including complement C3 precursor, alpha-1-antitrypsin(AAT), vitamin D binding protein precursor(DBP), alpha-1-B-glycoprotein(A1BG) and inter alpha trypsin inhibitor(ITI) heavy chain-related protein were significantly altered in workers exposed to styrene compared with controls. While expression of complement C3 precursor and AAT increased by exposure to styrene, expression of DBP, A1BG and ITI heavy chain-related protein decreased. These results suggest that the exposure of styrene might affects levels of plasma proteinase, carriers of endogenous substances and immune system. In particular, increasing of AAT with the increase in exposure level of styrene can explain the tissue damage and inflammation by the imbalance of proteinase/antiproteinase and decrease of DBP, A1BG and ITI heavy chain-related protein in workers exposed to styrene is associated with dysfunction and/or declination in immune system and signal transduction

Proteomic Analysis to Identify Tightly-Bound Cell Wall Protein in Rice Calli

  • Cho, Won Kyong;Hyun, Tae Kyung;Kumar, Dhinesh;Rim, Yeonggil;Chen, Xiong Yan;Jo, Yeonhwa;Kim, Suwha;Lee, Keun Woo;Park, Zee-Yong;Lucas, William J.;Kim, Jae-Yean
    • Molecules and Cells
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    • v.38 no.8
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    • pp.685-696
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    • 2015
  • Rice is a model plant widely used for basic and applied research programs. Plant cell wall proteins play key roles in a broad range of biological processes. However, presently, knowledge on the rice cell wall proteome is rudimentary in nature. In the present study, the tightly-bound cell wall proteome of rice callus cultured cells using sequential extraction protocols was developed using mass spectrometry and bioinformatics methods, leading to the identification of 1568 candidate proteins. Based on bioinformatics analyses, 389 classical rice cell wall proteins, possessing a signal peptide, and 334 putative non-classical cell wall proteins, lacking a signal peptide, were identified. By combining previously established rice cell wall protein databases with current data for the classical rice cell wall proteins, a comprehensive rice cell wall proteome, comprised of 496 proteins, was constructed. A comparative analysis of the rice and Arabidopsis cell wall proteomes revealed a high level of homology, suggesting a predominant conservation between monocot and eudicot cell wall proteins. This study importantly increased information on cell wall proteins, which serves for future functional analyses of these identified rice cell wall proteins.