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Pesquisa : A11.284.430.214.190.500.585.250 [Categoria DeCS]
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[PMID]:25955696
[Au] Autor:Eprintsev AT; Fedorin DN; Salnikov AV; Igamberdiev AU
[Ad] Endereço:Department of Biochemistry and Cell Physiology, Voronezh State University, Voronezh 394006, Russia.
[Ti] Título:Expression and properties of the glyoxysomal and cytosolic forms of isocitrate lyase in Amaranthus caudatus L.
[So] Source:J Plant Physiol;181:1-8, 2015 Jun 01.
[Is] ISSN:1618-1328
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Isocitrate lyase (EC 4.1.3.1) catalyzes the reversible conversion of d-isocitrate to succinate and glyoxylate. It is usually associated with the glyoxylate cycle in glyoxysomes, although the non-glyoxysomal form has been reported and its relation to interconversion of organic acids outside the glyoxylate cycle suggested. We investigated the expression of two isocitrate lyase genes and activities of the glyoxysomal (ICL1) and cytosolic (ICL2) forms of isocitrate lyase in amaranth (Amaranthus caudatus L.) seedlings. Both forms were separated and purified. The cytosolic form had a low optimum pH (6.5) and was activated by Mn(2+) ions, while Mg(2+) was ineffective, and had a lower affinity to d, l-isocitrate (Km 63 µM) as compared to the glyoxysomal form (optimum pH 7.5, K(m) 45 µM), which was activated by Mg(2+). The highest ICL1 activity was observed on the 3rd day of germination; then the activity and expression of the corresponding gene decreased, while the activity of ICL2 and gene expression increased to the 7th day of germination and then remained at the same level. It is concluded that the function of ICL1 is related to the glyoxylate cycle while ICL2 functions independently from the glyoxylate cycle and interconverts organic acids in the cytosol.
[Mh] Termos MeSH primário: Amaranthus/enzimologia
Amaranthus/genética
Citosol/enzimologia
Regulação da Expressão Gênica de Plantas
Glioxissomos/enzimologia
Isocitrato Liase/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Centrifugação com Gradiente de Concentração
DNA Complementar/genética
Eletroforese em Gel de Ágar
Regulação Enzimológica da Expressão Gênica
Genes de Plantas
Germinação
Concentração de Íons de Hidrogênio
Isocitrato Liase/isolamento & purificação
Isocitrato Liase/metabolismo
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
Dados de Sequência Molecular
Fator 1 de Elongação de Peptídeos/metabolismo
Plântulas/enzimologia
Frações Subcelulares/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (Isoenzymes); 0 (Peptide Elongation Factor 1); EC 4.1.3.1 (Isocitrate Lyase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150609
[Lr] Data última revisão:
150609
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150509
[St] Status:MEDLINE


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[PMID]:25933369
[Au] Autor:Eprintsev AT; Fedorin DN; Nikitina MV; Igamberdiev AU
[Ad] Endereço:Department of Biochemistry and Cell Physiology, Voronezh State University, Voronezh 394006, Russia.
[Ti] Título:Expression and properties of the mitochondrial and cytosolic forms of aconitase in maize scutellum.
[So] Source:J Plant Physiol;181:14-9, 2015 Jun 01.
[Is] ISSN:1618-1328
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Aconitase (EC 4.2.1.3) catalyzes the reversible interconversion of citrate, cis-aconitate, and D-isocitrate. It operates in mitochondria and cytosol. We investigated the expression of two aconitase genes (Aco1 and Aco4) and activities of the mitochondrial and cytosolic forms in maize (Zea mays L.) scutellum during germination. Both forms were isolated and purified. The cytosolic form had a higher pH optimum (8.0), twice higher affinity to citrate (K(m) 9.5 mM), and slightly lower affinity to D,L-isocitrate (K(m) 1.7 mM) as compared to the mitochondrial form (optimum pH 7.5, K(m) with citrate 21 mM, and K(m) with isocitrate 1.5 mM). The highest activity of both forms of aconitase was observed on the 4th day of germination; then the activity and expression of the cytosolic form sharply decreased, while the mitochondrial form decreased more slowly. The mitochondrial aconitase was more strongly inhibited by H2O2 (half-inhibition at 35 µM) than the cytosolic form (60 µM). Aconitase activity was not detected in the glyoxysomal fraction beyond the cross-contamination level. It is suggested that the mitochondrial form operates in the tricarboxylic acid cycle, whereas the cytosolic form participates in the reactions of the glyoxylate cycle taking place outside the glyoxysome.
[Mh] Termos MeSH primário: Aconitato Hidratase/genética
Citosol/enzimologia
Regulação da Expressão Gênica de Plantas
Mitocôndrias/enzimologia
Zea mays/enzimologia
Zea mays/genética
[Mh] Termos MeSH secundário: Aconitato Hidratase/isolamento & purificação
Aconitato Hidratase/metabolismo
Regulação Enzimológica da Expressão Gênica
Genes de Plantas
Germinação
Glioxissomos/enzimologia
Concentração de Íons de Hidrogênio
Isoenzimas/metabolismo
Cinética
Frações Subcelulares/enzimologia
Zea mays/anatomia & histologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); EC 4.2.1.3 (Aconitate Hydratase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150609
[Lr] Data última revisão:
150609
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150502
[St] Status:MEDLINE


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[PMID]:25413007
[Au] Autor:Hayashi Y; Sato N; Shinozaki A; Watanabe M
[Ad] Endereço:Faculty of Science, Niigata University, 8050 Ikarashi, Ninochou, Niigata, 950-2181, Japan, yhayashi@env.sc.niigata-u.ac.jp.
[Ti] Título:Increase in peroxisome number and the gene expression of putative glyoxysomal enzymes in Chlamydomonas cells supplemented with acetate.
[So] Source:J Plant Res;128(1):177-85, 2015 Jan.
[Is] ISSN:1618-0860
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:We cultured Chlamydomonas reinhardtii cells in a minimal culture medium supplemented with various concentrations of acetate, fatty acids, ethanol, fatty alcohols, or sucrose. The presence of acetate (0.5 or 1.0%, w/v) was advantageous for cell growth. To determine whether peroxisomes are involved in fatty acid and fatty alcohol metabolism, we investigated the dynamics of peroxisomes, including changes in their number and size, in the presence of acetate, ethanol, and sucrose. The total volume of peroxisomes increased when cells were grown with acetate, but did not change when cells were grown with ethanol or sucrose. We analyzed cell growth on minimal culture medium supplemented with various fatty acids (carbon chain length ranging from one to ten) to investigate which fatty acids are metabolized by C. reinhardtii. Among them, acetate caused the greatest increase in growth when added to minimal culture media. We analyzed the transcript levels of genes encoding putative glyoxysomal enzymes. The transcript levels of genes encoding malate synthase, malate dehydrogenase, isocitrate lyase, and citrate synthase increased when Chlamydomonas cells were grown on minimal culture medium supplemented with acetate. Our results suggest that Chlamydomonas peroxisomes are involved in acetate metabolism via the glyoxylate cycle.
[Mh] Termos MeSH primário: Acetatos/farmacologia
Chlamydomonas/enzimologia
Chlamydomonas/genética
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Glioxissomos/enzimologia
Peroxissomos/metabolismo
[Mh] Termos MeSH secundário: Proliferação Celular/efeitos dos fármacos
Células Cultivadas
Chlamydomonas/citologia
Chlamydomonas/ultraestrutura
Meios de Cultura/farmacologia
Genes de Plantas
Glioxissomos/efeitos dos fármacos
Glioxissomos/genética
Microscopia de Fluorescência
Peroxissomos/efeitos dos fármacos
Peroxissomos/ultraestrutura
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acetates); 0 (Culture Media); 0 (RNA, Messenger)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:171014
[Lr] Data última revisão:
171014
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141122
[St] Status:MEDLINE
[do] DOI:10.1007/s10265-014-0681-8


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[PMID]:24739336
[Au] Autor:Goto-Yamada S; Mano S; Oikawa K; Shibata M; Nishimura M
[Ad] Endereço:Department of Cell Biology; National Institute for Basic Biology; Okazaki, Japan.
[Ti] Título:Interaction between chaperone and protease functions of LON2, and autophagy during the functional transition of peroxisomes.
[So] Source:Plant Signal Behav;9(5):e28838, 2014.
[Is] ISSN:1559-2324
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Functional transition of glyoxysomes to leaf peroxisomes is observed in greening cotyledons. Glyoxysomal proteins are rapidly degraded and leaf-peroxisomal proteins are transported into peroxisomes after cotyledons are exposed to light, but the molecular mechanisms underlying these processes remain unclear. We recently discovered that two degradation pathways are involved in the functional transition of peroxisomes using Arabidopsis thaliana. Lon protease 2 (LON2) is responsible for the degradation of glyoxysomal proteins inside peroxisomes, and, in parallel, autophagy eliminates damaged or obsolete peroxisomes. A double mutant defective in both the LON2- and autophagy-dependent degradation pathways accumulated glyoxysomal proteins after the cotyledons became green. Our study also demonstrated that the LON2- and autophagy-dependent pathways are interdependent, with the chaperone function of LON2 suppressing autophagic peroxisome degradation. Moreover, the peptidase domain of LON2 interferes with the suppression of autophagy, indicating that autophagy is regulated by intramolecular modulation between the proteolysis and chaperone functions of LON2.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/enzimologia
Autofagia
Chaperonas Moleculares/metabolismo
Peptídeo Hidrolases/metabolismo
Peroxissomos/metabolismo
[Mh] Termos MeSH secundário: Glioxissomos/metabolismo
Redes e Vias Metabólicas
Modelos Biológicos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Molecular Chaperones); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140418
[St] Status:MEDLINE


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[PMID]:24207097
[Au] Autor:Meyer D; Herrfurth C; Brodhun F; Feussner I
[Ti] Título:Degradation of lipoxygenase-derived oxylipins by glyoxysomes from sunflower and cucumber cotyledons.
[So] Source:BMC Plant Biol;13:177, 2013 Nov 09.
[Is] ISSN:1471-2229
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Oilseed germination is characterized by the degradation of storage lipids. It may proceed either via the direct action of a triacylglycerol lipase, or in certain plant species via a specific lipid body 13-lipoxygenase. For the involvement of a lipoxygenase previous results suggested that the hydroxy- or oxo-group that is being introduced into the fatty acid backbone by this lipoxygenase forms a barrier to continuous ß-oxidation. RESULTS: This study shows however that a complete degradation of oxygenated fatty acids is possible by isolated cucumber and sunflower glyoxysomes. Interestingly, degradation is accompanied by the formation of saturated short chain acyl-CoAs with chain length between 4 and 12 carbon atoms lacking the hydroxy- or oxo-diene system of the oxygenated fatty acid substrate. The presence of these CoA esters suggests the involvement of a specific reduction of the diene system at a chain length of 12 carbon atoms including conversion of the hydroxy-group at C7. CONCLUSIONS: To our knowledge this metabolic pathway has not been described for the degradation of polyunsaturated fatty acids so far. It may represent a new principle to degrade oxygenated fatty acid derivatives formed by lipoxygenases or chemical oxidation initiated by reactive oxygen species.
[Mh] Termos MeSH primário: Cotilédone/enzimologia
Cucumis sativus/metabolismo
Glioxissomos/metabolismo
Helianthus/metabolismo
Lipoxigenase/metabolismo
Oxilipinas/metabolismo
[Mh] Termos MeSH secundário: Cotilédone/metabolismo
Cucumis sativus/enzimologia
Estiolamento
Glioxissomos/enzimologia
Helianthus/enzimologia
Ácidos Linoleicos/metabolismo
Ácidos Linolênicos/metabolismo
Peróxidos Lipídicos/metabolismo
Redes e Vias Metabólicas
NAD/metabolismo
Oxirredução
Plântulas/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Linoleic Acids); 0 (Linolenic Acids); 0 (Lipid Peroxides); 0 (Oxylipins); 0U46U6E8UK (NAD); 23017-93-8 (13-hydroperoxy-9,11-octadecadienoic acid); 31385-09-8 (13-oxo-9,11-octadecadienoic acid); EC 1.13.11.- (13-lipoxygenase); EC 1.13.11.12 (Lipoxygenase)
[Em] Mês de entrada:1408
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131112
[St] Status:MEDLINE
[do] DOI:10.1186/1471-2229-13-177


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[PMID]:23162115
[Au] Autor:Pagnussat L; Burbach C; Baluska F; de la Canal L
[Ad] Endereço:Instituto de Investigaciones Biológicas, Universidad Nacional de Mar del Plata-CONICET, Funes 3250, 7600 Mar del Plata, Argentina.
[Ti] Título:An extracellular lipid transfer protein is relocalized intracellularly during seed germination.
[So] Source:J Exp Bot;63(18):6555-63, 2012 Nov.
[Is] ISSN:1460-2431
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Plant lipid transfer proteins (LTPs) constitute a family of small proteins recognized as being extracellular. In agreement with this notion, several lines of evidence have shown the apoplastic localization of HaAP10, a LTP from Helianthus annuus dry seeds. However, HaAP10 was recently detected intracellularly in imbibing seeds. To clarify its distribution, immunolocalization experiments were performed during the course of germination and confirmed its intracellular localization upon early seed imbibition. Further assays using a hydrophobic dye, FM4-64, inhibitors of vesicular traffic, and immunolocalization of the pectin rhamnogalacturonan-II, allowed the conclusion that endocytosis is activated as soon as seed imbibition starts. Furthermore, this study demonstrated that HaAP10 is endocytosed throughout imbibition. Biochemical and cellular approaches indicate that the intracellular fraction of this LTP appears associated with oil bodies and some evidence also suggest its presence in glyoxysomes. So, HaAP10 is apoplastic in dry seeds and upon imbibition is rapidly internalized and relocalized to organelles involved in lipid metabolism. The results suggest that HaAP10 may be acting as a fatty acid shuttle between the oil body and the glyoxysome during seed germination. This concept is consistent with the initial proposition that LTPs participate in the intracellular transfer of lipids which was further denied based on their apparent extracellular localization. This report reveals for the first time the relocalization of a lipid transfer protein and opens new perspectives on its role.
[Mh] Termos MeSH primário: Antígenos de Plantas/metabolismo
Proteínas de Transporte/metabolismo
Germinação
Helianthus/crescimento & desenvolvimento
Helianthus/metabolismo
Proteínas de Plantas/metabolismo
Sementes/metabolismo
[Mh] Termos MeSH secundário: Citosol/metabolismo
Eletroforese em Gel de Poliacrilamida
Fluorimunoensaio
Glioxissomos/metabolismo
Helianthus/citologia
Microscopia Confocal
Microscopia Eletrônica de Transmissão
Pectinas/metabolismo
Estruturas Vegetais/metabolismo
Transporte Proteico
Compostos de Piridínio/metabolismo
Compostos de Amônio Quaternário/metabolismo
Sementes/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, Plant); 0 (Carrier Proteins); 0 (FM 4-64); 0 (Pectins); 0 (Plant Proteins); 0 (Pyridinium Compounds); 0 (Quaternary Ammonium Compounds); 0 (lipid transfer proteins, plant); 0 (rhamnogalacturonan II)
[Em] Mês de entrada:1305
[Cu] Atualização por classe:121123
[Lr] Data última revisão:
121123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121120
[St] Status:MEDLINE
[do] DOI:10.1093/jxb/ers311


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[PMID]:22683191
[Au] Autor:Liu X; Ma C; Subramani S
[Ad] Endereço:Section of Molecular Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093-0322, United States.
[Ti] Título:Recent advances in peroxisomal matrix protein import.
[So] Source:Curr Opin Cell Biol;24(4):484-9, 2012 Aug.
[Is] ISSN:1879-0410
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Peroxisomes are essential organelles responsible for many metabolic reactions, such as the oxidation of very long chain and branched fatty acids, D-amino acids and polyamines, as well as the production and turnover of hydrogen peroxide. They comprise a class of organelles called microbodies, including glycosomes, glyoxysomes and Woronin bodies. Dysfunction of human peroxisomes causes severe and often fatal peroxisome biogenesis disorders (PBDs). Peroxisomal matrix protein import is mediated by receptors that shuttle between the cytosol and peroxisomal matrix using ubiquitination/deubiquitination reactions and ATP hydrolysis for receptor recycling. We focus on the machinery involved in the peroxisomal matrix protein import cycle, highlighting recent advances in peroxisomal matrix protein import, cargo release and receptor recycling/degradation.
[Mh] Termos MeSH primário: Peroxissomos/metabolismo
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Citosol/metabolismo
Glioxissomos/metabolismo
Seres Humanos
Membranas Intracelulares/metabolismo
Sinais Direcionadores de Proteínas
Transporte Proteico
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Protein Sorting Signals); 0 (Proteins)
[Em] Mês de entrada:1304
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120612
[St] Status:MEDLINE
[do] DOI:10.1016/j.ceb.2012.05.003


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[PMID]:20679226
[Au] Autor:Prestele J; Hierl G; Scherling C; Hetkamp S; Schwechheimer C; Isono E; Weckwerth W; Wanner G; Gietl C
[Ad] Endereço:LS Botanik and LS Systembiologie der Pflanzen, Technische Universität München, D-85350 Freising, Germany.
[Ti] Título:Different functions of the C3HC4 zinc RING finger peroxins PEX10, PEX2, and PEX12 in peroxisome formation and matrix protein import.
[So] Source:Proc Natl Acad Sci U S A;107(33):14915-20, 2010 Aug 17.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The integral peroxisomal membrane proteins PEX10, PEX2, and PEX12 contain a zinc RING finger close to the C terminus. Loss of function of these peroxins causes embryo lethality at the heart stage in Arabidopsis. Preventing the coordination of Zn(2+) ions by amino acid substitutions in PEX10, PEX2, and PEX12 and overexpressing the resulting conditional sublethal mutations in WT uncovered additional functions of PEX10. Plants overexpressing DeltaZn-mutant PEX10 display deformed peroxisomal shapes causing diminished contact with chloroplasts and possibly with mitochondria. These changes correlated with impaired metabolite transfer and, at high CO(2), recoverable defective photorespiration plus dwarfish phenotype. The N-terminal PEX10 domain is critical for peroxisome biogenesis and plant development. A point mutation in the highly conserved TLGEEY motif results in vermiform peroxisome shape without impairing organelle contact. Addition of an N-terminal T7 tag to WT PEX0 resulted in partially recoverable reduced growth and defective inflorescences persisting under high CO(2). In contrast, plants overexpressing PEX2-DeltaZn-T7 grow like WT in normal atmosphere, contain normal-shaped peroxisomes, but display impaired peroxisomal matrix protein import. PEX12-DeltaZn-T7 mutants exhibit unimpaired import of matrix protein and normal-shaped peroxisomes when grown in normal atmosphere. During seed germination, glyoxysomes form a reticulum around the lipid bodies for mobilization of storage oil. The formation of this glyoxysomal reticulum seemed to be impaired in PEX10-DeltaZn but not in PEX2-DeltaZn-T7 or PEX12-DeltaZn-T7 plants. Both cytosolic PEX10 domains seem essential for peroxisome structure but differ in metabolic function, suggesting a role for this plant peroxin in addition to the import of matrix protein via ubiquitination of PEX5.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Proteínas de Membrana/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
Peroxissomos/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos/genética
Sequência de Aminoácidos
Arabidopsis/genética
Proteínas de Arabidopsis/genética
Transporte Biológico
Dióxido de Carbono/metabolismo
Proteínas da Matriz Extracelular/metabolismo
Regulação da Expressão Gênica de Plantas
Glioxissomos/metabolismo
Glioxissomos/ultraestrutura
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Proteínas de Membrana/genética
Proteínas de Membrana Transportadoras/genética
Metabolômica/métodos
Microscopia Confocal
Microscopia Eletrônica
Modelos Biológicos
Dados de Sequência Molecular
Mutação
Peroxinas
Receptor 1 de Sinal de Orientação para Peroxissomos
Peroxissomos/ultraestrutura
Fotossíntese
Plantas Geneticamente Modificadas
Domínios RING Finger/genética
Receptores Citoplasmáticos e Nucleares/genética
Receptores Citoplasmáticos e Nucleares/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência de Aminoácidos
Dedos de Zinco/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Extracellular Matrix Proteins); 0 (Membrane Proteins); 0 (Membrane Transport Proteins); 0 (PEX10 protein, Arabidopsis); 0 (Peroxins); 0 (Peroxisome-Targeting Signal 1 Receptor); 0 (Receptors, Cytoplasmic and Nuclear); 0 (TED3 protein, Arabidopsis); 0 (peroxin 12 protein, Arabidopsis); 142M471B3J (Carbon Dioxide); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1009
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100804
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1009174107


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[PMID]:20464792
[Au] Autor:Canvin DT; Beevers H
[Ti] Título:The discovery of glyoxysomes: the work of Harry Beevers. 1961.
[So] Source:J Biol Chem;285(20):e6-7, 2010 May 14.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Glioxissomos
[Mh] Termos MeSH secundário: Inglaterra
História do Século XX
[Pt] Tipo de publicação:BIOGRAPHY; CLASSICAL ARTICLE; HISTORICAL ARTICLE; JOURNAL ARTICLE
[Ps] Nome de pessoa como assunto:Canvin DT; Beevers H
[Em] Mês de entrada:1006
[Cu] Atualização por classe:141203
[Lr] Data última revisão:
141203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100514
[St] Status:MEDLINE


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[PMID]:20067829
[Au] Autor:Bhatla SC; Kaushik V; Yadav MK
[Ad] Endereço:Department of Botany, University of Delhi, North Campus, Delhi-110007, India. bhatlasc@gmail.com
[Ti] Título:Use of oil bodies and oleosins in recombinant protein production and other biotechnological applications.
[So] Source:Biotechnol Adv;28(3):293-300, 2010 May-Jun.
[Is] ISSN:1873-1899
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Oil bodies obtained from oilseeds have been exploited for a variety of applications in biotechnology in the recent past. These applications are based on their non-coalescing nature, ease of extraction and presence of unique membrane proteins-oleosins. In suspension, oil bodies exist as separate entities and, hence, they can serve as emulsifying agent for a wide variety of products, ranging from vaccines, food, cosmetics and personal care products. Oil bodies have found significant uses in the production and purification of recombinant proteins with specific applications. The desired protein can be targeted to oil bodies in oilseeds by affinity tag or by fusing it directly to the N or C terminal of oleosins. Upon targeting, the hydrophobic domain of oleosin embeds into the TAG matrix of oil body, whereas the protein fused with N and/or C termini is exposed on the oil body surface, where it acquires correct confirmation spontaneously. Oil bodies with the attached foreign protein can be separated easily from other cellular components. They can be used directly or the protein can be cleaved from the fusion. The desired protein can be a pharmaceutically important polypeptide (e.g. hirudin, insulin and epidermal growth factor), a neutraceutical polypeptide (somatotropin), a commercially important enzyme (e.g. xylanase), a protein important for improvement of crops (e.g. chitinase) or a multimeric protein. These applications can further be widened as oil bodies can also be made artificially and oleosin gene can be expressed in bacterial systems. Thus, a protein fused to oleosin can be expressed in Escherichia coli and after cell lysis it can be incorporated into artificial oil bodies, thereby facilitating the extraction and purification of the desired protein. Artificial oil bodies can also be used for encapsulation of probiotics. The manipulation of oleosin gene for the expression of polyoleosins has further expanded the arena of the applications of oil bodies in biotechnology.
[Mh] Termos MeSH primário: Biotecnologia/tendências
Glioxissomos/fisiologia
Óleos Vegetais/metabolismo
Proteínas de Plantas/fisiologia
Plantas Geneticamente Modificadas/metabolismo
Engenharia de Proteínas/tendências
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Plant Oils); 0 (Plant Proteins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1006
[Cu] Atualização por classe:100329
[Lr] Data última revisão:
100329
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100114
[St] Status:MEDLINE
[do] DOI:10.1016/j.biotechadv.2010.01.001



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