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[PMID]: 28950028 [Au] Autor: Basak P; Maitra-Majee S; Das JK; Mukherjee A; Ghosh Dastidar S; Pal Choudhury P; Lahiri Majumder A [Ad] Endereço: Division of Plant Biology, Bose Institute (Centenary Campus), Kolkata, West Bengal, India. [Ti] Título: An evolutionary analysis identifies a conserved pentapeptide stretch containing the two essential lysine residues for rice L-myo-inositol 1-phosphate synthase catalytic activity. [So] Source: PLoS One;12(9):e0185351, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: A molecular evolutionary analysis of a well conserved protein helps to determine the essential amino acids in the core catalytic region. Based on the chemical properties of amino acid residues, phylogenetic analysis of a total of 172 homologous sequences of a highly conserved enzyme, L-myo-inositol 1-phosphate synthase or MIPS from evolutionarily diverse organisms was performed. This study revealed the presence of six phylogenetically conserved blocks, out of which four embrace the catalytic core of the functional protein. Further, specific amino acid modifications targeting the lysine residues, known to be important for MIPS catalysis, were performed at the catalytic site of a MIPS from monocotyledonous model plant, Oryza sativa (OsMIPS1). Following this study, OsMIPS mutants with deletion or replacement of lysine residues in the conserved blocks were made. Based on the enzyme kinetics performed on the deletion/replacement mutants, phylogenetic and structural comparison with the already established crystal structures from non-plant sources, an evolutionarily conserved peptide stretch was identified at the active pocket which contains the two most important lysine residues essential for catalytic activity. [Mh] Termos MeSH primário: Evolução Biológica Lisina/metabolismo Mio-Inositol-1-Fosfato Sintase/metabolismo Oligopeptídeos/metabolismo Oryza/enzimologia [Mh] Termos MeSH secundário: Sequência de Aminoácidos Biocatálise Domínio Catalítico Cristalografia por Raios X Mutagênese Sítio-Dirigida Mio-Inositol-1-Fosfato Sintase/química Oligopeptídeos/química Oryza/genética Filogenia Homologia de Sequência de Aminoácidos [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Oligopeptides); EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase); K3Z4F929H6 (Lysine) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171019 [Lr] Data última revisão: 171019 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170927 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0185351

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[PMID]: 28817575 [Au] Autor: Yu W; Daniel J; Mehta D; Maddipati KR; Greenberg ML [Ad] Endereço: Department of Biological Sciences, Wayne State University, Detroit, Michigan, United States of America. [Ti] Título: MCK1 is a novel regulator of myo-inositol phosphate synthase (MIPS) that is required for inhibition of inositol synthesis by the mood stabilizer valproate. [So] Source: PLoS One;12(8):e0182534, 2017. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Myo-inositol, the precursor of all inositol compounds, is essential for the viability of eukaryotes. Identifying the factors that regulate inositol homeostasis is of obvious importance to understanding cell function and the pathologies underlying neurological and metabolic resulting from perturbation of inositol metabolism. The current study identifies Mck1, a GSK3 homolog, as a novel positive regulator of inositol de novo synthesis in yeast. Mck1 was required for normal activity of myo-inositol phosphate synthase (MIPS), which catalyzes the rate-limiting step of inositol synthesis. mck1Δ cells exhibited a 50% decrease in MIPS activity and a decreased rate of incorporation of [13C6]glucose into [13C6]-inositol-3-phosphate and [13C6]-inositol compared to WT cells. mck1Δ cells also exhibited decreased growth in the presence of the inositol depleting drug valproate (VPA), which was rescued by supplementation of inositol. However, in contrast to wild type cells, which exhibited more than a 40% decrease in MIPS activity in the presence of VPA, the drug did not significantly decrease MIPS activity in mck1Δ cells. These findings indicate that VPA-induced MIPS inhibition is Mck1-dependent, and suggest a model that unifies two current hypotheses of the mechanism of action of VPA-inositol depletion and GSK3 inhibition. [Mh] Termos MeSH primário: Antimaníacos/farmacologia Inibidores Enzimáticos/farmacologia Quinase 3 da Glicogênio Sintase/metabolismo Inositol/metabolismo Mio-Inositol-1-Fosfato Sintase/metabolismo Proteínas de Saccharomyces cerevisiae/metabolismo Ácido Valproico/farmacologia [Mh] Termos MeSH secundário: Quinase 3 da Glicogênio Sintase/genética Mio-Inositol-1-Fosfato Sintase/antagonistas & inibidores Saccharomyces cerevisiae/efeitos dos fármacos Saccharomyces cerevisiae/genética Saccharomyces cerevisiae/metabolismo Proteínas de Saccharomyces cerevisiae/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Antimanic Agents); 0 (Enzyme Inhibitors); 0 (Saccharomyces cerevisiae Proteins); 4L6452S749 (Inositol); 614OI1Z5WI (Valproic Acid); EC 2.7.11.26 (Glycogen Synthase Kinase 3); EC 2.7.12.1 (MCK1 protein, S cerevisiae); EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase) [Em] Mês de entrada: 1710 [Cu] Atualização por classe: 171006 [Lr] Data última revisão: 171006 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 170818 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0182534

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[PMID]: 27832122 [Au] Autor: Vigoder FM; Parker DJ; Cook N; Tournière O; Sneddon T; Ritchie MG [Ad] Endereço: Centre for Biological Diversity, School of Biology, University of St Andrews, Fife, United Kingdom. [Ti] Título: Inducing Cold-Sensitivity in the Frigophilic Fly Drosophila montana by RNAi. [So] Source: PLoS One;11(11):e0165724, 2016. [Is] ISSN: 1932-6203 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Cold acclimation is a critical physiological adaptation for coping with seasonal cold. By increasing their cold tolerance individuals can remain active for longer at the onset of winter and can recover more quickly from a cold shock. In insects, despite many physiological studies, little is known about the genetic basis of cold acclimation. Recently, transcriptomic analyses in Drosophila virilis and D. montana revealed candidate genes for cold acclimation by identifying genes upregulated during exposure to cold. Here, we test the role of myo-inositol-1-phosphate synthase (Inos), in cold tolerance in D. montana using an RNAi approach. D. montana has a circumpolar distribution and overwinters as an adult in northern latitudes with extreme cold. We assessed cold tolerance of dsRNA knock-down flies using two metrics: chill-coma recovery time (CCRT) and mortality rate after cold acclimation. Injection of dsRNAInos did not alter CCRT, either overall or in interaction with the cold treatment, however it did induced cold-specific mortality, with high levels of mortality observed in injected flies acclimated at 5°C but not at 19°C. Overall, injection with dsRNAInos induced a temperature-sensitive mortality rate of over 60% in this normally cold-tolerant species. qPCR analysis confirmed that dsRNA injection successfully reduced gene expression of Inos. Thus, our results demonstrate the involvement of Inos in increasing cold tolerance in D. montana. The potential mechanisms involved by which Inos increases cold tolerance are also discussed. [Mh] Termos MeSH primário: Aclimatação Drosophila/genética Drosophila/fisiologia Mio-Inositol-1-Fosfato Sintase/genética [Mh] Termos MeSH secundário: Animais Temperatura Baixa Frio Extremo Feminino Perfilação da Expressão Gênica Regulação da Expressão Gênica Interferência de RNA [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase) [Em] Mês de entrada: 1706 [Cu] Atualização por classe: 170622 [Lr] Data última revisão: 170622 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 161111 [St] Status: MEDLINE [do] DOI: 10.1371/journal.pone.0165724

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[PMID]: 27577857 [Au] Autor: Kudo F; Tsunoda T; Takashima M; Eguchi T [Ad] Endereço: Department of Chemistry, Tokyo Institute of Technology, 2-12-1 O-Okayama, Meguro-ku, Tokyo, 152-8551 (, Japan). [Ti] Título: Five-Membered Cyclitol Phosphate Formation by a myo-Inositol Phosphate Synthase Orthologue in the Biosynthesis of the Carbocyclic Nucleoside Antibiotic Aristeromycin. [So] Source: Chembiochem;17(22):2143-2148, 2016 Nov 17. [Is] ISSN: 1439-7633 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: Aristeromycin is a unique carbocyclic nucleoside antibiotic produced by Streptomyces citricolor. In order to elucidate its intriguing carbocyclic formation, we used a genome-mining approach to identify the responsible enzyme. In silico screening with known cyclitol synthases involved in primary metabolism, such as myo-inositol-1-phosphate synthase (MIPS) and dehydroqunate synthase (DHQS), identified a unique MIPS orthologue (Ari2) encoded in the genome of S. citricolor. Heterologous expression of the gene cluster containing ari2 with a cosmid vector in Streptomyces albus resulted in the production of aristeromycin, thus indicating that the cloned DNA region (37.5 kb) with 33 open reading frames contains its biosynthetic gene cluster. We verified that Ari2 catalyzes the formation of a novel five-membered cyclitol phosphate from d-fructose 6-phosphate (F6P) with NAD as a cofactor. This provides insight into cyclitol phosphate synthase as a member of the MIPS family of enzymes. A biosynthetic pathway to aristeromycin is proposed based on bioinformatics analysis of the gene cluster. [Mh] Termos MeSH primário: Adenosina/análogos & derivados Antibacterianos/biossíntese Proteínas de Bactérias/metabolismo Ciclitóis/metabolismo Mio-Inositol-1-Fosfato Sintase/metabolismo Fósforo-Oxigênio Liases/metabolismo [Mh] Termos MeSH secundário: Adenosina/biossíntese Adenosina/química Antibacterianos/química Proteínas de Bactérias/genética Cosmídeos/genética Cosmídeos/metabolismo Ciclitóis/química Espectroscopia de Ressonância Magnética Família Multigênica Mio-Inositol-1-Fosfato Sintase/genética Nucleosídeos/química Fósforo-Oxigênio Liases/genética Espectrometria de Massas por Ionização por Electrospray Streptomyces coelicolor/enzimologia Streptomyces coelicolor/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Cyclitols); 0 (Nucleosides); 19186-33-5 (aristeromycin); EC 4.2.3.4 (3-dehydroquinate synthetase); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase); K72T3FS567 (Adenosine) [Em] Mês de entrada: 1705 [Cu] Atualização por classe: 170516 [Lr] Data última revisão: 170516 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160901 [St] Status: MEDLINE [do] DOI: 10.1002/cbic.201600348

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[PMID]: 27252471 [Au] Autor: Kalujnaia S; Hazon N; Cramb G [Ad] Endereço: School of Medicine, University of St. Andrews, St. Andrews, United Kingdom; and. [Ti] Título: Myo-inositol phosphate synthase expression in the European eel (Anguilla anguilla) and Nile tilapia (Oreochromis niloticus): effect of seawater acclimation. [So] Source: Am J Physiol Regul Integr Comp Physiol;311(2):R287-98, 2016 Aug 01. [Is] ISSN: 1522-1490 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: A single MIPS gene (Isyna1/Ino1) exists in eel and tilapia genomes with a single myo-d-inositol 3-phosphate synthase (MIPS) transcript identified in all eel tissues, although two MIPS spliced variants [termed MIPS(s) and MIPS(l)] are found in all tilapia tissues. The larger tilapia transcript [MIPS(l)] results from the inclusion of the 87-nucleotide intron between exons 5 and 6 in the genomic sequence. In most tilapia tissues, the MIPS(s) transcript exhibits much higher abundance (generally >10-fold) with the exception of white skeletal muscle and oocytes, in which the MIPS(l) transcript predominates. SW acclimation resulted in large (6- to 32-fold) increases in mRNA expression for both MIPS(s) and MIPS(l) in all tilapia tissues tested, whereas in the eel, changes in expression were limited to a more modest 2.5-fold increase and only in the kidney. Western blots identified a number of species- and tissue-specific immunoreactive MIPS proteins ranging from 40 to 67 kDa molecular weight. SW acclimation failed to affect the abundance of any immunoreactive protein in any tissue tested from the eel. However, a major 67-kDa immunoreactive protein (presumed to be MIPS) found in tilapia tissues exhibited 11- and 54-fold increases in expression in gill and fin samples from SW-acclimated fish. Immunohistochemical investigations revealed specific immunoreactivity in the gill, fin, skin, and intestine taken from only SW-acclimated tilapia. Immunofluorescence indicated that MIPS was expressed within gill chondrocytes and epithelial cells of the primary filaments, basal epithelial cell layers of the skin and fin, the cytosol of columnar intestinal epithelial and mucous cells, as well as unknown entero-endocrine-like cells. [Mh] Termos MeSH primário: Aclimatação/fisiologia Anguilla/fisiologia Mio-Inositol-1-Fosfato Sintase/química Mio-Inositol-1-Fosfato Sintase/metabolismo Água do Mar Tilápia/fisiologia [Mh] Termos MeSH secundário: Animais Ativação Enzimática Regulação Enzimológica da Expressão Gênica/fisiologia Peso Molecular Mio-Inositol-1-Fosfato Sintase/classificação Especificidade de Órgãos Salinidade Especificidade da Espécie [Pt] Tipo de publicação: COMPARATIVE STUDY; JOURNAL ARTICLE [Nm] Nome de substância: EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase) [Em] Mês de entrada: 1706 [Cu] Atualização por classe: 170626 [Lr] Data última revisão: 170626 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160603 [St] Status: MEDLINE [do] DOI: 10.1152/ajpregu.00056.2016

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[PMID]: 27035231 [Au] Autor: Koguchi T; Tanikawa C; Mori J; Kojima Y; Matsuda K [Ad] Endereço: Laboratory of Clinical Sequence, Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Tokyo, Japan. [Ti] Título: Regulation of myo-inositol biosynthesis by p53-ISYNA1 pathway. [So] Source: Int J Oncol;48(6):2415-24, 2016 Jun. [Is] ISSN: 1791-2423 [Cp] País de publicação: Greece [La] Idioma: eng [Ab] Resumo: In response to various cellular stresses, p53 exerts its tumor suppressive effects such as apoptosis, cell cycle arrest, and senescence through the induction of its target genes. Recently, p53 was shown to control cellular homeostasis by regulating energy metabolism, glycolysis, antioxidant effect, and autophagy. However, its function in inositol synthesis was not reported. Through a microarray screening, we found that five genes related with myo-inositol metabolism were induced by p53. DNA damage enhanced intracellular myo-inositol content in HCT116 p53+/+ cells, but not in HCT116 p53-/- cells. We also indicated that inositol 3-phosphate synthase (ISYNA1) which encodes an enzyme essential for myo-inositol biosynthesis as a direct target of p53. Activated p53 regulated ISYNA1 expression through p53 response element in the seventh exon. Ectopic ISYNA1 expression increased myo-inositol levels in the cells and suppressed tumor cell growth. Knockdown of ISYNA1 caused resistance to adriamycin treatment, demonstrating the role of ISYNA1 in p53-mediated growth suppression. Furthermore, ISYNA1 expression was significantly associated with p53 mutation in bladder, breast cancer, head and neck squamous cell carcinoma, lung squamous cell carcinoma, and pancreatic adenocarcinoma. Our findings revealed a novel role of p53 in myo-inositol biosynthesis which could be a potential therapeutic target. [Mh] Termos MeSH primário: Inositol/biossíntese Mio-Inositol-1-Fosfato Sintase/metabolismo Proteína Supressora de Tumor p53/metabolismo [Mh] Termos MeSH secundário: Animais Células HCT116 Células HEK293 Células Hep G2 Seres Humanos Camundongos Camundongos Knockout Mio-Inositol-1-Fosfato Sintase/genética Análise de Sequência com Séries de Oligonucleotídeos RNA Mensageiro/genética RNA Mensageiro/metabolismo Proteína Supressora de Tumor p53/genética [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (RNA, Messenger); 0 (Tumor Suppressor Protein p53); 4L6452S749 (Inositol); EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase) [Em] Mês de entrada: 1703 [Cu] Atualização por classe: 170306 [Lr] Data última revisão: 170306 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160402 [St] Status: MEDLINE [do] DOI: 10.3892/ijo.2016.3456

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[PMID]: 26747283 [Au] Autor: Bruggeman Q; Mazubert C; Prunier F; Lugan R; Chan KX; Phua SY; Pogson BJ; Krieger-Liszkay A; Delarue M; Benhamed M; Bergounioux C; Raynaud C [Ad] Endereço: Institute of Plant Sciences Paris-Saclay (IPS2), UMR 9213/UMR1403, CNRS, INRA, Université Paris-Sud, Université d'Evry, Université Paris-Diderot, Sorbonne Paris-Cité, Bâtiment 630, 91405 Orsay, France (Q.B., C.M., F.P., M.D., M.B., C.B., C.R.);Institut de Biologie Moléculaire des Plantes, Unité Prop [Ti] Título: Chloroplast Activity and 3'phosphadenosine 5'phosphate Signaling Regulate Programmed Cell Death in Arabidopsis. [So] Source: Plant Physiol;170(3):1745-56, 2016 Mar. [Is] ISSN: 1532-2548 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Programmed cell death (PCD) is a crucial process both for plant development and responses to biotic and abiotic stress. There is accumulating evidence that chloroplasts may play a central role during plant PCD as for mitochondria in animal cells, but it is still unclear whether they participate in PCD onset, execution, or both. To tackle this question, we have analyzed the contribution of chloroplast function to the cell death phenotype of the myoinositol phosphate synthase1 (mips1) mutant that forms spontaneous lesions in a light-dependent manner. We show that photosynthetically active chloroplasts are required for PCD to occur in mips1, but this process is independent of the redox state of the chloroplast. Systematic genetic analyses with retrograde signaling mutants reveal that 3'-phosphoadenosine 5'-phosphate, a chloroplast retrograde signal that modulates nuclear gene expression in response to stress, can inhibit cell death and compromises plant innate immunity via inhibition of the RNA-processing 5'-3' exoribonucleases. Our results provide evidence for the role of chloroplast-derived signal and RNA metabolism in the control of cell death and biotic stress response. [Mh] Termos MeSH primário: Difosfato de Adenosina/metabolismo Apoptose/fisiologia Arabidopsis/metabolismo Cloroplastos/metabolismo Transdução de Sinais/fisiologia [Mh] Termos MeSH secundário: Apoptose/genética Arabidopsis/genética Arabidopsis/microbiologia Clorofila/metabolismo Cloroplastos/genética Resistência à Doença/genética Mutação Mio-Inositol-1-Fosfato Sintase/genética Mio-Inositol-1-Fosfato Sintase/metabolismo Oxirredução Fotossíntese/genética Fotossíntese/fisiologia Doenças das Plantas/genética Doenças das Plantas/microbiologia Imunidade Vegetal/genética Pseudomonas syringae/fisiologia Transdução de Sinais/genética [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 1406-65-1 (Chlorophyll); 61D2G4IYVH (Adenosine Diphosphate); C65F80D52U (adenosine 3'-phosphate-5'-phosphate); EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase) [Em] Mês de entrada: 1612 [Cu] Atualização por classe: 171116 [Lr] Data última revisão: 171116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160110 [St] Status: MEDLINE [do] DOI: 10.1104/pp.15.01872

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[PMID]: 26714049 [Au] Autor: Ma L; Tian T; Lin R; Deng XW; Wang H; Li G [Ad] Endereço: State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an 271018, China. [Ti] Título: Arabidopsis FHY3 and FAR1 Regulate Light-Induced myo-Inositol Biosynthesis and Oxidative Stress Responses by Transcriptional Activation of MIPS1. [So] Source: Mol Plant;9(4):541-57, 2016 Apr 04. [Is] ISSN: 1752-9867 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: myo-Inositol-1-phosphate synthase (MIPS) catalyzes the limiting step of inositol biosynthesis and has crucial roles in plant growth and development. In response to stress, the transcription of MIPS1 is induced and the biosynthesis of inositol or inositol derivatives is promoted by unknown mechanisms. Here, we found that the light signaling protein FAR-RED ELONGATED HYPOCOTYL3 (FHY3) and its homolog FAR-RED IMPAIRED RESPONSE1 (FAR1) regulate light-induced inositol biosynthesis and oxidative stress responses by activating the transcription of MIPS1. Disruption of FHY3 and FAR1 caused light-induced cell death after dark-light transition, precocious leaf senescence, and increased sensitivity to oxidative stress. Reduction of salicylic acid (SA) accumulation by overexpression of SALICYLIC ACID 3-HYDROXYLASE largely suppressed the cell death phenotype of fhy3 far1 mutant plants, suggesting that FHY3- and FAR1-mediated cell death is dependent on SA. Furthermore, comparative analysis of chromatin immunoprecipitation sequencing and microarray results revealed that FHY3 and FAR1 directly target both MIPS1 and MIPS2. The fhy3 far1 mutant plants showed severely decreased MIPS1/2 transcript levels and reduced inositol levels. Conversely, constitutive expression of MIPS1 partially rescued the inositol contents, caused reduced transcript levels of SA-biosynthesis genes, and prevented oxidative stress in fhy3 far1. Taken together, our results indicate that the light signaling proteins FHY3 and FAR1 directly bind the promoter of MIPS1 to activate its expression and thereby promote inositol biosynthesis to prevent light-induced oxidative stress and SA-dependent cell death. [Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo Arabidopsis/efeitos da radiação Inositol/biossíntese Luz Mio-Inositol-1-Fosfato Sintase/genética Proteínas Nucleares/metabolismo Estresse Oxidativo/efeitos da radiação Fitocromo/metabolismo [Mh] Termos MeSH secundário: Arabidopsis/genética Arabidopsis/metabolismo Morte Celular/efeitos da radiação Escuridão Regiões Promotoras Genéticas/genética Espécies Reativas de Oxigênio/metabolismo Ativação Transcricional/efeitos da radiação [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Arabidopsis Proteins); 0 (FAR1 protein, Arabidopsis); 0 (FHY3 protein, Arabidopsis); 0 (Nuclear Proteins); 0 (Reactive Oxygen Species); 11121-56-5 (Phytochrome); 4L6452S749 (Inositol); EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase) [Em] Mês de entrada: 1701 [Cu] Atualização por classe: 170116 [Lr] Data última revisão: 170116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 151230 [St] Status: MEDLINE

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[PMID]: 26011089 [Au] Autor: Zhai H; Wang F; Si Z; Huo J; Xing L; An Y; He S; Liu Q [Ad] Endereço: Beijing Key Laboratory of Crop Genetic Improvement/Laboratory of Crop Heterosis and Utilization, Ministry of Education, China Agricultural University, Beijing, China. [Ti] Título: A myo-inositol-1-phosphate synthase gene, IbMIPS1, enhances salt and drought tolerance and stem nematode resistance in transgenic sweet potato. [So] Source: Plant Biotechnol J;14(2):592-602, 2016 Feb. [Is] ISSN: 1467-7652 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Myo-inositol-1-phosphate synthase (MIPS) is a key rate limiting enzyme in myo-inositol biosynthesis. The MIPS gene has been shown to improve tolerance to abiotic stresses in several plant species. However, its role in resistance to biotic stresses has not been reported. In this study, we found that expression of the sweet potato IbMIPS1 gene was induced by NaCl, polyethylene glycol (PEG), abscisic acid (ABA) and stem nematodes. Its overexpression significantly enhanced stem nematode resistance as well as salt and drought tolerance in transgenic sweet potato under field conditions. Transcriptome and real-time quantitative PCR analyses showed that overexpression of IbMIPS1 up-regulated the genes involved in inositol biosynthesis, phosphatidylinositol (PI) and ABA signalling pathways, stress responses, photosynthesis and ROS-scavenging system under salt, drought and stem nematode stresses. Inositol, inositol-1,4,5-trisphosphate (IP3 ), phosphatidic acid (PA), Ca(2+) , ABA, K(+) , proline and trehalose content was significantly increased, whereas malonaldehyde (MDA), Na(+) and H2 O2 content was significantly decreased in the transgenic plants under salt and drought stresses. After stem nematode infection, the significant increase of inositol, IP3 , PA, Ca(2+) , ABA, callose and lignin content and significant reduction of MDA content were found, and a rapid increase of H2 O2 levels was observed, peaked at 1 to 2 days and thereafter declined in the transgenic plants. This study indicates that the IbMIPS1 gene has the potential to be used to improve the resistance to biotic and abiotic stresses in plants. [Mh] Termos MeSH primário: Adaptação Fisiológica Secas Ipomoea batatas/enzimologia Mio-Inositol-1-Fosfato Sintase/genética Nematoides/fisiologia Caules de Planta/parasitologia Tolerância a Sal/efeitos dos fármacos Cloreto de Sódio/farmacologia [Mh] Termos MeSH secundário: Ácido Abscísico/farmacologia Adaptação Fisiológica/efeitos dos fármacos Adaptação Fisiológica/genética Animais Resistência à Doença/efeitos dos fármacos Genes de Plantas Ipomoea batatas/genética Ipomoea batatas/parasitologia Ipomoea batatas/fisiologia Mio-Inositol-1-Fosfato Sintase/metabolismo Nematoides/efeitos dos fármacos Doenças das Plantas/parasitologia Caules de Planta/efeitos dos fármacos Plantas Geneticamente Modificadas Polietilenoglicóis/farmacologia Tolerância a Sal/genética Transdução de Sinais/efeitos dos fármacos Estresse Fisiológico/efeitos dos fármacos Regulação para Cima/efeitos dos fármacos Regulação para Cima/genética [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 30IQX730WE (Polyethylene Glycols); 451W47IQ8X (Sodium Chloride); 72S9A8J5GW (Abscisic Acid); EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase) [Em] Mês de entrada: 1612 [Cu] Atualização por classe: 161230 [Lr] Data última revisão: 161230 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150527 [St] Status: MEDLINE [do] DOI: 10.1111/pbi.12402

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[PMID]: 25346288 [Au] Autor: Liu X; Lai Y; Sun H; Wang Y; Zou N [Ad] Endereço: School of Life Sciences, Ludong University, Yantai 264025, People's Republic of China. [Ti] Título: The interactive effects of mercury and selenium on metabolic profiles, gene expression and antioxidant enzymes in halophyte Suaeda salsa. [So] Source: Environ Toxicol;31(4):440-51, 2016 Apr. [Is] ISSN: 1522-7278 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Suaeda salsa is the pioneer halophyte in the Yellow River Delta and was consumed as a popular vegetable. Mercury has become a highly risky contaminant in the sediment of intertidal zones of the Yellow River Delta. In this work, we investigated the interactive effects of mercury and selenium in S. salsa on the basis of metabolic profiling, antioxidant enzyme activities and gene expression quantification. Our results showed that mercury exposure (20 µg L(-1)) inhibited plant growth of S. salsa and induced significant metabolic responses and altered expression levels of INPS, CMO, and MDH in S. salsa samples, together with the increased activities of antioxidant enzymes including SOD and POD. Overall, these results indicated osmotic and oxidative stresses, disturbed protein degradation and energy metabolism change in S. salsa after mercury exposures. Additionally, the addition of selenium could induce both antagonistic and synergistic effects including alleviating protein degradation and aggravating osmotic stress caused by mercury. [Mh] Termos MeSH primário: Chenopodiaceae/efeitos dos fármacos Mercúrio/toxicidade Plantas Tolerantes a Sal/efeitos dos fármacos Selênio/farmacologia [Mh] Termos MeSH secundário: Chenopodiaceae/crescimento & desenvolvimento Chenopodiaceae/metabolismo Expressão Gênica/efeitos dos fármacos Malato Desidrogenase (NADP+)/genética Metaboloma Metabolômica Mio-Inositol-1-Fosfato Sintase/genética Estresse Oxidativo Oxigenases/genética Peroxidase/metabolismo Proteínas de Plantas/genética Proteínas de Plantas/metabolismo Plantas Tolerantes a Sal/crescimento & desenvolvimento Plantas Tolerantes a Sal/metabolismo Superóxido Dismutase/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Plant Proteins); EC 1.- (choline monooxygenase); EC 1.1.1.82 (Malate Dehydrogenase (NADP+)); EC 1.11.1.7 (Peroxidase); EC 1.13.- (Oxygenases); EC 1.15.1.1 (Superoxide Dismutase); EC 5.5.1.4 (Myo-Inositol-1-Phosphate Synthase); FXS1BY2PGL (Mercury); H6241UJ22B (Selenium) [Em] Mês de entrada: 1610 [Cu] Atualização por classe: 161230 [Lr] Data última revisão: 161230 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 141028 [St] Status: MEDLINE [do] DOI: 10.1002/tox.22057

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