Base de dados : MEDLINE
Pesquisa : B03.440.400.450 [Categoria DeCS]
Referências encontradas : 148 [refinar]
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  1 / 148 MEDLINE  
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[PMID]:29424215
[Au] Autor:Chesnokova MG; Shalai VV; Kraus YA; Mironov AY; Blinova EG
[Ti] Título:[Informative indices of the biocorrosion activity for the determination of the character of the aggression ground].
[So] Source:Gig Sanit;95(6):513-7, 2016.
[Is] ISSN:0016-9900
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Underground corrosion is referred to the most difficult types of corrosion in connection with that it is multifactorial and differs in progressive dynamics of the participation of each parameter in the process of destruction of the metal. With the aim of the evaluation of the informativeness of the index of the biocorrosion activity caused by the influence of various factors to determine the character of the soil aggressiveness in the district of pipeline laying there was studied the complex of microbiological and physical-chemical indices). There was determined the amount of sulfur cycle bacteria (autotrophic thiobacteria and sulphate-reducing bacteria), the total concentration of sulfur and iron in the soil samples adjacent to the surface of the underground pipelines in the territory of the Khanty-Mansi Autonomous District of Yugra, and the ratio of these indices with a specific electrical resistance of the soil. There was established the predominance ofsamples with weak aggressiveness of the soil (55.17% of cases), with the criterion ofbiocorrosion soil activity of 2,44 ± 0,19. The results show significant differences in the thiobacteria content and mobile iron in the studied soil-ground samples. There was revealed a direct correlation of the average force of concentrations of identified bacteria and iron content in the soil. There was shown the necessity of the implementation of dynamic control and the development of methods of protection of metal structures to prevent biocorrosion in the design and in the process of the operation of the pipeline.
[Mh] Termos MeSH primário: Fenômenos Bioquímicos
Fenômenos Biofísicos
Microbiologia do Solo
Solo/química
[Mh] Termos MeSH secundário: Corrosão
Ecossistema
Bactérias Gram-Negativas Quimiolitotróficas/isolamento & purificação
Bactérias Redutoras de Enxofre/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Soil)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180210
[St] Status:MEDLINE


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[PMID]:28791907
[Au] Autor:Del Prete S; Perfetto R; Rossi M; Alasmary FAS; Osman SM; AlOthman Z; Supuran CT; Capasso C
[Ad] Endereço:a Dipartimento di Scienze Bio-Agroalimentari, CNR-Istituto di Bioscienze e Biorisorse , CNR , Napoli , Italy.
[Ti] Título:A one-step procedure for immobilising the thermostable carbonic anhydrase (SspCA) on the surface membrane of Escherichia coli.
[So] Source:J Enzyme Inhib Med Chem;32(1):1120-1128, 2017 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The carbonic anhydrase superfamily (CA, EC 4.2.1.1) of metalloenzymes is present in all three domains of life (Eubacteria, Archaea, and Eukarya), being an interesting example of convergent/divergent evolution, with its seven families (α-, ß-, γ-, δ-, ζ-, η-, and θ-CAs) described so far. CAs catalyse the simple, but physiologically crucial reaction of carbon dioxide hydration to bicarbonate and protons. Recently, our groups characterised the α-CA from the thermophilic bacterium, Sulfurihydrogenibium yellowstonense finding a very high catalytic activity for the CO hydration reaction (k = 9.35 × 10 s and k /K = 1.1 × 10 M s ) which was maintained after heating the enzyme at 80 °C for 3 h. This highly thermostable SspCA was covalently immobilised within polyurethane foam and onto the surface of magnetic Fe O nanoparticles. Here, we describe a one-step procedure for immobilising the thermostable SspCA directly on the surface membrane of Escherichia coli, using the INPN domain of Pseudomonas syringae. This strategy has clear advantages with respect to other methods, which require as the first step the production and the purification of the biocatalyst, and as the second step the immobilisation of the enzyme onto a specific support. Our results demonstrate that thermostable SspCA fused to the INPN domain of P. syringae ice nucleation protein (INP) was correctly expressed on the outer membrane of engineered E. coli cells, affording for an easy approach to design biotechnological applications for this highly effective thermostable catalyst.
[Mh] Termos MeSH primário: Proteínas da Membrana Bacteriana Externa/metabolismo
Anidrases Carbônicas/metabolismo
Escherichia coli/metabolismo
Bactérias Gram-Negativas Quimiolitotróficas/enzimologia
Temperatura Ambiente
[Mh] Termos MeSH secundário: Relação Estrutura-Atividade
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); EC 4.2.1.1 (Carbonic Anhydrases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2017.1355794


  3 / 148 MEDLINE  
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[PMID]:28497711
[Au] Autor:Perfetto R; Del Prete S; Vullo D; Sansone G; Barone CMA; Rossi M; Supuran CT; Capasso C
[Ad] Endereço:a Istituto di Bioscienze e Biorisorse, CNR , Napoli , Italy.
[Ti] Título:Production and covalent immobilisation of the recombinant bacterial carbonic anhydrase (SspCA) onto magnetic nanoparticles.
[So] Source:J Enzyme Inhib Med Chem;32(1):759-766, 2017 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Carbonic anhydrases (CAs; EC 4.2.1.1) are metalloenzymes with a pivotal potential role in the biomimetic CO capture process (CCP) because these biocatalysts catalyse the simple but physiologically crucial reaction of carbon dioxide hydration to bicarbonate and protons in all life kingdoms. The CAs are among the fastest known enzymes, with k values of up to 10 s for some members of the superfamily, providing thus advantages when compared with other CCP methods, as they are specific for CO . Thermostable CAs might be used in CCP technology because of their ability to perform catalysis in operatively hard conditions, typical of the industrial processes. Moreover, the improvement of the enzyme stability and its reuse are important for lowering the costs. These aspects can be overcome by immobilising the enzyme on a specific support. We report in this article that the recombinant thermostable SspCA (α-CA) from the thermophilic bacterium Sulfurihydrogenibium yellowstonense can been heterologously produced by a high-density fermentation of Escherichia coli cultures, and covalently immobilised onto the surface of magnetic Fe O nanoparticles (MNP) via carbodiimide activation reactions. Our results demonstrate that using a benchtop bioprocess station and strategies for optimising the bacterial growth, it is possible to produce at low cost a large amount SspCA. Furthermore, the enzyme stability and storage greatly increased through the immobilisation, as SspCA bound to MNP could be recovered from the reaction mixture by simply using a magnet or an electromagnetic field, due to the strong ferromagnetic properties of Fe O .
[Mh] Termos MeSH primário: Anidrases Carbônicas/biossíntese
Bactérias Gram-Negativas Quimiolitotróficas/enzimologia
Nanopartículas de Magnetita/química
[Mh] Termos MeSH secundário: Anidrases Carbônicas/metabolismo
Bactérias Gram-Negativas Quimiolitotróficas/crescimento & desenvolvimento
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Magnetite Nanoparticles); 0 (Recombinant Proteins); EC 4.2.1.1 (Carbonic Anhydrases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170513
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2017.1316719


  4 / 148 MEDLINE  
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[PMID]:23279131
[Au] Autor:Hamamura N; Meneghin J; Reysenbach AL
[Ad] Endereço:Center for Marine Environmental Studies, Ehime University, Matsuyama, Ehime, 790-8577, Japan. nhama@ehimeu.ac.jp
[Ti] Título:Comparative community gene expression analysis of Aquificales-dominated geothermal springs.
[So] Source:Environ Microbiol;15(4):1226-37, 2013 Apr.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Members of Sulfurihydrogenibium are often observed as visible filamentous biomass in circumneutral hot springs and play roles in sulfur-cycling, hydrogen oxidation and iron mineralization. To gain insight into the ecophysiology of Sulfurihydrogenibium populations, we conducted preliminary metatranscriptomic analysis of three distinct thermal springs; Calcite Springs (YNP-CS) and Mammoth Springs (YNP-MHS) in Yellowstone National Park, USA, and Furnas Springs (AZ) in Azores, Portugal. Genes to which transcripts were assigned revealed commonly expressed functions among the sites, while several differences were also observed. All three sites, Sulfurihydrogenibium spp. dominate and are obtaining energy via metabolism of sulfur compounds under microaerophilic conditions. Cell motility was one of the expressed functions in two sites (YNP-CS and AZ) with slower stream flow rates and thicker well-formed biofilms. The transcripts from YNP-CS and -MHS exhibited varying levels of sequence divergence from the reference genomes and corresponding metagenomes, suggesting the presence of microdiversity among Sulfurihydrogenibium populations in situ. Conversely, the majority of the AZ transcripts were identical to the S. azorense genome. Our initial results show that the metatranscriptomes in these similar Aquificales-dominated communities can reveal community-level gene function in geochemically distinct thermal environments.
[Mh] Termos MeSH primário: Bactérias Gram-Negativas Quimiolitotróficas/classificação
Bactérias Gram-Negativas Quimiolitotróficas/genética
Fontes Termais/microbiologia
Metagenoma
[Mh] Termos MeSH secundário: Biomassa
DNA Complementar/análise
Regulação Bacteriana da Expressão Gênica
Variação Genética
Filogenia
Portugal
Especificidade da Espécie
Estados Unidos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (DNA, Complementary)
[Em] Mês de entrada:1307
[Cu] Atualização por classe:130405
[Lr] Data última revisão:
130405
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130103
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.12061


  5 / 148 MEDLINE  
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[PMID]:22999416
[Au] Autor:Vullo D; De Luca V; Scozzafava A; Carginale V; Rossi M; Supuran CT; Capasso C
[Ad] Endereço:Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Sesto Fiorentino, Florence, Italy.
[Ti] Título:The first activation study of a bacterial carbonic anhydrase (CA). The thermostable α-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines.
[So] Source:Bioorg Med Chem Lett;22(20):6324-7, 2012 Oct 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The α-carbonic anhydrase (CA, EC 4.2.1.1) from the newly discovered thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 (SspCA) was investigated for its activation with a series of amino acids and amines. D-His, L-Phe, L-Tyr, L- and D-Trp were the most effective SspCA activators, with activation constants in the range of 1-12 nM, whereas L-His, L/D-DOPA, D-Tyr, and several biogenic amines/catecholamines were slightly less effective activators (K(A) in the range of 37 nM-0.97 µM). The least effective SspCA activator was d-Phe (K(A) of 5.13 µM). The thermal stability, robustness and very high catalytic activity of SspCA make this enzyme an ideal candidate for biomimetic CO(2) capture processes.
[Mh] Termos MeSH primário: Anidrases Carbônicas/metabolismo
Bactérias Gram-Negativas Quimiolitotróficas/enzimologia
[Mh] Termos MeSH secundário: Aminas/metabolismo
Aminoácidos/metabolismo
Dióxido de Carbono/metabolismo
Ativação Enzimática
Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amines); 0 (Amino Acids); 142M471B3J (Carbon Dioxide); EC 4.2.1.1 (Carbonic Anhydrases)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120925
[St] Status:MEDLINE


  6 / 148 MEDLINE  
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[PMID]:22835873
[Au] Autor:De Luca V; Vullo D; Scozzafava A; Carginale V; Rossi M; Supuran CT; Capasso C
[Ad] Endereço:Istituto di Biochimica delle Proteine-CNR, Via P. Castellino 111, 80131 Napoli, Italy.
[Ti] Título:Anion inhibition studies of an α-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1.
[So] Source:Bioorg Med Chem Lett;22(17):5630-4, 2012 Sep 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The newly discovered thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 encodes an α-carbonic anhydrases (CAs, EC 4.2.1.1) which is highly catalytically active and thermostable. Here we report the inhibition of this enzyme, denominated SspCA, with inorganic and complex anions and other molecules interacting with zinc proteins. SspCA was inhibited in the micromolar range by diethyldithiocarbamate, sulfamide, sulfamic acid, phenylboronic and phenylarsonic acid, trithiocarbonate and selenocyanide (K(I)s of 4-70 µM) and in the submillimolar one by iodide, cyanide, (thio)cyanate, hydrogen sulfide, azide, nitrate, nitrite, many complex anions incorporating heavy metal ions and iminodisulfonate (K(I)s of 0.48-0.86 mM). SspCA was not substantially inhibited by bicarbonate and carbonate, hydrogensulfite and peroxidisulfate (K(I)s in the range of 21.1-84.6mM). The exceptional thermostability and lack of strong affinity for hydrogensulfide, bicarbonate, and carbonate make this enzyme an interesting candidate for biotechnological applications of enzymatic CO(2) fixation.
[Mh] Termos MeSH primário: Inibidores da Anidrase Carbônica/química
Inibidores da Anidrase Carbônica/farmacologia
Anidrases Carbônicas/metabolismo
Bactérias Gram-Negativas Quimiolitotróficas/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Ânions/química
Ânions/farmacologia
Anidrases Carbônicas/química
Infecções por Bactérias Gram-Negativas/tratamento farmacológico
Bactérias Gram-Negativas Quimiolitotróficas/efeitos dos fármacos
Seres Humanos
Dados de Sequência Molecular
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anions); 0 (Carbonic Anhydrase Inhibitors); EC 4.2.1.1 (Carbonic Anhydrases)
[Em] Mês de entrada:1301
[Cu] Atualização por classe:120820
[Lr] Data última revisão:
120820
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120728
[St] Status:MEDLINE
[do] DOI:10.1016/j.bmcl.2012.06.106


  7 / 148 MEDLINE  
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[PMID]:22803664
[Au] Autor:Capasso C; De Luca V; Carginale V; Cannio R; Rossi M
[Ad] Endereço:CNR, Istituto di Biochimica delle Proteine (IBP), Napoli, Italy. c.capasso@ibp.cnr.it
[Ti] Título:Biochemical properties of a novel and highly thermostable bacterial α-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1.
[So] Source:J Enzyme Inhib Med Chem;27(6):892-7, 2012 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A new carbonic anhydrase (CA, EC 4.2.1.1) from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 was identified and characterized. The bacterial carbonic anhydrase gene was expressed in Escherichia coli yielding an active enzyme, which was purified in large amounts. The recombinant protein (SspCA) was found to belong to the α-CA class and displays esterase activity. The kinetic parameters were determined by using CO(2) and p-nitrophenylacetate (p-NpA) as substrates. The bacterial enzyme presented specific activity comparable to that of bovine carbonic anhydrase (bCA II) but it showed biochemical properties never observed for the mammalian enzyme. The thermophilic enzyme, in fact, was endowed with high thermostability and with unaltered residual activity after prolonged exposure to heat up to 100°C. SspCA and the bovine carbonic anhydrase (bCA II) were immobilized within a polyurethane (PU) foam. The immobilized bacterial enzyme was found to be active and stable at 100°C up to 50 h.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Dióxido de Carbono/química
Anidrases Carbônicas/química
Bactérias Gram-Negativas Quimiolitotróficas/química
Nitrofenóis/química
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/isolamento & purificação
Anidrase Carbônica II/química
Anidrases Carbônicas/isolamento & purificação
Bovinos
Eletroforese em Gel de Poliacrilamida
Ensaios Enzimáticos
Estabilidade Enzimática
Escherichia coli/genética
Bactérias Gram-Negativas Quimiolitotróficas/enzimologia
Temperatura Alta
Proteínas Imobilizadas/química
Proteínas Imobilizadas/isolamento & purificação
Cinética
Poliuretanos
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Immobilized Proteins); 0 (Nitrophenols); 0 (Polyurethanes); 0 (Recombinant Proteins); 142M471B3J (Carbon Dioxide); 830-03-5 (4-nitrophenyl acetate); 9009-54-5 (polyurethane foam); EC 4.2.1.- (Carbonic Anhydrase II); EC 4.2.1.1 (Carbonic Anhydrases)
[Em] Mês de entrada:1306
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120719
[St] Status:MEDLINE
[do] DOI:10.3109/14756366.2012.703185


  8 / 148 MEDLINE  
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[PMID]:22199218
[Au] Autor:Slobodkin AI; Reysenbach AL; Slobodkina GB; Baslerov RV; Kostrikina NA; Wagner ID; Bonch-Osmolovskaya EA
[Ad] Endereço:Winogradsky Institute of Microbiology, Russian Academy of Sciences, Prospect 60-letiya Oktyabrya 7/2, 117312 Moscow, Russia. aslobodkin@hotmail.com
[Ti] Título:Thermosulfurimonas dismutans gen. nov., sp. nov., an extremely thermophilic sulfur-disproportionating bacterium from a deep-sea hydrothermal vent.
[So] Source:Int J Syst Evol Microbiol;62(Pt 11):2565-71, 2012 Nov.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An extremely thermophilic, anaerobic, chemolithoautotrophic bacterium (strain S95(T)) was isolated from a deep-sea hydrothermal vent chimney located on the Eastern Lau Spreading Center, Pacific Ocean, at a depth of 1910 m. Cells of strain S95(T) were oval to short Gram-negative rods, 0.5-0.6 µm in diameter and 1.0-1.5 µm in length, growing singly or in pairs. Cells were motile with a single polar flagellum. The temperature range for growth was 50-92 °C, with an optimum at 74 °C. The pH range for growth was 5.5-8.0, with an optimum at pH 7.0. Growth of strain S95(T) was observed at NaCl concentrations ranging from 1.5 to 3.5% (w/v). Strain S95(T) grew anaerobically with elemental sulfur as an energy source and bicarbonate/CO(2) as a carbon source. Elemental sulfur was disproportionated to sulfide and sulfate. Growth was enhanced in the presence of poorly crystalline iron(III) oxide (ferrihydrite) as a sulfide-scavenging agent. Strain S95(T) was also able to grow by disproportionation of thiosulfate and sulfite. Sulfate was not used as an electron acceptor. Analysis of the 16S rRNA gene sequence revealed that the isolate belongs to the phylum Thermodesulfobacteria. On the basis of its physiological properties and results of phylogenetic analyses, it is proposed that the isolate represents the sole species of a new genus, Thermosulfurimonas dismutans gen. nov., sp. nov.; S95(T) (=DSM 24515(T)=VKM B-2683(T)) is the type strain of the type species. This is the first description of a thermophilic micro-organism that disproportionates elemental sulfur.
[Mh] Termos MeSH primário: Fontes Hidrotermais/microbiologia
Filogenia
Bactérias Redutoras de Enxofre/classificação
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Composição de Bases
DNA Bacteriano/genética
Bactérias Gram-Negativas Quimiolitotróficas/classificação
Bactérias Gram-Negativas Quimiolitotróficas/genética
Bactérias Gram-Negativas Quimiolitotróficas/isolamento & purificação
Dados de Sequência Molecular
Oceano Pacífico
RNA Ribossômico 16S/genética
Água do Mar/microbiologia
Análise de Sequência de DNA
Enxofre/metabolismo
Bactérias Redutoras de Enxofre/genética
Bactérias Redutoras de Enxofre/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (RNA, Ribosomal, 16S); 70FD1KFU70 (Sulfur)
[Em] Mês de entrada:1303
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111227
[St] Status:MEDLINE
[do] DOI:10.1099/ijs.0.034397-0


  9 / 148 MEDLINE  
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[PMID]:21138449
[Au] Autor:Lebedeva EV; Off S; Zumbrägel S; Kruse M; Shagzhina A; Lücker S; Maixner F; Lipski A; Daims H; Spieck E
[Ad] Endereço:Winogradsky Institute of Microbiology, Russian Academy of Sciences, Moscow, Russia.
[Ti] Título:Isolation and characterization of a moderately thermophilic nitrite-oxidizing bacterium from a geothermal spring.
[So] Source:FEMS Microbiol Ecol;75(2):195-204, 2011 Feb.
[Is] ISSN:1574-6941
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Geothermal environments are a suitable habitat for nitrifying microorganisms. Conventional and molecular techniques indicated that chemolithoautotrophic nitrite-oxidizing bacteria affiliated with the genus Nitrospira are widespread in environments with elevated temperatures up to 55 °C in Asia, Europe, and Australia. However, until now, no thermophilic pure cultures of Nitrospira were available, and the physiology of these bacteria was mostly uncharacterized. Here, we report on the isolation and characterization of a novel thermophilic Nitrospira strain from a microbial mat of the terrestrial geothermal spring Gorjachinsk (pH 8.6; temperature 48 °C) from the Baikal rift zone (Russia). Based on phenotypic properties, chemotaxonomic data, and 16S rRNA gene phylogeny, the isolate was assigned to the genus Nitrospira as a representative of a novel species, for which the name Nitrospira calida is proposed. A highly similar 16S rRNA gene sequence (99.6% similarity) was detected in a Garga spring enrichment grown at 46 °C, whereas three further thermophilic Nitrospira enrichments from the Garga spring and from a Kamchatka Peninsula (Russia) terrestrial hot spring could be clearly distinguished from N. calida (93.6-96.1% 16S rRNA gene sequence similarity). The findings confirmed that Nitrospira drive nitrite oxidation in moderate thermophilic habitats and also indicated an unexpected diversity of heat-adapted Nitrospira in geothermal hot springs.
[Mh] Termos MeSH primário: Bactérias Gram-Negativas Quimiolitotróficas/isolamento & purificação
Fontes Termais/microbiologia
Nitritos/metabolismo
[Mh] Termos MeSH secundário: DNA Bacteriano/genética
Bactérias Gram-Negativas Quimiolitotróficas/classificação
Bactérias Gram-Negativas Quimiolitotróficas/genética
Bactérias Gram-Negativas Quimiolitotróficas/metabolismo
Temperatura Alta
Nitrificação
Oxirredução
Filogenia
RNA Ribossômico 16S/genética
Federação Russa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Nitrites); 0 (RNA, Ribosomal, 16S)
[Em] Mês de entrada:1102
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:101209
[St] Status:MEDLINE
[do] DOI:10.1111/j.1574-6941.2010.01006.x


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[PMID]:20421637
[Au] Autor:Valanne S; Myllymäki H; Kallio J; Schmid MR; Kleino A; Murumägi A; Airaksinen L; Kotipelto T; Kaustio M; Ulvila J; Esfahani SS; Engström Y; Silvennoinen O; Hultmark D; Parikka M; Rämet M
[Ad] Endereço:Institute of Medical Technology, University of Tampere, Tampere, Finland.
[Ti] Título:Genome-wide RNA interference in Drosophila cells identifies G protein-coupled receptor kinase 2 as a conserved regulator of NF-kappaB signaling.
[So] Source:J Immunol;184(11):6188-98, 2010 Jun 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Because NF-kappaB signaling pathways are highly conserved in evolution, the fruit fly Drosophila melanogaster provides a good model to study these cascades. We carried out an RNA interference (RNAi)-based genome-wide in vitro reporter assay screen in Drosophila for components of NF-kappaB pathways. We analyzed 16,025 dsRNA-treatments and identified 10 novel NF-kappaB regulators. Of these, nine dsRNA-treatments affect primarily the Toll pathway. G protein-coupled receptor kinase (Gprk)2, CG15737/Toll pathway activation mediating protein, and u-shaped were required for normal Drosomycin response in vivo. Interaction studies revealed that Gprk2 interacts with the Drosophila IkappaB homolog Cactus, but is not required in Cactus degradation, indicating a novel mechanism for NF-kappaB regulation. Morpholino silencing of the zebrafish ortholog of Gprk2 in fish embryos caused impaired cytokine expression after Escherichia coli infection, indicating a conserved role in NF-kappaB signaling. Moreover, small interfering RNA silencing of the human ortholog GRK5 in HeLa cells impaired NF-kappaB reporter activity. Gprk2 RNAi flies are susceptible to infection with Enterococcus faecalis and Gprk2 RNAi rescues Toll(10b)-induced blood cell activation in Drosophila larvae in vivo. We conclude that Gprk2/GRK5 has an evolutionarily conserved role in regulating NF-kappaB signaling.
[Mh] Termos MeSH primário: Proteínas de Drosophila/imunologia
Quinase 2 de Receptor Acoplado a Proteína G/imunologia
Quinase 5 de Receptor Acoplado a Proteína G/metabolismo
Imunidade Inata
NF-kappa B/imunologia
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Drosophila
Proteínas de Drosophila/metabolismo
Quinase 2 de Receptor Acoplado a Proteína G/metabolismo
Quinase 5 de Receptor Acoplado a Proteína G/imunologia
Bactérias Gram-Negativas Quimiolitotróficas/imunologia
Bactérias Gram-Negativas Quimiolitotróficas/metabolismo
Seres Humanos
Imuno-Histoquímica
Imunoprecipitação
NF-kappa B/metabolismo
Interferência de RNA
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (NF-kappa B); EC 2.7.11.16 (G-Protein-Coupled Receptor Kinase 2); EC 2.7.11.16 (G-Protein-Coupled Receptor Kinase 5); EC 2.7.11.16 (Gprk2 protein, Drosophila)
[Em] Mês de entrada:1006
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:100428
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1000261



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