Base de dados : MEDLINE
Pesquisa : B02.200.850 [Categoria DeCS]
Referências encontradas : 78 [refinar]
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[PMID]:27476211
[Au] Autor:Bulaev AG; Sukhacheva MV; Kuznetsov BB
[Ti] Título:[Typing of the Closely Related Strains of Euryarchaeal Genus Acidiplasma (Thermoplasmatales) Using REP-PCR DNA Fingerprinting Technique].
[So] Source:Mikrobiologiia;85(2):223-6, 2016 Mar-Apr.
[Is] ISSN:0026-3656
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Mh] Termos MeSH primário: Impressões Digitais de DNA/métodos
DNA Arqueal/genética
Reação em Cadeia da Polimerase/métodos
Thermoplasmales
[Mh] Termos MeSH secundário: Thermoplasmales/classificação
Thermoplasmales/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Archaeal)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160801
[Lr] Data última revisão:
160801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160802
[St] Status:MEDLINE


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[PMID]:27472444
[Au] Autor:Li N; Wang H; Li L; Cheng H; Liu D; Cheng H; Deng Z
[Ti] Título:Integrated Approach To Producing High-Purity Trehalose from Maltose by the Yeast Yarrowia lipolytica Displaying Trehalose Synthase (TreS) on the Cell Surface.
[So] Source:J Agric Food Chem;64(31):6179-87, 2016 Aug 10.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An alternative strategy that integrated enzyme production, trehalose biotransformation, and bioremoval in one bioreactor was developed in this study, thus simplifying the traditional procedures used for trehalose production. The trehalose synthase gene from a thermophilic archaea, Picrophilus torridus, was first fused to the YlPir1 anchor gene and then inserted into the genome of Yarrowia lipolytica, thus yielding an engineered yeast strain. The trehalose yield reached 73% under optimal conditions. The thermal and pH stabilities of the displayed enzyme were improved compared to those of its free form purified from recombinant Escherichia coli. After biotransformation, the glucose byproduct and residual maltose were directly fermented to ethanol by a Saccharomyces cerevisiae strain. Ethanol can be separated by distillation, and high-purity trehalose can easily be obtained from the fermentation broth. The results show that this one-pot procedure is an efficient approach to the economical production of trehalose from maltose.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Glucosiltransferases/metabolismo
Maltose/metabolismo
Thermoplasmales/enzimologia
Trealose/metabolismo
Yarrowia/metabolismo
[Mh] Termos MeSH secundário: Proteínas Arqueais/química
Proteínas Arqueais/genética
Estabilidade Enzimática
Etanol/metabolismo
Fermentação
Glucose/metabolismo
Glucosiltransferases/química
Glucosiltransferases/genética
Thermoplasmales/genética
Yarrowia/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 3K9958V90M (Ethanol); 69-79-4 (Maltose); B8WCK70T7I (Trehalose); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.- (trehalose synthase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160730
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.6b02175


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[PMID]:27094682
[Au] Autor:Aihara T; Ito T; Yamanaka Y; Noguchi K; Odaka M; Sekine M; Homma H; Yohda M
[Ad] Endereço:Department of Biotechnology and Life Science, Graduate School of Technology, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo, 184-8588, Japan.
[Ti] Título:Structural and functional characterization of aspartate racemase from the acidothermophilic archaeon Picrophilus torridus.
[So] Source:Extremophiles;20(4):385-93, 2016 Jul.
[Is] ISSN:1433-4909
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Functional and structural characterizations of pyridoxal 5'-phosphate-independent aspartate racemase of the acidothermophilic archaeon Picrophilus torridus were performed. Picrophilus aspartate racemase exhibited high substrate specificity to aspartic acid. The optimal reaction temperature was 60 °C, which is almost the same as the optimal growth temperature. Reflecting the low pH in the cytosol, the optimal reaction pH of Picrophilus aspartate racemase was approximately 5.5. However, the activity at the putative cytosolic pH of 4.6 was approximately 6 times lower than that at the optimal pH of 5.5. The crystal structure of Picrophilus aspartate racemase was almost the same as that of other pyridoxal 5'-phosphate -independent aspartate racemases. In two molecules of the dimer, one molecule contained a tartaric acid molecule in the catalytic site; the structure of the other molecule was relatively flexible. Finally, we examined the intracellular existence of D-amino acids. Unexpectedly, the proportion of D-aspartate to total aspartate was not very high. In contrast, both D-proline and D-alanine were observed. Because Picrophilus aspartate racemase is highly specific to aspartate, other amino acid racemases might exist in Picrophilus torridus.
[Mh] Termos MeSH primário: Isomerases de Aminoácido/química
Proteínas Arqueais/química
Thermoplasmales/enzimologia
[Mh] Termos MeSH secundário: Isomerases de Aminoácido/genética
Isomerases de Aminoácido/metabolismo
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Estabilidade Enzimática
Especificidade por Substrato
Thermoplasmales/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); EC 5.1.1.- (Amino Acid Isomerases); EC 5.1.1.13 (aspartate racemase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:160421
[St] Status:MEDLINE
[do] DOI:10.1007/s00792-016-0829-7


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[PMID]:26518885
[Au] Autor:Golyshina OV; Lünsdorf H; Kublanov IV; Goldenstein NI; Hinrichs KU; Golyshin PN
[Ad] Endereço:1​ School of Biological Sciences, Bangor University, Deiniol Rd, Bangor LL57 2UW, UK.
[Ti] Título:The novel extremely acidophilic, cell-wall-deficient archaeon Cuniculiplasma divulgatum gen. nov., sp. nov. represents a new family, Cuniculiplasmataceae fam. nov., of the order Thermoplasmatales.
[So] Source:Int J Syst Evol Microbiol;66(1):332-40, 2016 Jan.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Two novel cell-wall-less, acidophilic, mesophilic, organotrophic and facultatively anaerobic archaeal strains were isolated from acidic streamers formed on the surfaces of copper-ore-containing sulfidic deposits in south-west Spain and North Wales, UK. Cells of the strains varied from 0.1 to 2 µm in size and were pleomorphic, with a tendency to form filamentous structures. The optimal pH and temperature for growth for both strains were 1.0-1.2 and 37-40 °C, with the optimal substrates for growth being beef extract (3 g l- 1) for strain S5T and beef extract with tryptone (3 and 1 g l- 1, respectively) for strain PM4. The lipid composition was dominated by intact polar lipids consisting of a glycerol dibiphytanyl glycerol tetraether (GDGT) core attached to predominantly glycosidic polar headgroups. In addition, free GDGT and small relative amounts of intact and core diether lipids were present. Strains S5T and PM4 possessed mainly menaquinones with minor fractions of thermoplasmaquinones. The DNA G+C content was 37.3 mol% in strain S5T and 37.16 mol% for strain PM4. A similarity matrix of 16S rRNA gene sequences (identical for both strains) showed their affiliation to the order Thermoplasmatales, with 73.9-86.3 % identity with sequences from members of the order with validly published names. The average nucleotide identity between genomes of the strains determined in silico was 98.75 %, suggesting, together with the 16S rRNA gene-based phylogenetic analysis, that the strains belong to the same species. A novel family, Cuniculiplasmataceae fam. nov., genus Cuniculiplasma gen. nov. and species Cuniculiplasma divulgatum sp. nov. are proposed based on the phylogenetic, chemotaxonomic analyses and physiological properties of the two isolates, S5T and PM4 ( = JCM 30641 = VKM B-2940). The type strain of Cuniculiplasma divulgatum is S5T ( = JCM 30642T = VKM B-2941T).
[Mh] Termos MeSH primário: Filogenia
Thermoplasmales/classificação
Microbiologia da Água
[Mh] Termos MeSH secundário: Composição de Bases
Parede Celular/química
DNA Arqueal/genética
Lipídeos/química
Mineração
Dados de Sequência Molecular
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Espanha
Thermoplasmales/genética
Thermoplasmales/isolamento & purificação
Reino Unido
Vitamina K 2/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Archaeal); 0 (Lipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151101
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.000725


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[PMID]:26026939
[Au] Autor:von der Heyde A; Lockhauserbäumer J; Uetrecht C; Elleuche S
[Ad] Endereço:Hamburg University of Technology (TUHH), Institute of Technical Microbiology, Kasernenstr. 12, 21073, Hamburg, Germany.
[Ti] Título:A hydrolase-based reporter system to uncover the protein splicing performance of an archaeal intein.
[So] Source:Appl Microbiol Biotechnol;99(18):7613-24, 2015 Sep.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Extein amino acid residues around the splice site junctions affect the functionality of inteins. To identify an optimal sequence context for efficient protein splicing of an intein from the thermoacidophilic archaeon Picrophilus torridus, single extein amino acid residues at the splice site junctions were continuously deleted. The construction of a set of different truncated extein variants showed that this intein tolerates multiple amino acid variations near the excision sites and exhibits full activity when -1 and +1 extein amino acid residues are conserved in an artificial GST-intein-HIS fusion construct. Moreover, splicing of the recombinant intein took place at temperatures between 4 and 42 °C with high efficiency, when produced in Escherichia coli. Therefore, structural model predictions were used to identify optimal insertion sites for the intein to be embedded within a hemicellulase from the psychrophilic bacterium Pseudoalteromonas arctica. The P. torridus intein inserted before amino acid residue Thr75 of the reporter enzyme retained catalytic activity. Moreover, the catalytic activity of the xylan-degrading hydrolase could be easily monitored in routine plate assays and in liquid test measurements at room temperature when produced in recombinant form in E. coli. This tool allows the indirect detection of the intein's catalytic activity to be used in screenings.
[Mh] Termos MeSH primário: Genes Reporter
Hidrolases/genética
Hidrolases/metabolismo
Inteínas
Processamento de Proteína
Thermoplasmales/enzimologia
Thermoplasmales/genética
[Mh] Termos MeSH secundário: Escherichia coli/genética
Escherichia coli/metabolismo
Pseudoalteromonas/genética
Pseudoalteromonas/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 3.- (Hydrolases)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:150821
[Lr] Data última revisão:
150821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150601
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-015-6689-8


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[PMID]:25896560
[Au] Autor:Castelle CJ; Roger M; Bauzan M; Brugna M; Lignon S; Nimtz M; Golyshina OV; Giudici-Orticoni MT; Guiral M
[Ad] Endereço:CNRS, Aix Marseille Université, BIP UMR 7281, FR 3479, 13402 Marseille, France.
[Ti] Título:The aerobic respiratory chain of the acidophilic archaeon Ferroplasma acidiphilum: A membrane-bound complex oxidizing ferrous iron.
[So] Source:Biochim Biophys Acta;1847(8):717-28, 2015 Aug.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The extremely acidophilic archaeon Ferroplasma acidiphilum is found in iron-rich biomining environments and is an important micro-organism in naturally occurring microbial communities in acid mine drainage. F. acidiphilum is an iron oxidizer that belongs to the order Thermoplasmatales (Euryarchaeota), which harbors the most extremely acidophilic micro-organisms known so far. At present, little is known about the nature or the structural and functional organization of the proteins in F. acidiphilum that impact the iron biogeochemical cycle. We combine here biochemical and biophysical techniques such as enzyme purification, activity measurements, proteomics and spectroscopy to characterize the iron oxidation pathway(s) in F. acidiphilum. We isolated two respiratory membrane protein complexes: a 850 kDa complex containing an aa3-type cytochrome oxidase and a blue copper protein, which directly oxidizes ferrous iron and reduces molecular oxygen, and a 150 kDa cytochrome ba complex likely composed of a di-heme cytochrome and a Rieske protein. We tentatively propose that both of these complexes are involved in iron oxidation respiratory chains, functioning in the so-called uphill and downhill electron flow pathways, consistent with autotrophic life. The cytochrome ba complex could possibly play a role in regenerating reducing equivalents by a reverse ('uphill') electron flow. This study constitutes the first detailed biochemical investigation of the metalloproteins that are potentially directly involved in iron-mediated energy conservation in a member of the acidophilic archaea of the genus Ferroplasma.
[Mh] Termos MeSH primário: Proteínas Arqueais/metabolismo
Membrana Celular/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Compostos Ferrosos/química
Complexos Multiproteicos/metabolismo
Oxigênio/metabolismo
Thermoplasmales/classificação
[Mh] Termos MeSH secundário: Ácidos/química
Aerobiose/fisiologia
Proteínas Arqueais/química
Membrana Celular/química
Transporte de Elétrons
Complexo IV da Cadeia de Transporte de Elétrons/química
Compostos Ferrosos/metabolismo
Complexos Multiproteicos/química
Óperon
Oxirredução
Thermoplasmales/crescimento & desenvolvimento
Thermoplasmales/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acids); 0 (Archaeal Proteins); 0 (Ferrous Compounds); 0 (Multiprotein Complexes); EC 1.9.3.1 (Electron Transport Complex IV); S88TT14065 (Oxygen)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150422
[St] Status:MEDLINE


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[PMID]:25762096
[Au] Autor:Goswami K; Arora J; Saha S
[Ad] Endereço:Department of Microbiology, University of Delhi South Campus, Benito Juarez Road, New Delhi 110021, India.
[Ti] Título:Characterization of the MCM homohexamer from the thermoacidophilic euryarchaeon Picrophilus torridus.
[So] Source:Sci Rep;5:9057, 2015 Mar 12.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The typical archaeal MCM exhibits helicase activity independently in vitro. This study characterizes MCM from the euryarchaeon Picrophilus torridus. While PtMCM hydrolyzes ATP in DNA-independent manner, it displays very poor ability to unwind DNA independently, and then too only under acidic conditions. The protein exists stably in complex with PtGINS in whole cell lysates, interacting directly with PtGINS under neutral and acidic conditions. GINS strongly activates MCM helicase activity, but only at low pH. In consonance with this, PtGINS activates PtMCM-mediated ATP hydrolysis only at low pH, with the amount of ATP hydrolyzed during the helicase reaction increasing more than fifty-fold in the presence of GINS. While the stimulation of MCM-mediated helicase activity by GINS has been reported in MCMs from P.furiosus, T.kodakarensis, and very recently, T.acidophilum, to the best of our knowledge, this is the first report of an MCM helicase demonstrating DNA unwinding activity only at such acidic pH, across all archaea and eukaryotes. PtGINS may induce/stabilize a conducive conformation of PtMCM under acidic conditions, favouring PtMCM-mediated DNA unwinding coupled to ATP hydrolysis. Our findings underscore the existence of divergent modes of replication regulation among archaea and the importance of investigating replication events in more archaeal organisms.
[Mh] Termos MeSH primário: Proteínas de Manutenção de Minicromossomo/genética
Proteínas de Manutenção de Minicromossomo/metabolismo
Thermoplasmales/genética
Thermoplasmales/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Clonagem Molecular
DNA/genética
DNA/metabolismo
DNA Helicases/química
DNA Helicases/genética
DNA Helicases/metabolismo
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Ativação Enzimática
Expressão Gênica
Concentração de Íons de Hidrogênio
Hidrólise
Proteínas de Manutenção de Minicromossomo/química
Ligação Proteica
Multimerização Proteica
Estabilidade Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 8L70Q75FXE (Adenosine Triphosphate); 9007-49-2 (DNA); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (Minichromosome Maintenance Proteins)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:151027
[Lr] Data última revisão:
151027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150313
[St] Status:MEDLINE
[do] DOI:10.1038/srep09057


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[PMID]:25636853
[Au] Autor:Rossoni L; Hall SJ; Eastham G; Licence P; Stephens G
[Ad] Endereço:Department of Chemical and Environmental Engineering, Biorenewables and Bioprocessing Research Group, University of Nottingham, Nottingham, United Kingdom enxlr@nottingham.ac.uk.
[Ti] Título:The Putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene.
[So] Source:Appl Environ Microbiol;81(7):2625-34, 2015 Apr.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mevalonate diphosphate decarboxylase (MVD) is an ATP-dependent enzyme that catalyzes the phosphorylation/decarboxylation of (R)-mevalonate-5-diphosphate to isopentenyl pyrophosphate in the mevalonate (MVA) pathway. MVD is a key enzyme in engineered metabolic pathways for bioproduction of isobutene, since it catalyzes the conversion of 3-hydroxyisovalerate (3-HIV) to isobutene, an important platform chemical. The putative homologue from Picrophilus torridus has been identified as a highly efficient variant in a number of patents, but its detailed characterization has not been reported. In this study, we have successfully purified and characterized the putative MVD from P. torridus. We discovered that it is not a decarboxylase per se but an ATP-dependent enzyme, mevalonate-3-kinase (M3K), which catalyzes the phosphorylation of MVA to mevalonate-3-phosphate. The enzyme's potential in isobutene formation is due to the conversion of 3-HIV to an unstable 3-phosphate intermediate that undergoes consequent spontaneous decarboxylation to form isobutene. Isobutene production rates were as high as 507 pmol min(-1) g cells(-1) using Escherichia coli cells expressing the enzyme and 2,880 pmol min(-1) mg protein(-1) with the purified histidine-tagged enzyme, significantly higher than reported previously. M3K is a key enzyme of the novel MVA pathway discovered very recently in Thermoplasma acidophilum. We suggest that P. torridus metabolizes MVA by the same pathway.
[Mh] Termos MeSH primário: Alcenos/metabolismo
Carboxiliases/metabolismo
Ácido Mevalônico/análogos & derivados
Ácido Mevalônico/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Thermoplasmales/enzimologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Carboxiliases/genética
Carboxiliases/isolamento & purificação
Clonagem Molecular
Escherichia coli/enzimologia
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Fosfotransferases (Aceptor do Grupo Álcool)/isolamento & purificação
Thermoplasmales/genética
Valeratos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Alkenes); 0 (Valerates); 1189-94-2 (phosphomevalonic acid); 3F752311CD (beta-hydroxyisovaleric acid); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.36 (mevalonate kinase); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.33 (pyrophosphomevalonate decarboxylase); QA2LMR467H (isobutylene); S5UOB36OCZ (Mevalonic Acid)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150201
[St] Status:MEDLINE
[do] DOI:10.1128/AEM.04033-14


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[PMID]:25504621
[Au] Autor:Merino MP; Andrews BA; Asenjo JA
[Ad] Endereço:Dept. of Chemical Engineering and Biotechnology, Centre for Biotechnology and Bioengineering, CeBiB, University of Chile, Beauchef, 850, Santiago, Chile.
[Ti] Título:Stoichiometric model and flux balance analysis for a mixed culture of Leptospirillum ferriphilum and Ferroplasma acidiphilum.
[So] Source:Biotechnol Prog;31(2):307-15, 2015 Mar-Apr.
[Is] ISSN:1520-6033
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The oxidation process of sulfide minerals in natural environments is achieved by microbial communities from the Archaea and Bacteria domains. A metabolic reconstruction of two dominant species, Leptospirillum ferriphilum and Ferroplasma acidiphilum, which are always found together as a mixed culture in this natural environments, was made. The metabolic model, composed of 152 internal reactions and 29 transport reactions, describes the main interactions between these species, assuming that both use ferrous iron as energy source, and F. acidiphilum takes advantage of the organic compounds secreted by L. ferriphilum for chemomixotrophic growth. A first metabolic model for a mixed culture used in bacterial leaching is proposed in this article, which pretends to represent the characteristics of the mixed culture in a simplified manner. It was evaluated with experimental data through flux balance analysis (FBA) using as objective function the maximization of biomass. The growth yields on ferrous iron obtained for each microorganism are consistent with experimental data, and the flux distribution obtained allows understanding of the metabolic capabilities of both microorganisms growing together in a bioleaching process. The model was used to simulate the growth of F. acidiphilum on different substrates, to determine in silico which compounds maximize cell growth, and which are essential. Knockout simulations were carried out for L. ferriphilum and F. acidiphilum metabolic models, predicting key enzymes of central metabolism. The results of this analysis are consistent with experimental data from literature, showing a robust behavior of the metabolic model.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Ferro/metabolismo
Análise do Fluxo Metabólico/métodos
Modelos Biológicos
Thermoplasmales/metabolismo
[Mh] Termos MeSH secundário: Técnicas de Cocultura
Engenharia Metabólica
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
E1UOL152H7 (Iron)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:150423
[Lr] Data última revisão:
150423
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141216
[St] Status:MEDLINE
[do] DOI:10.1002/btpr.2028


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[PMID]:25142282
[Au] Autor:Xie W; Zhang CL; Wang J; Chen Y; Zhu Y; de la Torre JR; Dong H; Hartnett HE; Hedlund BP; Klotz MG
[Ad] Endereço:State Key Laboratory of Marine Geology, Tongji University, Shanghai, 200092, China; Department of Marine Sciences, University of Georgia, Athens, GA, 30602, USA.
[Ti] Título:Distribution of ether lipids and composition of the archaeal community in terrestrial geothermal springs: impact of environmental variables.
[So] Source:Environ Microbiol;17(5):1600-14, 2015 May.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Archaea can respond to changes in the environment by altering the composition of their membrane lipids, for example, by modification of the abundance and composition of glycerol dialkyl glycerol tetraethers (GDGTs). Here, we investigated the abundance and proportions of polar GDGTs (P-GDGTs) and core GDGTs (C-GDGTs) sampled in different seasons from Tengchong hot springs (Yunnan, China), which encompassed a pH range of 2.5-10.1 and a temperature range of 43.7-93.6°C. The phylogenetic composition of the archaeal community (reanalysed from published work) divided the Archaea in spring sediment samples into three major groups that corresponded with spring pH: acidic, circumneutral and alkaline. Cluster analysis showed correlation between spring pH and the composition of P- and C-GDGTs and archaeal 16S rRNA genes, indicating an intimate link between resident Archaea and the distribution of P- and C-GDGTs in Tengchong hot springs. The distribution of GDGTs in Tengchong springs was also significantly affected by temperature; however, the relationship was weaker than with pH. Analysis of published datasets including samples from Tibet, Yellowstone and the US Great Basin hot springs revealed a similar relationship between pH and GDGT content. Specifically, low pH springs had higher concentrations of GDGTs with high numbers of cyclopentyl rings than neutral and alkaline springs, which is consistent with the predominance of high cyclopentyl ring-characterized Sulfolobales and Thermoplasmatales present in some of the low pH springs. Our study suggests that the resident Archaea in these hot springs are acclimated if not adapted to low pH by their genetic capacity to effect the packing density of their membranes by increasing cyclopentyl rings in GDGTs at the rank of community.
[Mh] Termos MeSH primário: Archaea/metabolismo
Sedimentos Geológicos/microbiologia
Éteres de Glicerila/metabolismo
Fontes Termais/microbiologia
Lipídeos de Membrana/metabolismo
[Mh] Termos MeSH secundário: Archaea/genética
Desulfurococcales/genética
Desulfurococcales/isolamento & purificação
Meio Ambiente
Éteres de Glicerila/análise
Concentração de Íons de Hidrogênio
Lipídeos de Membrana/análise
Oxigênio/metabolismo
Filogenia
RNA Ribossômico 16S/genética
Estações do Ano
Microbiologia do Solo
Sulfolobales/genética
Sulfolobales/isolamento & purificação
Temperatura Ambiente
Thermoplasmales/genética
Thermoplasmales/isolamento & purificação
Tibet
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Glyceryl Ethers); 0 (Membrane Lipids); 0 (RNA, Ribosomal, 16S); S88TT14065 (Oxygen)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:150427
[Lr] Data última revisão:
150427
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140822
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.12595



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