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[PMID]:27771364
[Au] Autor:Loder AJ; Han Y; Hawkins AB; Lian H; Lipscomb GL; Schut GJ; Keller MW; Adams MWW; Kelly RM
[Ad] Endereço:Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, United States.
[Ti] Título:Reaction kinetic analysis of the 3-hydroxypropionate/4-hydroxybutyrate CO fixation cycle in extremely thermoacidophilic archaea.
[So] Source:Metab Eng;38:446-463, 2016 11.
[Is] ISSN:1096-7184
[Cp] País de publicação:Belgium
[La] Idioma:eng
[Ab] Resumo:The 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle fixes CO in extremely thermoacidophilic archaea and holds promise for metabolic engineering because of its thermostability and potentially rapid pathway kinetics. A reaction kinetics model was developed to examine the biological and biotechnological attributes of the 3HP/4HB cycle as it operates in Metallosphaera sedula, based on previous information as well as on kinetic parameters determined here for recombinant versions of five of the cycle enzymes (malonyl-CoA/succinyl-CoA reductase, 3-hydroxypropionyl-CoA synthetase, 3-hydroxypropionyl-CoA dehydratase, acryloyl-CoA reductase, and succinic semialdehyde reductase). The model correctly predicted previously observed features of the cycle: the 35-65% split of carbon flux through the acetyl-CoA and succinate branches, the high abundance and relative ratio of acetyl-CoA/propionyl-CoA carboxylase (ACC) and MCR, and the significance of ACC and hydroxybutyryl-CoA synthetase (HBCS) as regulated control points for the cycle. The model was then used to assess metabolic engineering strategies for incorporating CO into chemical intermediates and products of biotechnological importance: acetyl-CoA, succinate, and 3-hydroxypropionate.
[Mh] Termos MeSH primário: Dióxido de Carbono/metabolismo
Hidroxibutiratos/metabolismo
Ácido Láctico/análogos & derivados
Análise do Fluxo Metabólico/métodos
Redes e Vias Metabólicas/fisiologia
Modelos Biológicos
Sulfolobaceae/metabolismo
[Mh] Termos MeSH secundário: Archaea/metabolismo
Extremófilos/metabolismo
Cinética
Ácido Láctico/metabolismo
Taxa de Depuração Metabólica
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Hydroxybutyrates); 142M471B3J (Carbon Dioxide); 30IW36W5B2 (4-hydroxybutyric acid); 33X04XA5AT (Lactic Acid); C4ZF6XLD2X (hydracrylic acid)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


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[PMID]:28629504
[Au] Autor:Sakai HD; Kurosawa N
[Ad] Endereço:Department of Science and Engineering for Sustainable Innovation, Faculty of Science and Engineering, Soka University, 1-236 Tangi-machi, Hachioji, Tokyo 192-8577, Japan.
[Ti] Título:Sulfodiicoccus acidiphilus gen. nov., sp. nov., a sulfur-inhibited thermoacidophilic archaeon belonging to the order Sulfolobales isolated from a terrestrial acidic hot spring.
[So] Source:Int J Syst Evol Microbiol;67(6):1880-1886, 2017 Jun.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A novel thermoacidophilic archaeon, strain HS-1T, was isolated from the Hakone Ohwaku-dani hot spring in Japan. Cells of strain HS-1T in exponential phase were cocci to irregular cocci with a diameter of 0.8-1.5 µm. The strain grew within a temperature range of 50-70 °C (optimal: 65-70 °C), a pH range of pH 1.4-5.5 (optimal: pH 3.0-3.5) and a NaCl concentration range of 0-2.5 % (w/v). The novel strain grew in aerobic conditions but did not grow anaerobically. Moreover, this strain utilized various complex substrates (beef extract, casamino acids, peptone, tryptone and yeast extract) and sugars (arabinose, xylose, galactose, glucose, maltose, sucrose, raffinose and lactose) as sole carbon sources. No chemolithoautotrophic growth occurred on elemental sulfur, pyrite, K2S4O6, Na2S2O3 or FeSO4 . 7H2O; however, growth by the oxidation of hydrogen occurred weakly. The core lipids were calditoglycerocaldarchaeol (CGTE) and caldarchaeol (DGTE). The DNA G+C content of the strain was 52.0 mol%, which was remarkably higher than those of known species of the order Sulfolobales(31-46.2 %). The growth of the strain was significantly inhibited in the presence of elemental sulfur. Analyses of 16S rRNA and 23S rRNA gene sequences showed that HS-1T belonged to the order Sulfolobales; however, it was distantly related to all known species of the order Sulfolobales (less than 89 % sequence similarity). On the basis of these results, we propose the novel genus, Sulfodiicoccus, in the order Sulfolobales (in the family Sulfolobaceae). The type species of the genus is Sulfodiicoccus acidiphilus sp. nov., and the type strain of the species is HS-1T (=JCM 31740T=InaCC Ar79T).
[Mh] Termos MeSH primário: Fontes Termais/microbiologia
Filogenia
Sulfolobaceae/classificação
[Mh] Termos MeSH secundário: Crescimento Quimioautotrófico
DNA Arqueal/genética
Temperatura Alta
Japão
Lipídeos/química
RNA Ribossômico 16S/genética
RNA Ribossômico 23S/genética
Análise de Sequência de DNA
Sulfolobaceae/genética
Sulfolobaceae/isolamento & purificação
Enxofre
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Archaeal); 0 (Lipids); 0 (RNA, Ribosomal, 16S); 0 (RNA, Ribosomal, 23S); 70FD1KFU70 (Sulfur)
[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:170621
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.001881


  3 / 66 MEDLINE  
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[PMID]:28213285
[Au] Autor:Li Q; Sand W
[Ad] Endereço:Biofilm Centre, Aquatische Biotechnologie, Universität Duisburg-Essen, Universitätsstraße 5, 45141 Essen, Germany.
[Ti] Título:Mechanical and chemical studies on EPS from Sulfobacillus thermosulfidooxidans: from planktonic to biofilm cells.
[So] Source:Colloids Surf B Biointerfaces;153:34-40, 2017 May 01.
[Is] ISSN:1873-4367
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Bacteria attach to minerals and form biofilms, which can initiate and enhance bioleaching. Extracellular polymeric substances (EPS) play a crucial role during the whole process. Little is known how the cell surface/EPS mechanically and chemically respond to transformation from planktonic to biofilm cells. In this study the attachment and biofilm formation by Sulfobacillus thermosulfidooxidans were followed during pyrite leaching. Adhesiveness and stiffness of the cell/biofilm and the pyrite surface were checked by atomic force microscopy (AFM) in force mapping mode under real living conditions. The EPS components were analysed by colorimetry, fourier transform infrared spectroscopy and energy dispersive X-ray spectroscopy. The results indicate that slimy and soft EPS heterogeneously accumulated in the biofilms and on the surface of pyrite to induce bacterial adhesion and form robust biofilms. After attaching to the pyrite surface, the cells started to change the components of their EPS. Huge amounts of humic substances were detected in the biofilm EPS.
[Mh] Termos MeSH primário: Biofilmes
Plâncton
Polímeros/química
Sulfolobaceae/química
[Mh] Termos MeSH secundário: Microscopia de Força Atômica
Tamanho da Partícula
Sulfolobaceae/metabolismo
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polymers)
[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:170219
[St] Status:MEDLINE


  4 / 66 MEDLINE  
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[PMID]:27520549
[Au] Autor:Ai C; McCarthy S; Eckrich V; Rudrappa D; Qiu G; Blum P
[Ad] Endereço:School of Biological Sciences, University of Nebraska-Lincoln, E234 Beadle Center for Genetics, 1901 Vine St., Lincoln, NE, 68588-0666, USA.
[Ti] Título:Increased acid resistance of the archaeon, Metallosphaera sedula by adaptive laboratory evolution.
[So] Source:J Ind Microbiol Biotechnol;43(10):1455-65, 2016 Oct.
[Is] ISSN:1476-5535
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Extremely thermoacidophilic members of the Archaea such as the lithoautotroph, Metallosphaera sedula, are among the most acid resistant forms of life and are of great relevance in bioleaching. Here, adaptive laboratory evolution was used to enhance the acid resistance of this organism while genomics and transcriptomics were used in an effort to understand the molecular basis for this trait. Unlike the parental strain, the evolved derivative, M. sedula SARC-M1, grew well at pH of 0.90. Enargite (Cu3AsS4) bioleaching conducted at pH 1.20 demonstrated SARC-M1 leached 23.78 % more copper relative to the parental strain. Genome re-sequencing identified two mutations in SARC-M1 including a nonsynonymous mutation in Msed_0408 (an amino acid permease) and a deletion in pseudogene Msed_1517. Transcriptomic studies by RNA-seq of wild type and evolved strains at various low pH values demonstrated there was enhanced expression of genes in M. sedula SARC-M1 encoding membrane complexes and enzymes that extrude protons or that catalyze proton-consuming reactions. In addition, M. sedula SARC-M1 exhibited reduced expression of genes encoding enzymes that catalyze proton-generating reactions. These unique genomic and transcriptomic features support a model for increased acid resistance arising from enhanced control over cytoplasmic pH.
[Mh] Termos MeSH primário: Sulfolobaceae/genética
[Mh] Termos MeSH secundário: Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Cobre/metabolismo
Evolução Molecular Direcionada
Perfilação da Expressão Gênica
Genômica
Processos Heterotróficos
Concentração de Íons de Hidrogênio
Mutação
Sulfolobaceae/crescimento & desenvolvimento
Sulfolobaceae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 789U1901C5 (Copper)
[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:160814
[St] Status:MEDLINE
[do] DOI:10.1007/s10295-016-1812-0


  5 / 66 MEDLINE  
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[PMID]:27315782
[Au] Autor:Lian H; Zeldes BM; Lipscomb GL; Hawkins AB; Han Y; Loder AJ; Nishiyama D; Adams MW; Kelly RM
[Ad] Endereço:Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27587.
[Ti] Título:Ancillary contributions of heterologous biotin protein ligase and carbonic anhydrase for CO incorporation into 3-hydroxypropionate by metabolically engineered Pyrococcus furiosus.
[So] Source:Biotechnol Bioeng;113(12):2652-2660, 2016 Dec.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acetyl-Coenzyme A carboxylase (ACC), malonyl-CoA reductase (MCR), and malonic semialdehyde reductase (MRS) convert HCO and acetyl-CoA into 3-hydroxypropionate (3HP) in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation cycle resident in the extremely thermoacidophilic archaeon Metallosphaera sedula. These three enzymes, when introduced into the hyperthermophilic archaeon Pyrococcus furiosus, enable production of 3HP from maltose and CO . Sub-optimal function of ACC was hypothesized to be limiting for production of 3HP, so accessory enzymes carbonic anhydrase (CA) and biotin protein ligase (BPL) from M. sedula were produced recombinantly in Escherichia coli to assess their function. P. furiosus lacks a native, functional CA, while the M. sedula CA (Msed_0390) has a specific activity comparable to other microbial versions of this enzyme. M. sedula BPL (Msed_2010) was shown to biotinylate the ß-subunit (biotin carboxyl carrier protein) of the ACC in vitro. Since the native BPLs in E. coli and P. furiosus may not adequately biotinylate the M. sedula ACC, the carboxylase was produced in P. furiosus by co-expression with the M. sedula BPL. The baseline production strain, containing only the ACC, MCR, and MSR, grown in a CO -sparged bioreactor reached titers of approximately 40 mg/L 3HP. Strains in which either the CA or BPL accessory enzyme from M. sedula was added to the pathway resulted in improved titers, 120 or 370 mg/L, respectively. The addition of both M. sedula CA and BPL, however, yielded intermediate titers of 3HP (240 mg/L), indicating that the effects of CA and BPL on the engineered 3HP pathway were not additive, possible reasons for which are discussed. While further efforts to improve 3HP production by regulating gene dosage, improving carbon flux and optimizing bioreactor operation are needed, these results illustrate the ancillary benefits of accessory enzymes for incorporating CO into 3HP production in metabolically engineered P. furiosus, and hint at the important role that CA and BPL likely play in the native 3HP/4HB pathway in M. sedula. Biotechnol. Bioeng. 2016;113: 2652-2660. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Dióxido de Carbono/metabolismo
Carbono-Nitrogênio Ligases/metabolismo
Anidrases Carbônicas/genética
Proteínas de Escherichia coli/metabolismo
Ácido Láctico/análogos & derivados
Engenharia Metabólica/métodos
Pyrococcus furiosus/fisiologia
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Dióxido de Carbono/química
Ácido Láctico/biossíntese
Ácido Láctico/química
Engenharia de Proteínas/métodos
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Sulfolobaceae/genética
Sulfolobaceae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Recombinant Proteins); 0 (Repressor Proteins); 142M471B3J (Carbon Dioxide); 33X04XA5AT (Lactic Acid); C4ZF6XLD2X (hydracrylic acid); EC 4.2.1.1 (Carbonic Anhydrases); EC 6.3.- (Carbon-Nitrogen Ligases); EC 6.3.4.15 (birA protein, E coli)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160619
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26033


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[PMID]:27300329
[Au] Autor:Ye Z; Li X; Cheng Y; Liu Z; Tan G; Zhu F; Fu S; Deng Z; Liu T
[Ad] Endereço:Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, Wuhan University School of Pharmaceutical Sciences, Wuhan, 430071, People's Republic of China.
[Ti] Título:Evaluation of 3-hydroxypropionate biosynthesis in vitro by partial introduction of the 3-hydroxypropionate/4-hydroxybutyrate cycle from Metallosphaera sedula.
[So] Source:J Ind Microbiol Biotechnol;43(9):1313-21, 2016 Sep.
[Is] ISSN:1476-5535
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The chemical 3-hydroxypropionate (3HP) is an important starting reagent for the commercial synthesis of specialty chemicals. In this study, a part of the 3-hydroxypropionate/4-hydroxybutyrate cycle from Metallosphaera sedula was utilized for 3HP production. To study the basic biochemistry of this pathway, an in vitro-reconstituted system was established using acetyl-CoA as the substrate for the kinetic analysis of this system. The results indicated that 3HP formation was sensitive to acetyl-CoA carboxylase and malonyl-CoA reductase, but not malonate semialdehyde reductase. Also, the competition between 3HP formation and fatty acid production was analyzed both in vitro and in vivo. This study has highlighted how metabolic flux is controlled by different catalytic components. We believe that this reconstituted system would be valuable for understanding 3HP biosynthesis pathway and for future engineering studies to enhance 3HP production.
[Mh] Termos MeSH primário: Ácido Láctico/análogos & derivados
Oxibato de Sódio/metabolismo
Sulfolobaceae/metabolismo
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Acetil-CoA Carboxilase/metabolismo
Vias Biossintéticas
Ciclo do Carbono
Cinética
Ácido Láctico/biossíntese
Oxirredutases/metabolismo
Sulfolobaceae/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
33X04XA5AT (Lactic Acid); 72-89-9 (Acetyl Coenzyme A); 7G33012534 (Sodium Oxybate); C4ZF6XLD2X (hydracrylic acid); EC 1.- (Oxidoreductases); EC 1.- (malonyl-Coa reductase); EC 6.4.1.2 (Acetyl-CoA Carboxylase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160615
[St] Status:MEDLINE
[do] DOI:10.1007/s10295-016-1793-z


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[PMID]:27280585
[Au] Autor:Leger MM; Eme L; Hug LA; Roger AJ
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS, Canada.
[Ti] Título:Novel Hydrogenosomes in the Microaerophilic Jakobid Stygiella incarcerata.
[So] Source:Mol Biol Evol;33(9):2318-36, 2016 Sep.
[Is] ISSN:1537-1719
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrion-related organelles (MROs) have arisen independently in a wide range of anaerobic protist lineages. Only a few of these organelles and their functions have been investigated in detail, and most of what is known about MROs comes from studies of parasitic organisms such as the parabasalid Trichomonas vaginalis Here, we describe the MRO of a free-living anaerobic jakobid excavate, Stygiella incarcerata We report an RNAseq-based reconstruction of S. incarcerata's MRO proteome, with an associated biochemical map of the pathways predicted to be present in this organelle. The pyruvate metabolism and oxidative stress response pathways are strikingly similar to those found in the MROs of other anaerobic protists, such as Pygsuia and Trichomonas This elegant example of convergent evolution is suggestive of an anaerobic biochemical 'module' of prokaryotic origins that has been laterally transferred among eukaryotes, enabling them to adapt rapidly to anaerobiosis. We also identified genes corresponding to a variety of mitochondrial processes not found in Trichomonas, including intermembrane space components of the mitochondrial protein import apparatus, and enzymes involved in amino acid metabolism and cardiolipin biosynthesis. In this respect, the MROs of S. incarcerata more closely resemble those of the much more distantly related free-living organisms Pygsuia biforma and Cantina marsupialis, likely reflecting these organisms' shared lifestyle as free-living anaerobes.
[Mh] Termos MeSH primário: Eucariotos/genética
Organelas/metabolismo
[Mh] Termos MeSH secundário: Anaerobiose
Evolução Biológica
Eucariotos/metabolismo
Evolução Molecular
Membranas Intracelulares/metabolismo
Mitocôndrias/metabolismo
Filogenia
Proteoma
Proteínas de Protozoários/genética
Análise de Sequência de RNA/métodos
Sulfolobaceae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteome); 0 (Protozoan Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160610
[St] Status:MEDLINE
[do] DOI:10.1093/molbev/msw103


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[PMID]:27208114
[Au] Autor:Wheaton GH; Mukherjee A; Kelly RM
[Ad] Endereço:Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina, USAGeorgia Institute of Technology.
[Ti] Título:Transcriptomes of the Extremely Thermoacidophilic Archaeon Metallosphaera sedula Exposed to Metal "Shock" Reveal Generic and Specific Metal Responses.
[So] Source:Appl Environ Microbiol;82(15):4613-27, 2016 Aug 01.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: The extremely thermoacidophilic archaeon Metallosphaera sedula mobilizes metals by novel membrane-associated oxidase clusters and, consequently, requires metal resistance strategies. This issue was examined by "shocking" M. sedula with representative metals (Co(2+), Cu(2+), Ni(2+), UO2 (2+), Zn(2+)) at inhibitory and subinhibitory levels. Collectively, one-quarter of the genome (554 open reading frames [ORFs]) responded to inhibitory levels, and two-thirds (354) of the ORFs were responsive to a single metal. Cu(2+) (259 ORFs, 106 Cu(2+)-specific ORFs) and Zn(2+) (262 ORFs, 131 Zn(2+)-specific ORFs) triggered the largest responses, followed by UO2 (2+) (187 ORFs, 91 UO2 (2+)-specific ORFs), Ni(2+) (93 ORFs, 25 Ni(2+)-specific ORFs), and Co(2+) (61 ORFs, 1 Co(2+)-specific ORF). While one-third of the metal-responsive ORFs are annotated as encoding hypothetical proteins, metal challenge also impacted ORFs responsible for identifiable processes related to the cell cycle, DNA repair, and oxidative stress. Surprisingly, there were only 30 ORFs that responded to at least four metals, and 10 of these responded to all five metals. This core transcriptome indicated induction of Fe-S cluster assembly (Msed_1656-Msed_1657), tungsten/molybdenum transport (Msed_1780-Msed_1781), and decreased central metabolism. Not surprisingly, a metal-translocating P-type ATPase (Msed_0490) associated with a copper resistance system (Cop) was upregulated in response to Cu(2+) (6-fold) but also in response to UO2 (2+) (4-fold) and Zn(2+) (9-fold). Cu(2+) challenge uniquely induced assimilatory sulfur metabolism for cysteine biosynthesis, suggesting a role for this amino acid in Cu(2+) resistance or issues in sulfur metabolism. The results indicate that M. sedula employs a range of physiological and biochemical responses to metal challenge, many of which are specific to a single metal and involve proteins with yet unassigned or definitive functions. IMPORTANCE: The mechanisms by which extremely thermoacidophilic archaea resist and are negatively impacted by metals encountered in their natural environments are important to understand so that technologies such as bioleaching, which leverage microbially based conversion of insoluble metal sulfides to soluble species, can be improved. Transcriptomic analysis of the cellular response to metal challenge provided both global and specific insights into how these novel microorganisms negotiate metal toxicity in natural and technological settings. As genetics tools are further developed and implemented for extreme thermoacidophiles, information about metal toxicity and resistance can be leveraged to create metabolically engineered strains with improved bioleaching characteristics.
[Mh] Termos MeSH primário: Ácidos/metabolismo
Proteínas Arqueais/genética
Metais/metabolismo
Sulfolobaceae/genética
Sulfolobaceae/metabolismo
[Mh] Termos MeSH secundário: Proteínas Arqueais/metabolismo
Genoma Arqueal
Temperatura Alta
Fases de Leitura Aberta
Sulfolobaceae/isolamento & purificação
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acids); 0 (Archaeal Proteins); 0 (Metals)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160522
[St] Status:MEDLINE
[do] DOI:10.1128/AEM.01176-16


  9 / 66 MEDLINE  
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[PMID]:26632262
[Au] Autor:Caillat C; Macheboeuf P; Wu Y; McCarthy AA; Boeri-Erba E; Effantin G; Göttlinger HG; Weissenhorn W; Renesto P
[Ad] Endereço:Unit of Virus-Host Cell interactions (UVHCI), University of Grenoble Alpes, F-38042 Grenoble, France.
[Ti] Título:Asymmetric ring structure of Vps4 required for ESCRT-III disassembly.
[So] Source:Nat Commun;6:8781, 2015 Dec 03.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The vacuolar protein sorting 4 AAA-ATPase (Vps4) recycles endosomal sorting complexes required for transport (ESCRT-III) polymers from cellular membranes. Here we present a 3.6-Å X-ray structure of ring-shaped Vps4 from Metallosphera sedula (MsVps4), seen as an asymmetric pseudohexamer. Conserved key interface residues are shown to be important for MsVps4 assembly, ATPase activity in vitro, ESCRT-III disassembly in vitro and HIV-1 budding. ADP binding leads to conformational changes within the protomer, which might propagate within the ring structure. All ATP-binding sites are accessible and the pseudohexamer binds six ATP with micromolar affinity in vitro. In contrast, ADP occupies one high-affinity and five low-affinity binding sites in vitro, consistent with conformational asymmetry induced on ATP hydrolysis. The structure represents a snapshot of an assembled Vps4 conformation and provides insight into the molecular motions the ring structure undergoes in a concerted action to couple ATP hydrolysis to ESCRT-III substrate disassembly.
[Mh] Termos MeSH primário: Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Sulfolobaceae/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Trifosfato de Adenosina/metabolismo
Sítios de Ligação
Regulação da Expressão Gênica em Archaea/fisiologia
HIV-1/fisiologia
Modelos Moleculares
Mutação
Conformação Proteica
Sulfolobaceae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Endosomal Sorting Complexes Required for Transport); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151204
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms9781


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[PMID]:25983134
[Au] Autor:Liu HC; Xia JL; Nie ZY; Zhen XJ; Zhang LJ
[Ad] Endereço:School of Minerals Processing and Bioengineering, Central South University, Changsha, 410083, China.
[Ti] Título:Differential expression of extracellular thiol groups of moderately thermophilic Sulfobacillus thermosulfidooxidans and extremely thermophilic Acidianus manzaensis grown on S(0) and Fe (2.).
[So] Source:Arch Microbiol;197(6):823-31, 2015 Aug.
[Is] ISSN:1432-072X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Bio-oxidation of elemental sulfur (S(0)) is very important in bioleaching and sulfur cycle. S(0) was proposed to be first activated by reacting with reactive thiol groups (-SH) of outer membrane proteins, forming -S n H (n ≥ 2) complexes. The differential expression of -SH of moderately thermophilic Sulfobacillus thermosulfidooxidans and extremely thermophilic Acidianus manzaensis grown on Fe(2+) and S(0) was investigated by synchrotron radiation-based scanning transmission X-ray microscopy (STXM) imaging and micro-beam X-ray fluorescence (µ-XRF) mapping. The STXM imaging and µ-XRF mapping of extracellular -SH were based on the analysis of Ca(2+) bound on the cell. By comparing Ca(2+) of the cells with and without labeling by Ca(2+), the distribution and content of thiol groups were obtained. The results showed that, for both S. thermosulfidooxidans and A. manzaensis, the expression of extracellular -SH of S(0)-grown cells was higher than that of Fe(2+)-grown cells. Statistical analysis indicated that the expression of extracellular -SH for S. thermosulfidooxidans and A. manzaensis grown on S(0) was 2.37 times and 2.14 times, respectively, to that on Fe(2+). These results evidently demonstrate that the extracellular thiol groups are most probably involved in elemental sulfur activation and oxidation of the acidophilic sulfur-oxidizing microorganisms.
[Mh] Termos MeSH primário: Ferro/metabolismo
Compostos de Sulfidrila/metabolismo
Sulfolobaceae/metabolismo
Enxofre/metabolismo
[Mh] Termos MeSH secundário: Acidianus/metabolismo
Oxirredução
Microtomografia por Raio-X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Sulfhydryl Compounds); 70FD1KFU70 (Sulfur); E1UOL152H7 (Iron)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150718
[Lr] Data última revisão:
150718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150519
[St] Status:MEDLINE
[do] DOI:10.1007/s00203-015-1111-6



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