Base de dados : MEDLINE
Pesquisa : B02.075.800.780 [Categoria DeCS]
Referências encontradas : 7 [refinar]
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  1 / 7 MEDLINE  
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[PMID]:25483036
[Au] Autor:Hrle A; Maier LK; Sharma K; Ebert J; Basquin C; Urlaub H; Marchfelder A; Conti E
[Ad] Endereço:a Structural Cell Biology Department; Max Planck Institute of Biochemistry ; Martinsried , Germany.
[Ti] Título:Structural analyses of the CRISPR protein Csc2 reveal the RNA-binding interface of the type I-D Cas7 family.
[So] Source:RNA Biol;11(8):1072-82, 2014.
[Is] ISSN:1555-8584
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Upon pathogen invasion, bacteria and archaea activate an RNA-interference-like mechanism termed CRISPR (clustered regularly interspaced short palindromic repeats). A large family of Cas (CRISPR-associated) proteins mediates the different stages of this sophisticated immune response. Bioinformatic studies have classified the Cas proteins into families, according to their sequences and respective functions. These range from the insertion of the foreign genetic elements into the host genome to the activation of the interference machinery as well as target degradation upon attack. Cas7 family proteins are central to the type I and type III interference machineries as they constitute the backbone of the large interference complexes. Here we report the crystal structure of Thermofilum pendens Csc2, a Cas7 family protein of type I-D. We found that Csc2 forms a core RRM-like domain, flanked by three peripheral insertion domains: a lid domain, a Zinc-binding domain and a helical domain. Comparison with other Cas7 family proteins reveals a set of similar structural features both in the core and in the peripheral domains, despite the absence of significant sequence similarity. T. pendens Csc2 binds single-stranded RNA in vitro in a sequence-independent manner. Using a crosslinking - mass-spectrometry approach, we mapped the RNA-binding surface to a positively charged surface patch on T. pendens Csc2. Thus our analysis of the key structural and functional features of T. pendens Csc2 highlights recurring themes and evolutionary relationships in type I and type III Cas proteins.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Proteínas Associadas a CRISPR/química
Proteínas de Ligação a RNA/química
Thermofilaceae/química
[Mh] Termos MeSH secundário: Archaea
Proteínas Arqueais/genética
Sítios de Ligação
Proteínas Associadas a CRISPR/genética
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas/genética
Cristalografia por Raios X
Interações Hospedeiro-Patógeno/genética
Conformação Proteica
RNA Arqueal/química
RNA Arqueal/genética
Proteínas de Ligação a RNA/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (CRISPR-Associated Proteins); 0 (RNA, Archaeal); 0 (RNA-Binding Proteins)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141209
[St] Status:MEDLINE
[do] DOI:10.4161/rna.29893


  2 / 7 MEDLINE  
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[PMID]:23266119
[Au] Autor:Li D; Li X; Dang W; Tran PL; Park SH; Oh BC; Hong WS; Lee JS; Park KH
[Ad] Endereço:Key Laboratory of Agricultural Products Processing in Jilin Provincial Universities, Changchun University, Satellite Road 6543, Changchun 130022, People's Republic of China. drlidan@yahoo.com
[Ti] Título:Characterization and application of an acidophilic and thermostable ß-glucosidase from Thermofilum pendens.
[So] Source:J Biosci Bioeng;115(5):490-6, 2013 May.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The gene encoding a ß-glucosidase from the archaeon Thermofilum pendens (Tpbgl) was cloned and expressed in Escherichia coli. The purified recombinant enzyme had a molecular mass of 77.8 kDa and released glucose or mannose from p-nitrophenyl-ß-d-glucopyranoside (pNPG), cellobiose, mannobiose, and genistin. Peak Tpbgl activity was detected at 90°C, and 50% activity remained after incubation for 60 min at 95°C. The optimal pH for pNPG hydrolysis was 3.5. When the enzyme was incubated with pNPG in the presence of ethanol and propanol, the glucose moiety was transferred to acceptor alcohols. Tpbgl is the archaeal ß-glucosidase from glucoside hydrolase family 3 and found to be most heat stable under extremely acidic conditions (pH 3.5). The kinetic parameters revealed that Tpbgl had the highest catalytic efficiency toward pNPG (kcat/Km = 3.05) with strong substrate affinity for such natural substrates as cellobiose (Km = 0.149) and mannobiose (Km = 0.147). Genistin solubilized in 10-40% DMSO was hydrolyzed to genistein with nearly 99% conversion, indicating that high concentrations of the water-insoluble isoflavone glycoside can be treated by the enzyme. Our results indicate that Tpbgl has great potential in cellulose saccharification and the glucoside hydrolysis of natural compounds.
[Mh] Termos MeSH primário: Thermofilaceae/enzimologia
beta-Glucosidase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Celobiose/metabolismo
Estabilidade Enzimática
Glucosídeos/metabolismo
Temperatura Alta
Concentração de Íons de Hidrogênio
Isoflavonas/metabolismo
Cinética
Dados de Sequência Molecular
Alinhamento de Sequência
beta-Glucosidase/química
beta-Glucosidase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glucosides); 0 (Isoflavones); 16462-44-5 (Cellobiose); 1POG3SCN5T (genistin); 2492-87-7 (4-nitrophenyl beta-D-glucoside); EC 3.2.1.21 (beta-Glucosidase)
[Em] Mês de entrada:1401
[Cu] Atualização por classe:130415
[Lr] Data última revisão:
130415
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121226
[St] Status:MEDLINE


  3 / 7 MEDLINE  
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[PMID]:19707756
[Au] Autor:Li X; Li D; Yin Y; Park KH
[Ad] Endereço:Key Laboratory of Agricultural Products Processing in Jilin Province Universities, Changchun University, Changchun 130022, People's Republic of China.
[Ti] Título:Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity.
[So] Source:Appl Microbiol Biotechnol;85(6):1821-30, 2010 Feb.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A gene (Tpen_1458) encoding a putative alpha amylase from hyperthermophilic archaeon Thermofilum pendens (TfMA) was cloned and expressed in Escherichia coli. The recombinant amylolytic enzyme was purified by Ni-NTA affinity chromatography and its catalytic properties were examined. Purified TfMA was extremely thermostable with a half-life of 60 min at an optimal temperature of 95 degrees C. TfMA activity increased to 136% in the presence of 5 mM CaCl(2). Maximal activity was measured toward gamma-cyclodextrin with a specific activity of 56 U/mg using copper bicinchoninate method. TfMA catalyzed the ring-opening reaction by cleaving one alpha-1,4-glycosidic linkage of cyclodextrin to produce corresponding single maltooligosaccharide at the initial time. The final products from cyclodextrins, linear maltooligosaccharides, and starch were glucose and maltose, and TfMA could also degrade pullulan and amylase inhibitor acarbose to panose and acarviosine-glucose, respectively. These results revealed that TfMA is a novel maltogenic amylase.
[Mh] Termos MeSH primário: Amilases/química
Amilases/isolamento & purificação
Proteínas Arqueais/química
Proteínas Arqueais/isolamento & purificação
Ciclodextrinas/química
Thermofilaceae/enzimologia
[Mh] Termos MeSH secundário: Amilases/biossíntese
Amilases/genética
Proteínas Arqueais/biossíntese
Proteínas Arqueais/genética
Estabilidade Enzimática/fisiologia
Escherichia coli/genética
Glucose/química
Temperatura Alta
Maltose/química
Oligossacarídeos/química
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Thermofilaceae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Cyclodextrins); 0 (Oligosaccharides); 0 (Recombinant Proteins); 69-79-4 (Maltose); EC 3.2.1.- (Amylases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1004
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090827
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-009-2190-6


  4 / 7 MEDLINE  
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[PMID]:19341479
[Au] Autor:Anderson IJ; Dharmarajan L; Rodriguez J; Hooper S; Porat I; Ulrich LE; Elkins JG; Mavromatis K; Sun H; Land M; Lapidus A; Lucas S; Barry K; Huber H; Zhulin IB; Whitman WB; Mukhopadhyay B; Woese C; Bristow J; Kyrpides N
[Ad] Endereço:Genome Biology Program, Joint Genome Institute, Walnut Creek, USA. IJAnderson@lbl.gov
[Ti] Título:The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota.
[So] Source:BMC Genomics;10:145, 2009 Apr 02.
[Is] ISSN:1471-2164
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Staphylothermus marinus is an anaerobic, sulfur-reducing peptide fermenter of the archaeal phylum Crenarchaeota. It is the third heterotrophic, obligate sulfur reducing crenarchaeote to be sequenced and provides an opportunity for comparative analysis of the three genomes. RESULTS: The 1.57 Mbp genome of the hyperthermophilic crenarchaeote Staphylothermus marinus has been completely sequenced. The main energy generating pathways likely involve 2-oxoacid:ferredoxin oxidoreductases and ADP-forming acetyl-CoA synthases. S. marinus possesses several enzymes not present in other crenarchaeotes including a sodium ion-translocating decarboxylase likely to be involved in amino acid degradation. S. marinus lacks sulfur-reducing enzymes present in the other two sulfur-reducing crenarchaeotes that have been sequenced -- Thermofilum pendens and Hyperthermus butylicus. Instead it has three operons similar to the mbh and mbx operons of Pyrococcus furiosus, which may play a role in sulfur reduction and/or hydrogen production. The two marine organisms, S. marinus and H. butylicus, possess more sodium-dependent transporters than T. pendens and use symporters for potassium uptake while T. pendens uses an ATP-dependent potassium transporter. T. pendens has adapted to a nutrient-rich environment while H. butylicus is adapted to a nutrient-poor environment, and S. marinus lies between these two extremes. CONCLUSION: The three heterotrophic sulfur-reducing crenarchaeotes have adapted to their habitats, terrestrial vs. marine, via their transporter content, and they have also adapted to environments with differing levels of nutrients. Despite the fact that they all use sulfur as an electron acceptor, they are likely to have different pathways for sulfur reduction.
[Mh] Termos MeSH primário: Desulfurococcaceae/genética
Genoma Arqueal
Pyrodictiaceae/genética
Enxofre/metabolismo
Thermofilaceae/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Carboxiliases/metabolismo
Desulfurococcaceae/classificação
Desulfurococcaceae/metabolismo
Transporte de Elétrons
Genômica
Metilmalonil-CoA Descarboxilase/metabolismo
Dados de Sequência Molecular
Filogenia
Pyrodictiaceae/metabolismo
Thermofilaceae/metabolismo
Transposases/genética
[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:
70FD1KFU70 (Sulfur); EC 2.7.7.- (Transposases); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.3 (oxaloacetate decarboxylase); EC 4.1.1.41 (Methylmalonyl-CoA Decarboxylase)
[Em] Mês de entrada:0907
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090404
[St] Status:MEDLINE
[do] DOI:10.1186/1471-2164-10-145


  5 / 7 MEDLINE  
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[PMID]:18378597
[Au] Autor:Jenney FE; Adams MW
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Life Sciences Bldg. University of Georgia, Athens, GA 30602-7229, USA.
[Ti] Título:Hydrogenases of the model hyperthermophiles.
[So] Source:Ann N Y Acad Sci;1125:252-66, 2008 Mar.
[Is] ISSN:0077-8923
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hydrogenases are enzymes found in all domains of life that catalyze a remarkably simple chemistry, the reversible oxidation of molecular hydrogen to protons and electrons. In order to perform this chemistry, cells have evolved, several different times, intricate organometal complexes built around a binuclear Ni-Fe or Fe-Fe center, with bound CO and CN(-) groups, as well as multiple FeS centers. These complicated enzymes have been an area of intense study for many decades, with interest peaking on the occasions of major increases in national energy costs. Interest in biologically generated hydrogen as a potential substitute for fossil fuels is again at the forefront, and the new tools of the postgenomic world available for manipulating these enzymes make it a truly viable possibility. Hydrogenases from hyperthermophilic microorganisms such as Pyrococcus furiosus and Thermotoga maritima, with optimal growth temperatures near 100 degrees C, are of particular interest and promise for elucidating and manipulating these enzymatic mechanisms.
[Mh] Termos MeSH primário: Hidrogenase/metabolismo
Thermofilaceae/enzimologia
Thermotoga maritima/enzimologia
[Mh] Termos MeSH secundário: Proteínas Arqueais/metabolismo
Proteínas de Bactérias/metabolismo
Metabolismo Energético
Óleos Combustíveis
Hidrogênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; REVIEW
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Bacterial Proteins); 0 (Fuel Oils); 7YNJ3PO35Z (Hydrogen); EC 1.12.7.2 (Hydrogenase)
[Em] Mês de entrada:0808
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080402
[St] Status:MEDLINE
[do] DOI:10.1196/annals.1419.013


  6 / 7 MEDLINE  
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[PMID]:18263724
[Au] Autor:Anderson I; Rodriguez J; Susanti D; Porat I; Reich C; Ulrich LE; Elkins JG; Mavromatis K; Lykidis A; Kim E; Thompson LS; Nolan M; Land M; Copeland A; Lapidus A; Lucas S; Detter C; Zhulin IB; Olsen GJ; Whitman W; Mukhopadhyay B; Bristow J; Kyrpides N
[Ad] Endereço:Joint Genome Institute, 2800 Mitchell Dr., Walnut Creek, CA 94598, USA. IJAnderson@lbl.gov
[Ti] Título:Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction.
[So] Source:J Bacteriol;190(8):2957-65, 2008 Apr.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We report the complete genome of Thermofilum pendens, a deeply branching, hyperthermophilic member of the order Thermoproteales in the archaeal kingdom Crenarchaeota. T. pendens is a sulfur-dependent, anaerobic heterotroph isolated from a solfatara in Iceland. It is an extracellular commensal, requiring an extract of Thermoproteus tenax for growth, and the genome sequence reveals that biosynthetic pathways for purines, most amino acids, and most cofactors are absent. In fact, T. pendens has fewer biosynthetic enzymes than obligate intracellular parasites, although it does not display other features that are common among obligate parasites and thus does not appear to be in the process of becoming a parasite. It appears that T. pendens has adapted to life in an environment rich in nutrients. T. pendens was known previously to utilize peptides as an energy source, but the genome revealed a substantial ability to grow on carbohydrates. T. pendens is the first crenarchaeote and only the second archaeon found to have a transporter of the phosphotransferase system. In addition to fermentation, T. pendens may obtain energy from sulfur reduction with hydrogen and formate as electron donors. It may also be capable of sulfur-independent growth on formate with formate hydrogen lyase. Additional novel features are the presence of a monomethylamine:corrinoid methyltransferase, the first time that this enzyme has been found outside the Methanosarcinales, and the presence of a presenilin-related protein. The predicted highly expressed proteins do not include proteins encoded by housekeeping genes and instead include ABC transporters for carbohydrates and peptides and clustered regularly interspaced short palindromic repeat-associated proteins.
[Mh] Termos MeSH primário: Vias Biossintéticas
DNA Arqueal/genética
Genoma Arqueal
Thermofilaceae/genética
[Mh] Termos MeSH secundário: Proteínas Arqueais/genética
Composição de Bases
Proteínas de Transporte/genética
DNA Arqueal/química
Microbiologia Ambiental
Genes Arqueais
Islândia
Dados de Sequência Molecular
Análise de Sequência de DNA
Thermofilaceae/isolamento & purificação
[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 (Archaeal Proteins); 0 (Carrier Proteins); 0 (DNA, Archaeal)
[Em] Mês de entrada:0804
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080212
[St] Status:MEDLINE
[do] DOI:10.1128/JB.01949-07


  7 / 7 MEDLINE  
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[PMID]:17426919
[Au] Autor:Hetzer A; Morgan HW; McDonald IR; Daughney CJ
[Ad] Endereço:Thermophile Research Unit, University of Waikato, Te Whare Wananga o Waikato, Gate 1 Knighton Road, Private Bag 3105, Hamilton, 3240, New Zealand. hetzer.adrian@web.de
[Ti] Título:Microbial life in Champagne Pool, a geothermal spring in Waiotapu, New Zealand.
[So] Source:Extremophiles;11(4):605-14, 2007 Jul.
[Is] ISSN:1431-0651
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Surveys of Champagne Pool, one of New Zealand's largest terrestrial hot springs and rich in arsenic ions and compounds, have been restricted to geological and geochemical descriptions, and a few microbiological studies applying culture-independent methods. In the current investigation, a combination of culture and culture-independent approaches were chosen to determine microbial density and diversity in Champagne Pool. Recovered total DNA and adenosine 5'-triphosphate (ATP) content of spring water revealed relatively low values compared to other geothermal springs within New Zealand and are in good agreement with low cell numbers of 5.6 +/- 0.5 x 10(6) cells/ml obtained for Champagne Pool water samples by 4',6-diamidino-2-phenylindole (DAPI) staining. Denaturing Gradient Gel Electrophoresis (DGGE) and 16S rRNA (small-subunit ribosomal nucleic acid) gene clone library analyses of environmental DNA indicated the abundance of Sulfurihydrogenibium, Sulfolobus, and Thermofilum-like populations in Champagne Pool. From these results, media were selected to target the enrichment of hydrogen-oxidizing and sulfur-dependent microorganisms. Three isolates were successfully obtained having 16S rRNA gene sequences with similarities of approximately 98% to Thermoanaerobacter tengcongensis, 94% to Sulfurihydrogenibium azorense, and 99% to Thermococcus waiotapuensis, respectively.
[Mh] Termos MeSH primário: Archaea/isolamento & purificação
Bactérias/isolamento & purificação
Biodiversidade
Sedimentos Geológicos/microbiologia
Fontes Termais/microbiologia
Microbiologia da Água
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/análise
Archaea/classificação
Archaea/crescimento & desenvolvimento
Bactérias/classificação
Bactérias/crescimento & desenvolvimento
Meios de Cultura
DNA Arqueal/análise
DNA Bacteriano/análise
DNA Ribossômico/análise
Biblioteca Gênica
Sedimentos Geológicos/química
Fontes Termais/química
Concentração de Íons de Hidrogênio
Dados de Sequência Molecular
Nova Zelândia
Filogenia
RNA Ribossômico 16S
Ribotipagem
Sulfolobus/isolamento & purificação
Temperatura Ambiente
Thermoanaerobacter/isolamento & purificação
Thermococcus/isolamento & purificação
Thermofilaceae/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Culture Media); 0 (DNA, Archaeal); 0 (DNA, Bacterial); 0 (DNA, Ribosomal); 0 (RNA, Ribosomal, 16S); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:0712
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:070412
[St] Status:MEDLINE



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