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  1 / 1108 MEDLINE  
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[PMID]:28911108
[Au] Autor:Skowron PM; Anton BP; Czajkowska E; Zebrowska J; Sulecka E; Krefft D; Jezewska-Frackowiak J; Zolnierkiewicz O; Witkowska M; Morgan RD; Wilson GG; Fomenkov A; Roberts RJ; Zylicz-Stachula A
[Ad] Endereço:Department of Molecular Biotechnology, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland.
[Ti] Título:The third restriction-modification system from Thermus aquaticus YT-1: solving the riddle of two TaqII specificities.
[So] Source:Nucleic Acids Res;45(15):9005-9018, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Two restriction-modification systems have been previously discovered in Thermus aquaticus YT-1. TaqI is a 263-amino acid (aa) Type IIP restriction enzyme that recognizes and cleaves within the symmetric sequence 5'-TCGA-3'. TaqII, in contrast, is a 1105-aa Type IIC restriction-and-modification enzyme, one of a family of Thermus homologs. TaqII was originally reported to recognize two different asymmetric sequences: 5'-GACCGA-3' and 5'-CACCCA-3'. We previously cloned the taqIIRM gene, purified the recombinant protein from Escherichia coli, and showed that TaqII recognizes the 5'-GACCGA-3' sequence only. Here, we report the discovery, isolation, and characterization of TaqIII, the third R-M system from T. aquaticus YT-1. TaqIII is a 1101-aa Type IIC/IIL enzyme and recognizes the 5'-CACCCA-3' sequence previously attributed to TaqII. The cleavage site is 11/9 nucleotides downstream of the A residue. The enzyme exhibits striking biochemical similarity to TaqII. The 93% identity between their aa sequences suggests that they have a common evolutionary origin. The genes are located on two separate plasmids, and are probably paralogs or pseudoparalogs. Putative positions and aa that specify DNA recognition were identified and recognition motifs for 6 uncharacterized Thermus-family enzymes were predicted.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Desoxirribonucleases de Sítio Específico do Tipo II/genética
Motivos de Nucleotídeos
Plasmídeos/metabolismo
Thermus/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/metabolismo
Clonagem Molecular
Clivagem do DNA
Desoxirribonucleases de Sítio Específico do Tipo II/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Isoenzimas/genética
Isoenzimas/metabolismo
Peso Molecular
Plasmídeos/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Thermus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Isoenzymes); 0 (Recombinant Proteins); EC 3.1.21.- (endodeoxyribonuclease TaqII); EC 3.1.21.4 (Deoxyribonucleases, Type II Site-Specific)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170916
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx599


  2 / 1108 MEDLINE  
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[PMID]:28853682
[Au] Autor:Khan IU; Habib N; Hussain F; Xian WD; Amin A; Zhou EM; Ahmed I; Zhi XY; Li WJ
[Ad] Endereço:1​Yunnan Institute of Microbiology, School of Life Sciences, Yunnan University, Kunming 650091, PR China.
[Ti] Título:Thermus caldifontis sp. nov., a thermophilic bacterium isolated from a hot spring.
[So] Source:Int J Syst Evol Microbiol;67(8):2868-2872, 2017 Aug.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A thermophilic bacterial strain, designated YIM 73026T was isolated from a sediment sample collected from a hot spring in Tibet, PR China. The taxonomic position of the novel isolate was investigated by a polyphasic approach. The novel isolate was Gram-stain-negative, aerobic and rod-shaped. Colonies were circular, convex, opaque and yellow. The strain grew at 50-70 °C (optimum, 60 °C), pH 6.0-8.0 (optimum, pH 7.0) and in the presence of up to 1.0 % NaCl (w/v). Comparison of the 16S rRNA gene sequences of YIM 73026T and those of other members of the genus Thermus showed sequence similarities ranging from 91.2 to 97.5 %, with YIM 73026T showing closest sequence similarity to Thermus scotoductus SE-1T (97.5 %). DNA-DNA hybridization results, however, revealed that DNA-DNA reassociation values between YIM 73026T and T. scotoductus DSM 8553T (37.6 %), Thermusamyloliquefaciens YIM 77409T (34.5 %), Thermusantranikianii DSM 12462T (30.3 %), Thermuscaliditerrae YIM 77925T (28.6 %) and Thermustengchongensis YIM 77924T (27.3 %) were well below the 70 % limit for species identification. YIM 73026T contained MK-8 as the respiratory quinone, and iso-C15 : 0, iso-C16 : 0, iso-C17 : 0 and anteiso-C15 : 0 as the major cellular fatty acids (>10 %). The polar lipids consisted of one aminophospholipid, one phospholipid and two glycolipids. The genomic DNA G+C content of YIM 73026T was 65.4 mol%. On the basis of morphological, chemotaxonomic and genotypic characteristics, it is proposed that the isolate represents a novel species of the genus Thermus, for which the name Thermus caldifontis sp. nov. is proposed. The type strain is YIM 73026T (=NBRC 112415T=CCTCC AB 2016305T).
[Mh] Termos MeSH primário: Fontes Termais/microbiologia
Filogenia
Thermus/classificação
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Composição de Bases
DNA Bacteriano/genética
Ácidos Graxos/química
Glicolipídeos/química
Hibridização de Ácido Nucleico
Fosfolipídeos/química
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
Thermus/genética
Thermus/isolamento & purificação
Tibet
Vitamina K 2/análogos & derivados
Vitamina K 2/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (Fatty Acids); 0 (Glycolipids); 0 (Phospholipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2); 523-38-6 (vitamin MK 8)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170831
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002037


  3 / 1108 MEDLINE  
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[PMID]:28369621
[Au] Autor:Koch M; Willi J; Pradère U; Hall J; Polacek N
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland.
[Ti] Título:Critical 23S rRNA interactions for macrolide-dependent ribosome stalling on the ErmCL nascent peptide chain.
[So] Source:Nucleic Acids Res;45(11):6717-6728, 2017 Jun 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The nascent peptide exit tunnel has recently been identified as a functional region of ribosomes contributing to translation regulation and co-translational protein folding. Inducible expression of the erm resistance genes depends on ribosome stalling at specific codons of an upstream open reading frame in the presence of an exit tunnel-bound macrolide antibiotic. The molecular basis for this translation arrest is still not fully understood. Here, we used a nucleotide analog interference approach to unravel important functional groups on 23S rRNA residues in the ribosomal exit tunnel for ribosome stalling on the ErmC leader peptide. By replacing single nucleobase functional groups or even single atoms we were able to demonstrate the importance of A2062, A2503 and U2586 for drug-dependent ribosome stalling. Our data show that the universally conserved A2062 and A2503 are capable of forming a non-Watson-Crick base pair that is critical for sensing and transmitting the stalling signal from the exit tunnel back to the peptidyl transferase center of the ribosome. The nucleobases of A2062, A2503 as well as U2586 do not contribute significantly to the overall mechanism of protein biosynthesis, yet their elaborate role for co-translational monitoring of nascent peptide chains inside the exit tunnel can explain their evolutionary conservation.
[Mh] Termos MeSH primário: Antibacterianos/química
Macrolídeos/química
RNA Ribossômico 23S/química
[Mh] Termos MeSH secundário: Proteínas de Escherichia coli/biossíntese
Proteínas de Escherichia coli/química
Regulação Bacteriana da Expressão Gênica/efeitos dos fármacos
Biossíntese de Proteínas/efeitos dos fármacos
RNA Bacteriano/química
Thermus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Escherichia coli Proteins); 0 (Macrolides); 0 (RNA, Bacterial); 0 (RNA, Ribosomal, 23S)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx195


  4 / 1108 MEDLINE  
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[PMID]:28242762
[Au] Autor:Miropolskaya N; Esyunina D; Kulbachinskiy A
[Ad] Endereço:From the Institute of Molecular Genetics, Russian Academy of Sciences, Kurchatov Square 2, Moscow 123182, Russia.
[Ti] Título:Conserved functions of the trigger loop and Gre factors in RNA cleavage by bacterial RNA polymerases.
[So] Source:J Biol Chem;292(16):6744-6752, 2017 Apr 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNA cleavage by RNA polymerase (RNAP) is the central step in co-transcriptional RNA proofreading. Bacterial RNAPs were proposed to rely on the same mobile element of the active site, the trigger loop (TL), for both nucleotide addition and RNA cleavage. RNA cleavage can also be stimulated by universal Gre factors, which should replace the TL to get access to the RNAP active site. The contributions of the TL and Gre factors to RNA cleavage reportedly vary between RNAPs from different bacterial species and, probably, different types of transcription complexes. Here, by comparing RNAPs from , , and , we show that the functions of the TL and Gre factors in RNA cleavage are conserved in various species, with important variations that may be related to extremophilic adaptation. Deletions of the TL strongly impair intrinsic RNA cleavage by all three RNAPs and eliminate the interspecies differences in the reaction rates. GreA factors activate RNA cleavage by wild-type RNAPs to similar levels. The rates of GreA-dependent cleavage are lower for ΔTL RNAP variants, suggesting that the TL contributes to the Gre function. Finally, neither the TL nor GreA can efficiently activate RNA cleavage in certain types of backtracked transcription complexes, suggesting that these complexes adopt a catalytically inactive conformation probably important for transcription regulation.
[Mh] Termos MeSH primário: RNA Polimerases Dirigidas por DNA/química
Deinococcus/enzimologia
Escherichia coli/enzimologia
RNA/química
Thermus/enzimologia
[Mh] Termos MeSH secundário: Proteínas de Escherichia coli/química
Deleção de Genes
Variação Genética
Clivagem do RNA
Fatores de Transcrição/química
Transcrição Genética
Fatores de Elongação da Transcrição/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (GreA protein, E coli); 0 (Transcription Factors); 0 (Transcriptional Elongation Factors); 63231-63-0 (RNA); EC 2.7.7.6 (DNA-Directed RNA Polymerases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170301
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.766592


  5 / 1108 MEDLINE  
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[PMID]:28218714
[Au] Autor:Demina TA; Pietilä MK; Svirskaite J; Ravantti JJ; Atanasova NS; Bamford DH; Oksanen HM
[Ad] Endereço:Department of Biosciences and Institute of Biotechnology, Viikinkaari 9, FIN-00014, University of Helsinki, Helsinki, Finland. tatiana.demina@helsinki.fi.
[Ti] Título:HCIV-1 and Other Tailless Icosahedral Internal Membrane-Containing Viruses of the Family Sphaerolipoviridae.
[So] Source:Viruses;9(2), 2017 Feb 18.
[Is] ISSN:1999-4915
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Members of the virus family include both archaeal viruses and bacteriophages that possess a tailless icosahedral capsid with an internal membrane. The genera and comprise viruses that infect halophilic euryarchaea, whereas viruses of thermophilic bacteria belong to the genus . Both sequence-based and structural clustering of the major capsid proteins and ATPases of sphaerolipoviruses yield three distinct clades corresponding to these three genera. Conserved virion architectural principles observed in sphaerolipoviruses suggest that these viruses belong to the PRD1-adenovirus structural lineage. Here we focus on archaeal alphasphaerolipoviruses and their related putative proviruses. The highest sequence similarities among alphasphaerolipoviruses are observed in the core structural elements of their virions: the two major capsid proteins, the major membrane protein, and a putative packaging ATPase. A recently described tailless icosahedral haloarchaeal virus, icosahedral virus 1 (HCIV-1), has a double-stranded DNA genome and an internal membrane lining the capsid. HCIV-1 shares significant similarities with the other tailless icosahedral internal membrane-containing haloarchaeal viruses of the family . The proposal to include a new virus species, , into the genus was submitted to the International Committee on Taxonomy of Viruses (ICTV) in 2016.
[Mh] Termos MeSH primário: Vírus de Archaea/classificação
Vírus de Archaea/ultraestrutura
Bacteriófagos/classificação
Bacteriófagos/ultraestrutura
Filogenia
Vírion/ultraestrutura
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Archaea/virologia
Vírus de Archaea/genética
Bacteriófagos/genética
Proteínas do Capsídeo/genética
Análise de Sequência de DNA
Thermus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Capsid Proteins); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE


  6 / 1108 MEDLINE  
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[PMID]:28193326
[Au] Autor:Jia DX; Zhou L; Zheng YG
[Ad] Endereço:Key Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou 310014, PR China; Engineering Research Center of Bioconversion and Biopurification of the Ministry of Education, Zhejiang University of Technology, Hangzhou 310014, PR China.
[Ti] Título:Properties of a novel thermostable glucose isomerase mined from Thermus oshimai and its application to preparation of high fructose corn syrup.
[So] Source:Enzyme Microb Technol;99:1-8, 2017 Apr.
[Is] ISSN:1879-0909
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glucose isomerase (GI) is used in vitro to convert d-glucose to d-fructose, which is capable of commercial producing high fructose corn syrup (HFCS). To manufacture HFCS at elevated temperature and reduce the cost of enriching syrups, novel refractory GIs from Thermoanaerobacterium xylanolyticum (TxGI), Thermus oshimai (ToGI), Geobacillus thermocatenulatus (GtGI) and Thermoanaerobacter siderophilus (TsGI) were screened via genome mining approach. The enzymatic characteristics research showed that ToGI had higher catalytic efficiency and superior thermostability toward d-glucose among the screened GIs. Its optimum temperature reached 95°C and could retain more than 80% of initial activity in the presence of 20mM Mn at 85°C for 48h. The K and k /K values for ToGI were 81.46mM and 21.77min mM , respectively. Furthermore, the maximum conversion yield of 400g/L d-glucose to d-fructose at 85°C was 52.16%. Considering its excellent high thermostability and ameliorable application performance, ToGI might be promising for realization of future industrial production of HFCS at elevated temperature.
[Mh] Termos MeSH primário: Aldose-Cetose Isomerases/metabolismo
Proteínas de Bactérias/metabolismo
Xarope de Milho Rico em Frutose/isolamento & purificação
Thermus/enzimologia
[Mh] Termos MeSH secundário: Aldose-Cetose Isomerases/genética
Sequência de Aminoácidos
Proteínas de Bactérias/genética
Biotecnologia
Estabilidade Enzimática
Tecnologia de Alimentos
Frutose/biossíntese
Geobacillus/enzimologia
Geobacillus/genética
Glucose/metabolismo
Temperatura Alta
Concentração de Íons de Hidrogênio
Microbiologia Industrial
Cinética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Thermoanaerobacter/enzimologia
Thermoanaerobacter/genética
Thermoanaerobacterium/enzimologia
Thermoanaerobacterium/genética
Thermus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (High Fructose Corn Syrup); 0 (Recombinant Proteins); 30237-26-4 (Fructose); EC 5.3.1.- (Aldose-Ketose Isomerases); EC 5.3.1.5 (xylose isomerase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170215
[St] Status:MEDLINE


  7 / 1108 MEDLINE  
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[PMID]:27885192
[Au] Autor:Hamana K; Furuchi T; Hayashi H; Itoh T; Ohkuma M; Niitsu M
[Ad] Endereço:Faculty of Engineering, Maebashi Institute of Technology.
[Ti] Título:Occurrence of two novel linear penta-amines, pyropentamine and homopyropentamine, in extremely thermophilic Thermus composti.
[So] Source:J Gen Appl Microbiol;62(6):334-339, 2017 Jan 25.
[Is] ISSN:1349-8037
[Cp] País de publicação:Japan
[La] Idioma:eng
[Mh] Termos MeSH primário: Aminas/análise
Thermus/química
[Mh] Termos MeSH secundário: Aminas/química
Cromatografia Líquida de Alta Pressão
Escherichia coli/genética
Temperatura Alta
Especificidade da Espécie
Thermus/isolamento & purificação
Thermus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amines)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170411
[Lr] Data última revisão:
170411
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161126
[St] Status:MEDLINE
[do] DOI:10.2323/jgam.2016.05.007


  8 / 1108 MEDLINE  
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[PMID]:27815924
[Au] Autor:Taguchi H
[Ad] Endereço:Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba, 278-8510, Japan. htaguchi@rs.noda.tus.ac.jp.
[Ti] Título:The Simple and Unique Allosteric Machinery of Thermus caldophilus Lactate Dehydrogenase : Structure-Function Relationship in Bacterial Allosteric LDHs.
[So] Source:Adv Exp Med Biol;925:117-145, 2017.
[Is] ISSN:0065-2598
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many bacterial L-lactate dehydrogenases (LDH) are allosteric enzymes, and usually activated by fructose 1,6-bisphosphate (FBP) and often also by substrate pyruvate. The active and inactive state structures demonstrate that Thermus caldophilus, Lactobacillus casei, and Bifidobacterium longum LDHs consistently undergo allosteric transition according to Monod-Wyman-Changeux model, where the active (R) and inactive (T) states of the enzymes coexist in an allosteric equilibrium (pre-existing equilibrium) independently of allosteric effectors. The three enzymes consistently take on open and closed conformations of the homotetramers for the T and R states, coupling the quaternary structural changes with the structural changes in binding sites for substrate and FBP though tertiary structural changes. Nevertheless, the three enzymes undergo markedly different structural changes from one another, indicating that there is a high variety in the allosteric machineries of bacterial LDHs. L. casei LDH undergoes the largest quaternary structural change in the three enzymes, and regulates its catalytic activity though a large linkage frame for allosteric motion. In contrast, T. caldophilus LDH exhibits the simplest allosteric motion in the three enzymes, involving a simple mobile structural core for the allosteric motion. TcLDH likely mediates its allosteric equilibrium mostly through electrostatic repulsion within the protein molecule, providing an insight for regulation machineries in bacterial allosteric LDHs.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Bifidobacterium longum/enzimologia
Frutosedifosfatos/química
L-Lactato Desidrogenase/química
Lactobacillus casei/enzimologia
Ácido Pirúvico/química
Thermus/enzimologia
[Mh] Termos MeSH secundário: Regulação Alostérica
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Bifidobacterium longum/química
Bifidobacterium longum/genética
Sítios de Ligação
Frutosedifosfatos/metabolismo
Expressão Gênica
Cinética
L-Lactato Desidrogenase/genética
L-Lactato Desidrogenase/metabolismo
Lactobacillus casei/química
Lactobacillus casei/genética
Modelos Moleculares
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Quaternária de Proteína
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Ácido Pirúvico/metabolismo
Especificidade da Espécie
Relação Estrutura-Atividade
Especificidade por Substrato
Thermus/química
Thermus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fructosediphosphates); 0 (Protein Subunits); 8558G7RUTR (Pyruvic Acid); EC 1.1.1.27 (L-Lactate Dehydrogenase); M7522JYX1H (fructose-1,6-diphosphate)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161106
[St] Status:MEDLINE
[do] DOI:10.1007/5584_2016_171


  9 / 1108 MEDLINE  
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[PMID]:27695995
[Au] Autor:Zhao C; Chu Y; Li Y; Yang C; Chen Y; Wang X; Liu B
[Ad] Endereço:College of Food Science, Fujian Agriculture and Forestry University, Fuzhou, 350002, Fujian, China.
[Ti] Título:High-throughput pyrosequencing used for the discovery of a novel cellulase from a thermophilic cellulose-degrading microbial consortium.
[So] Source:Biotechnol Lett;39(1):123-131, 2017 Jan.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: To analyze the microbial diversity and gene content of a thermophilic cellulose-degrading consortium from hot springs in Xiamen, China using 454 pyrosequencing for discovering cellulolytic enzyme resources. RESULTS: A thermophilic cellulose-degrading consortium, XM70 that was isolated from a hot spring, used sugarcane bagasse as sole carbon and energy source. DNA sequencing of the XM70 sample resulted in 349,978 reads with an average read length of 380 bases, accounting for 133,896,867 bases of sequence information. The characterization of sequencing reads and assembled contigs revealed that most microbes were derived from four phyla: Geobacillus (Firmicutes), Thermus, Bacillus, and Anoxybacillus. Twenty-eight homologous genes belonging to 15 glycoside hydrolase families were detected, including several cellulase genes. A novel hot spring metagenome-derived thermophilic cellulase was expressed and characterized. CONCLUSIONS: The application value of thermostable sugarcane bagasse-degrading enzymes is shown for production of cellulosic biofuel. The practical power of using a short-read-based metagenomic approach for harvesting novel microbial genes is also demonstrated.
[Mh] Termos MeSH primário: Celulase/genética
Celulase/metabolismo
Celulose/metabolismo
[Mh] Termos MeSH secundário: Anoxybacillus/genética
Anoxybacillus/metabolismo
Bacillus/genética
Bacillus/metabolismo
Geobacillus/genética
Geobacillus/metabolismo
Fontes Termais/microbiologia
Metagenômica/métodos
Saccharum
Thermus/genética
Thermus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9004-34-6 (Cellulose); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170308
[Lr] Data última revisão:
170308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-016-2224-y


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[PMID]:27499380
[Au] Autor:Park KS; Lee CY; Kang KS; Park HG
[Ad] Endereço:Department of Chemical and Biomolecular Engineering (BK 21+ program), Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Yuseong-gu, Daejeon 305-338, Republic of Korea; Center for Systems Biology, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114, US
[Ti] Título:Aptamer-mediated universal enzyme assay based on target-triggered DNA polymerase activity.
[So] Source:Biosens Bioelectron;88:48-54, 2017 Feb 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We herein describe an innovative method for a universal fluorescence turn-on enzyme assay, which relies on the target enzyme-triggered DNA polymerase activity. In the first target recognition step, the target enzyme is designed to destabilize detection probe derived from an aptamer specific to DNA polymerase containing the overhang sequence and the complementary blocker DNA, which consequently leads to the recovery of DNA polymerase activity inhibited by the detection probe. This target-triggered polymerase activity is monitored in the second signal transduction step based on primer extension reaction coupled with TaqMan probe. Utilizing this design principle, we have successfully detected the activities of two model enzymes, exonuclease I and uracil DNA glycosylase with high sensitivity and selectivity. Since this strategy is composed of separated target recognition and signal transduction modules, it could be universally employed for the sensitive determination of numerous different target enzymes by simply redesigning the overhang sequence of detection probe, while keeping TaqMan probe-based signal transduction module as a universal signaling tool.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos/química
Técnicas Biossensoriais/métodos
DNA Polimerase Dirigida por DNA/química
Ensaios Enzimáticos/métodos
Exodesoxirribonucleases/análise
Taq Polimerase/química
Uracila-DNA Glicosidase/análise
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Exodesoxirribonucleases/metabolismo
Seres Humanos
Espectrometria de Fluorescência/métodos
Thermus/enzimologia
Uracila-DNA Glicosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aptamers, Nucleotide); EC 2.7.7.- (Taq Polymerase); EC 2.7.7.7 (DNA-Directed DNA Polymerase); EC 3.1.- (Exodeoxyribonucleases); EC 3.1.11.1 (exodeoxyribonuclease I); EC 3.2.2.- (Uracil-DNA Glycosidase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160809
[St] Status:MEDLINE



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