Base de dados : MEDLINE
Pesquisa : B03.300.390.400.810.768.500 [Categoria DeCS]
Referências encontradas : 352 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 36 ir para página                         

  1 / 352 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28712746
[Au] Autor:Gao G; Liu X; Xu M; Wang Y; Zhang F; Xu L; Lv J; Long Q; Kang Q; Ou HY; Wang Y; Rohr J; Deng Z; Jiang M; Lin S; Tao M
[Ad] Endereço:State Key Laboratory of Microbial Metabolism, Joint International Research Laboratory of Metabolic & Developmental Sciences, and School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200030, P. R. China.
[Ti] Título:Formation of an Angular Aromatic Polyketide from a Linear Anthrene Precursor via Oxidative Rearrangement.
[So] Source:Cell Chem Biol;24(7):881-891.e4, 2017 Jul 20.
[Is] ISSN:2451-9456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacterial aromatic polyketides are a group of natural products synthesized by polyketide synthases (PKSs) that show diverse structures and biological activities. They are structurally subclassified into linear, angular, and discoid aromatic polyketides, the formation of which is commonly determined by the shaping and folding of the poly-ß-keto intermediates under the concerted actions of the minimal PKSs, cyclases and ketoreductases. Murayaquinone, found in several streptomycetes, possesses an unusual tricyclic angular aromatic polyketide core containing a 9,10-phenanthraquinone. In this study, genes essential for murayaquinone biosynthesis were identified, and a linear anthraoxirene intermediate was discovered. A unique biosynthetic model for the angular aromatic polyketide formation was discovered and confirmed through in vivo and in vitro studies. Three oxidoreductases, MrqO3, MrqO6, and MrqO7, were identified to catalyze the conversion of the linear aromatic polyketide intermediate into the final angularly arranged framework, which exemplifies a novel strategy for the biosynthesis of angular aromatic polyketides.
[Mh] Termos MeSH primário: Oxirredutases/metabolismo
Fenantrenos/metabolismo
Policetídeos/metabolismo
Quinonas/metabolismo
[Mh] Termos MeSH secundário: Antracenos/química
Antracenos/metabolismo
Biocatálise
Espectroscopia de Ressonância Magnética
Espectrometria de Massas
Família Multigênica
Oxirredutases/genética
Fenantrenos/química
Policetídeo Sintases/genética
Policetídeo Sintases/metabolismo
Policetídeos/química
Quinonas/química
Streptomyces/química
Streptomyces/metabolismo
Streptomyces lividans/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anthracenes); 0 (Phenanthrenes); 0 (Polyketides); 0 (Quinones); 42L7BZ8H74 (9,10-phenanthrenequinone); 79956-01-7 (Polyketide Synthases); EC 1.- (Oxidoreductases)
[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:170718
[St] Status:MEDLINE


  2 / 352 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28436005
[Au] Autor:Koepff J; Keller M; Tsolis KC; Busche T; Rückert C; Hamed MB; Anné J; Kalinowski J; Wiechert W; Economou A; Oldiges M
[Ad] Endereço:Forschungszentrum Jülich GmbH, Institute of Bio- and Geosciences, IBG-1: Biotechnology, Leo-Brandt-Straße, 52428, Jülich, Germany.
[Ti] Título:Fast and reliable strain characterization of Streptomyces lividans through micro-scale cultivation.
[So] Source:Biotechnol Bioeng;114(9):2011-2022, 2017 Sep.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Filamentous organisms of the genus Streptomyces play an important role in industrial production processes, due to their extensive secondary metabolism variability, as well as their ability to secrete efficiently large amounts of (heterologous) proteins. While genetic engineering tools are available to rapidly build up large strain libraries, the subsequent strain screening and bioprocess development still constitutes a bottleneck. This is due to the lack of reliable parallelized and accelerated cultivation techniques for morphologically challenging organisms. To address this challenge, we developed an integrated cultivation workflow for Streptomyces lividans based on a parallelized shaken 48-well microtiter-plate (MTP) cultivation device. In a first step, a feasible pre-culture method was identified and validated, revealing high comparability in subsequent main cultivations (coefficient of variation of 1.1% for in-plate replicates and 3.2% between different pre-cultures). When validating the growth performance in 1 mL MTP cultivation against an established 1,000 mL lab-scale cultivation system, highly comparable cultivation patterns were found for online (pH, dissolved oxygen), as well as for offline derived parameters (glucose uptake, cell-dry-weight, and pellet size). Additionally, the two cultivation regimes were compared with respect to transcriptional and protein secretion activity of Streptomyces, showing overall good comparability with minor, but well explainable discrepancies, most probably caused by different energy dissipation (shaking vs. stirring) and adaption effects due to different illumination conditions. Embedded within the presented cultivation workflow, the 1 mL MTP-based parallelized cultivation system seems to be a suitable screening tool for filamentous and industrial relevant organisms like Streptomyces. This can contribute to widen the field of application for these organisms and facilitate screening and early-stage bioprocess development. Biotechnol. Bioeng. 2017;114: 2011-2022. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Técnicas de Cultura Celular por Lotes/instrumentação
Reatores Biológicos/microbiologia
Ensaios de Triagem em Larga Escala/métodos
Modelos Biológicos
Streptomyces lividans/citologia
Streptomyces lividans/fisiologia
[Mh] Termos MeSH secundário: Técnicas de Cultura Celular por Lotes/métodos
Proliferação Celular
Tamanho Celular
Simulação por Computador
Desenho de Equipamento
Análise de Falha de Equipamento
Miniaturização
Projetos Piloto
Reprodutibilidade dos Testes
Sensibilidade e Especificidade
Especificidade da Espécie
Fluxo de Trabalho
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170425
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26321


  3 / 352 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28369604
[Au] Autor:Yang CC; Tseng SM; Pan HY; Huang CH; Chen CW
[Ad] Endereço:Department of Chemistry, Chung-Yuan Christian University, Chung-li, Taiwan.
[Ti] Título:Telomere associated primase Tap repairs truncated telomeres of Streptomyces.
[So] Source:Nucleic Acids Res;45(10):5838-5849, 2017 Jun 02.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Replication of the linear chromosomes of soil bacteria Streptomyces proceeds from an internal origin towards the telomeres, followed by patching of the resulting terminal single-strand overhangs by DNA synthesis using terminal proteins as the primer, which remains covalently bound to the 5΄ ends of the DNA. In most Streptomyces chromosomes, the end patching requires the single-strand overhangs, terminal protein Tpg, and terminal associated protein Tap. The telomere overhangs contain several palindromic sequences capable of forming stable hairpins. Previous in vitro deoxynucleotidylation studies indicated that Tap adds the Palindrome I sequence to Tpg, which is extended by a polymerase to fill the gap. In this study, the stringency of Palindrome I sequence was examined by an in vitro deoxynucleotidylation system and in vivo replication. Several nt in Palindrome I were identified to be critical for priming. While the first 3 G on the template were required for deoxynucleotidylation in vitro, deletions of them could be suppressed by the presence of dGTP. In vivo, deletions of these G were also tolerated, and the telomere sequence was restored in the linear plasmid DNA. Our results indicated that the truncated telomeres were repaired by extension synthesis by Tap on the foldback Palindrome I sequence.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
DNA Primase/genética
Reparo do DNA
Replicação do DNA
Streptomyces coelicolor/genética
Streptomyces lividans/genética
Telômero/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Pareamento de Bases
Sequência de Bases
Cromossomos Bacterianos/química
DNA Primase/metabolismo
Conformação de Ácido Nucleico
Plasmídeos/química
Plasmídeos/metabolismo
Streptomyces coelicolor/metabolismo
Streptomyces lividans/metabolismo
Telômero/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 2.7.7.- (DNA Primase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx189


  4 / 352 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28358920
[Au] Autor:Yan L; Zhang Q; Virolle MJ; Xu D
[Ad] Endereço:Department of Ecology, Institute of Hydrobiology, School of Life Science and Technology, Key Laboratory of Eutrophication and Red Tide Prevention of Guangdong Higher Education Institutes, Engineering Research Center of Tropical and Subtropical Aquatic Ecological Engineering, Ministry of Education, J
[Ti] Título:In conditions of over-expression, WblI, a WhiB-like transcriptional regulator, has a positive impact on the weak antibiotic production of Streptomyces lividans TK24.
[So] Source:PLoS One;12(3):e0174781, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulators of the WhiB-like (wbl) family are playing important role in the complex regulation of metabolic and morphological differentiation in Streptomyces. In this study, we investigated the role of wblI, a member of this family, in the regulation of secondary metabolite production in Streptomyces lividans. The over-expression of wblI was correlated with an enhanced biosynthesis of undecylprodigiosin and actinorhodin and with a reduction of the biosynthesis of yCPK and of the grey spore pigment encoded by the whiE locus. Five regulatory targets of WblI were identified using in vitro formaldehyde crosslinking and confirmed by EMSA and qRT-PCR. These included the promoter regions of wblI itself, two genes of the ACT cluster (actVA3 and the intergenic region between the divergently orientated genes actII-1 and actII-2) and that of wblA, another member of the Wbl family. Quantitative RT-PCR analysis indicated that the expression of actVA3 encoding a protein of unknown function as well as that of actII-1, a TetR regulator repressing the expression of actII-2, encoding the ACT transporter, were down regulated in the WblI over-expressing strain. Consistently the expression of the transporter actII-2 was up-regulated. The expression of WblA, that is known to have a negative impact on ACT biosynthesis, was strongly down regulated in the WblI over-expressing strain. These data are consistent with the positive impact that WblI over-expression has on ACT biosynthesis. The latter might result from direct activation of ACT biosynthesis and export and from repression of the expression of WblA, a likely indirect, repressor of ACT biosynthesis.
[Mh] Termos MeSH primário: Antibacterianos/biossíntese
Proteínas de Bactérias/metabolismo
Streptomyces lividans/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Ensaio de Desvio de Mobilidade Eletroforética
Regulação Bacteriana da Expressão Gênica/genética
Regulação Bacteriana da Expressão Gênica/fisiologia
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Streptomyces lividans/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174781


  5 / 352 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28093470
[Au] Autor:Chaplin AK; Svistunenko DA; Hough MA; Wilson MT; Vijgenboom E; Worrall JA
[Ad] Endereço:School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, U.K.
[Ti] Título:Active-site maturation and activity of the copper-radical oxidase GlxA are governed by a tryptophan residue.
[So] Source:Biochem J;474(5):809-825, 2017 Feb 20.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:GlxA from is a mononuclear copper-radical oxidase and a member of the auxiliary activity family 5 (AA5). Its domain organisation and low sequence homology make it a distinct member of the AA5 family in which the fungal galactose 6-oxidase (Gox) is the best characterised. GlxA is a key cuproenzyme in the copper-dependent morphological development of with a function that is linked to the processing of an extracytoplasmic glycan. The catalytic sites in GlxA and Gox contain two distinct one-electron acceptors comprising the copper ion and a 3'-( -cysteinyl) tyrosine. The latter is formed post-translationally through a covalent bond between a cysteine and a copper-co-ordinating tyrosine ligand and houses a radical. In GlxA and Gox, a second co-ordination sphere tryptophan residue (Trp288 in GlxA) is present, but the orientation of the indole ring differs between the two enzymes, creating a marked difference in the π-π stacking interaction of the benzyl ring with the 3'-( -cysteinyl) tyrosine. Differences in the spectroscopic and enzymatic activity have been reported between GlxA and Gox with the indole orientation suggested as a reason. Here, we report a series of and studies using the W288F and W288A variants of GlxA to assess the role of Trp288 on the morphology, maturation, spectroscopic and enzymatic properties. Our findings point towards a salient role for Trp288 in the kinetics of copper loading and maturation of GlxA, with its presence essential for stabilising the metalloradical site required for coupling catalytic activity and morphological development.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Cobre/química
Galactose Oxidase/química
Oxirredutases/química
Streptomyces lividans/química
Triptofano/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Substituição de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Domínio Catalítico
Cátions Bivalentes
Clonagem Molecular
Cobre/metabolismo
Cristalografia por Raios X
Cisteína/química
Cisteína/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Fusarium/química
Fusarium/enzimologia
Fusarium/crescimento & desenvolvimento
Galactose Oxidase/genética
Galactose Oxidase/metabolismo
Expressão Gênica
Cinética
Ligantes
Mutação
Oxirredutases/genética
Oxirredutases/metabolismo
Ligação Proteica
Domínios Proteicos
Estrutura Secundária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Streptomyces lividans/enzimologia
Streptomyces lividans/crescimento & desenvolvimento
Homologia Estrutural de Proteína
Especificidade por Substrato
Triptofano/metabolismo
Tirosina/química
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cations, Divalent); 0 (Ligands); 0 (Recombinant Proteins); 42HK56048U (Tyrosine); 789U1901C5 (Copper); 8DUH1N11BX (Tryptophan); EC 1.- (Oxidoreductases); EC 1.1.3.9 (Galactose Oxidase); EC 1.16.- (copper oxidase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170614
[Lr] Data última revisão:
170614
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170118
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160968


  6 / 352 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27960258
[Au] Autor:Altrichter S; Haase M; Loh B; Kuhn A; Leptihn S
[Ad] Endereço:Institute of Microbiology and Molecular Biology, University of Hohenheim , Garbenstrasse 30, 70599 Stuttgart, Germany.
[Ti] Título:Mechanism of the Spontaneous and Directional Membrane Insertion of a 2-Transmembrane Ion Channel.
[So] Source:ACS Chem Biol;12(2):380-388, 2017 Feb 17.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein insertion into membranes is a process occurring in every cell and every cellular compartment. Yet, many thermodynamic aspects of this fundamental biophysical process are not well understood. We investigated physicochemical parameters that influence protein insertion using the model protein KcsA, a 2-transmembrane ion channel. To understand what drives insertion and to identify individual steps of protein integration into a highly apolar environment, we investigated the contribution of electrostatic interactions and lipid composition on protein insertion on a single molecule level. We show that insertion of KcsA is spontaneous and directional as the cytosolic part of the protein does not translocate across the membrane barrier. Surprisingly, not hydrophobic residues but charged amino acids are crucial for the insertion of the unfolded protein into the membrane. Our results demonstrate the importance of electrostatic interactions between membrane and protein during the insertion process of hydrophobic polypeptides into the apolar membrane. On the basis of the observation that negatively charged lipids increase insertion events while high ionic strength in the surrounding aqueous phase decreases insertion events, a two-step mechanism is proposed. Here, an initial electrostatic attraction between membrane and protein represents the first step prior to insertion of hydrophobic residues into the hydrocarbon core of the membrane.
[Mh] Termos MeSH primário: Canais Iônicos/metabolismo
[Mh] Termos MeSH secundário: Membrana Celular/metabolismo
Cromatografia Líquida de Alta Pressão
Dicroísmo Circular
Detergentes/química
Lipossomos
Concentração Osmolar
Desnaturação Proteica
Espectrometria de Fluorescência
Eletricidade Estática
Streptomyces lividans/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Detergents); 0 (Ion Channels); 0 (Liposomes)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161215
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.6b01085


  7 / 352 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27488682
[Au] Autor:Esnault C; Leiber D; Toffano-Nioche C; Tanfin Z; Virolle MJ
[Ad] Endereço:Institute of Integrative Biology of the Cell (I2BC), Group "Energetic Metabolism of Streptomyces", CEA, CNRS, University of Paris-Sud, INRA, University Paris-Saclay, F-91198, Gif-sur-Yvette Cedex, France.
[Ti] Título:Another example of enzymatic promiscuity: the polyphosphate kinase of Streptomyces lividans is endowed with phospholipase D activity.
[So] Source:Appl Microbiol Biotechnol;101(1):139-145, 2017 Jan.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Polyphosphate kinases (PPK) from different bacteria, including that of Streptomyces lividans, were shown to contain the typical HKD motif present in phospholipase D (PLD) and showed structural similarities to the latter. This observation prompted us to investigate the PLD activity of PPK of S. lividans, in vitro. The ability of PPK to catalyze the hydrolysis of phosphatidylcholine (PC), the PLD substrate, was assessed by the quantification of [ H]phosphatidic acid (PA) released from [ H]PC-labeled ELT3 cell membranes. Basal cell membrane PLD activity as well as GTPγS-activated PLD activity was higher in the presence than in absence of PPK. After abolition of the basal PLD activity of the membranes by heat or tryptic treatment, the addition of PPK to cell membranes was still accompanied by an increased production of PA demonstrating that PPK also bears a PLD activity. PLD activity of PPK was also assessed by the production of choline from hydrolysis of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) in the presence of the Amplex Red reagent and compared to two commercial PLD enzymes. These data demonstrated that PPK is endowed with a weak but clearly detectable PLD activity. The question of the biological signification, if any, of this enzymatic promiscuity is discussed.
[Mh] Termos MeSH primário: Fosfolipase D/metabolismo
Fosfotransferases (Aceptor do Grupo Fosfato)/metabolismo
Streptomyces lividans/enzimologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Membrana Celular/enzimologia
Colina/metabolismo
Hidrólise
Ácidos Fosfatídicos/metabolismo
Fosfatidilcolinas/metabolismo
Fosfolipase D/química
Fosfolipase D/genética
Fosfotransferases (Aceptor do Grupo Fosfato)/química
Fosfotransferases (Aceptor do Grupo Fosfato)/genética
Conformação Proteica
Streptomyces lividans/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphatidic Acids); 0 (Phosphatidylcholines); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.4.1 (polyphosphate kinase); EC 3.1.4.4 (Phospholipase D); EDS2L3ODLV (1,2-oleoylphosphatidylcholine); N91BDP6H0X (Choline)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160805
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-7743-x


  8 / 352 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27977736
[Au] Autor:Vicente RL; Gullón S; Marín S; Mellado RP
[Ad] Endereço:Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain.
[Ti] Título:The Three Streptomyces lividans HtrA-Like Proteases Involved in the Secretion Stress Response Act in a Cooperative Manner.
[So] Source:PLoS One;11(12):e0168112, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Overproduction of Sec-proteins in S. lividans accumulates misfolded proteins outside of the cytoplasmic membrane where the accumulated proteins interfere with the correct functioning of the secretion machinery and with the correct cell functionality, triggering the expression in S. lividans of a CssRS two-component system which regulates the degradation of the accumulated protein, the so-called secretion stress response. Optimization of secretory protein production via the Sec route requires the identification and characterisation of quality factors involved in this process. The phosphorylated regulator (CssR) interacts with the regulatory regions of three genes encoding three different HtrA-like proteases. Individual mutations in each of these genes render degradation of the misfolded protein inoperative, and propagation in high copy number of any of the three proteases encoding genes results on indiscriminate alpha-amylase degradation. None of the proteases could complement the other two deficiencies and only propagation of each single copy protease gene can restore its own deficiency. The obtained results strongly suggest that the synthesis of the three HtrA-like proteases needs to be properly balanced to ensure the effective degradation of misfolded overproduced secretory proteins and, at the same time, avoid negative effects in the secreted proteins and the secretion machinery. This is particularly relevant when considering the optimisation of Streptomyces strains for the overproduction of homologous or heterologous secretory proteins of industrial application.
[Mh] Termos MeSH primário: Regulação Bacteriana da Expressão Gênica
Peptídeo Hidrolases/metabolismo
Streptomyces lividans/metabolismo
[Mh] Termos MeSH secundário: Peptídeo Hidrolases/genética
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170703
[Lr] Data última revisão:
170703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0168112


  9 / 352 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27793152
[Au] Autor:Liu S; Wang M; Du G; Chen J
[Ad] Endereço:Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, China. liusong@jiangnan.edu.cn.
[Ti] Título:Improving the active expression of transglutaminase in Streptomyces lividans by promoter engineering and codon optimization.
[So] Source:BMC Biotechnol;16(1):75, 2016 Oct 28.
[Is] ISSN:1472-6750
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Transglutaminases (TGase), which are synthesized as a zymogen (pro-TGase) in Streptomyces sp., are important enzymes in the food industry. Because this pro-peptide is essential for the correct folding of Streptomyces TGase, TGase is usually expressed in an inactive pro-TGase form, which is then converted to active TGase by the addition of activating proteases in vitro. In this study, Streptomyces hygroscopicus TGase was actively produced by Streptomyces lividans through promoter engineering and codon optimization. RESULTS: A gene fragment (tg1, 2.6 kb) that encoded the pro-TGase and its endogenous promoter region, signal peptide and terminator was amplified from S. hygroscopicus WSH03-13 and cloned into plasmid pIJ86, which resulted in pIJ86/tg1. After fermentation for 2 days, S. lividans TK24 that harbored pIJ86/tg1 produced 1.8 U/mL of TGase, and a clear TGase band (38 kDa) was detected in the culture supernatant. These results indicated that the pro-TGase was successfully expressed and correctly processed into active TGase in S. lividans TK24 by using the TGase promoter. Based on deletion analysis, the complete sequence of the TGase promoter is restricted to the region from -693 to -48. We also identified a negative element (-198 to -148) in the TGase promoter, and the deletion of this element increased the TGase production by 81.3 %, in contrast to the method by which S. lividans expresses pIJ86/tg1. Combining the deletion of the negative element of the promoter and optimization of the gene codons, the yield and productivity of TGase reached 5.73 U/mL and 0.14 U/mL/h in the recombinant S. lividans, respectively. CONCLUSIONS: We constructed an active TGase-producing strain that had a high yield and productivity, and the optimized TGase promoter could be a good candidate promoter for the expression of other proteins in Streptomyces.
[Mh] Termos MeSH primário: Códon/genética
Regiões Promotoras Genéticas/genética
Streptomyces lividans/enzimologia
Streptomyces lividans/genética
Transglutaminases/biossíntese
Transglutaminases/genética
[Mh] Termos MeSH secundário: Regulação Bacteriana da Expressão Gênica/genética
Regulação Enzimológica da Expressão Gênica/genética
Melhoramento Genético/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); EC 2.3.2.13 (Transglutaminases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161030
[St] Status:MEDLINE


  10 / 352 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27405271
[Au] Autor:Fujiwara R; Noda S; Tanaka T; Kondo A
[Ad] Endereço:Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.
[Ti] Título:Styrene production from a biomass-derived carbon source using a coculture system of phenylalanine ammonia lyase and phenylacrylic acid decarboxylase-expressing Streptomyces lividans transformants.
[So] Source:J Biosci Bioeng;122(6):730-735, 2016 Dec.
[Is] ISSN:1347-4421
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:To produce styrene from a biomass-derived carbon source, Streptomyces lividans was adopted as a host strain. The gene encoding ferulic acid decarboxylase from Saccharomyces cerevisiae (FDC1) was introduced into S. lividans, and the resulting S. lividans transformant successfully expressed FDC1 and converted trans-cinnamic acid (CA) to styrene. A key factor in styrene production using microbes is the recovery of volatile styrene. In the present study, we selected polystyrene resin beads XRD-4 as the absorbent agent to recover styrene produced using S. lividans transformants, which enabled recovery of styrene from the culture broth. For styrene production from biomass-derived carbon sources, S. lividans/FDC1 was cultured together with S. lividans/p-encP, which we previously reported as a CA-producing S. lividans strain. This coculture system combined with the recovery of styrene using XAD-4 allowed the production of styrene from glucose, cellobiose, or xylo-oligosaccharide, respectively.
[Mh] Termos MeSH primário: Biomassa
Carboxiliases/genética
Carboxiliases/metabolismo
Fenilalanina Amônia-Liase/genética
Fenilalanina Amônia-Liase/metabolismo
Streptomyces lividans
Estireno/metabolismo
[Mh] Termos MeSH secundário: Carbono/metabolismo
Celobiose/metabolismo
Cinamatos/metabolismo
Técnicas de Cocultura
Glucose/metabolismo
Glucuronatos/metabolismo
Engenharia Metabólica/métodos
Oligossacarídeos/metabolismo
Organismos Geneticamente Modificados
Saccharomyces cerevisiae/genética
Streptomyces/genética
Streptomyces lividans/genética
Streptomyces lividans/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cinnamates); 0 (Glucuronates); 0 (Oligosaccharides); 0 (xylooligosaccharide); 16462-44-5 (Cellobiose); 44LJ2U959V (Styrene); 7440-44-0 (Carbon); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.- (phenylacrylic acid decarboxylase); EC 4.3.1.24 (Phenylalanine Ammonia-Lyase); IY9XDZ35W2 (Glucose); U14A832J8D (cinnamic acid)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160714
[St] Status:MEDLINE



página 1 de 36 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde