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[PMID]:29458666
[Au] Autor:Yang ZW; Salam N; Asem MD; Fang BZ; Lan L; Xiao M; Wadaan MAM; Hozzein WN; Li WJ
[Ad] Endereço:1​State Key Laboratory of Biocontrol and Guangdong Provincial Key Laboratory of Plant Resources, School of Life Sciences, Sun Yat-Sen University, Guangzhou 510275, PR China.
[Ti] Título:Saccharopolyspora deserti sp. nov., a novel halotolerant actinobacterium isolated from a desert.
[So] Source:Int J Syst Evol Microbiol;68(3):860-864, 2018 Mar.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Strain SYSU D8010 was isolated from a desert sand sample collected in Saudi Arabia. The taxonomic position of the isolate was investigated by the polyphasic taxonomic approach. The isolate was found to be Gram-positive and aerobic. The strain was able to grow at 14-40 °C, pH 5.0-9.0 and in the presence of up to 22 % (w/v) NaCl. Strain SYSU D8010 contained meso-diaminopimelic acid as cell-wall diamino acid, and arabinose, fucose, galactose, glucose and rhamnose as the whole-cell sugars. The primary polar lipids were diphosphatidylglycerol, phosphatidylcholine, phosphatidylglycerol, phosphatidylinositol and phosphatidylinositolmannosides. Menaquinone MK-9(H4) was detected as the respiratory quinone; and anteiso-C17 : 0, iso-C16 : 0, iso-C15 : 0 and iso-C17 : 0 as the predominant fatty acids. Pairwise comparison of the 16S rRNA gene sequences indicated that strain SYSU D8010 had a sequence similarity of 97.8 % to Saccharopolyspora halophila YIM 90500 . The genomic DNA G+C content of strain SYSU D8010 was determined to be 69.9 mol%. Based on the analyses of the phenotypic, genotypic and phylogenetic characteristics, strain SYSU D8010 was determined to represent a novel species of the genus Saccharopolyspora, for which the name Saccharopolyspora deserti sp. nov. is proposed. The type strain of the species is SYSU D8010 (=KCTC 39989 =CPCC 204620 ).
[Mh] Termos MeSH primário: Clima Desértico
Filogenia
Saccharopolyspora/classificação
Salinidade
[Mh] Termos MeSH secundário: Técnicas de Tipagem Bacteriana
Composição de Bases
DNA Bacteriano/genética
Ácido Diaminopimélico/química
Ácidos Graxos/química
Fosfolipídeos/química
RNA Ribossômico 16S/genética
Saccharopolyspora/genética
Saccharopolyspora/isolamento & purificação
Arábia Saudita
Análise de Sequência de DNA
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 (Phospholipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2); 523-39-7 (menaquinone 9); 583-93-7 (Diaminopimelic Acid)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180221
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002598


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[PMID]:28920832
[Au] Autor:Moshtaghi Nikou M; Ramezani M; Harirchi S; Makzoom S; Amoozegar MA; Shahzadeh Fazeli SA; Schumann P; Ventosa A
[Ad] Endereço:1​Microorganisms Bank, Iranian Biological Resource Centre (IBRC), ACECR, Tehran, Iran.
[Ti] Título:Salinifilum gen. nov., with description of Salinifilum proteinilyticum sp. nov., an extremely halophilic actinomycete isolated from Meighan wetland, Iran, and reclassification of Saccharopolyspora aidingensis as Salinifilum aidingensis comb. nov. and Saccharopolyspora ghardaiensis as Salinifilum ghardaiensis comb. nov.
[So] Source:Int J Syst Evol Microbiol;67(10):4221-4227, 2017 Oct.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A Gram-positive, halophilic actinobacterial strain Miq-12 was isolated from Meighan wetland in Iran. Strain Miq-12 was strictly aerobic, catalase positive and oxidase negative. The isolate grew at 12-25 % NaCl, at 30-50 °C and pH 5.5-10.5. The optimum NaCl, temperature and pH for growth were 15-20 %, 40 °C and 7.0-8.0, respectively. The cell wall of strain Miq-12 contained meso-diaminopimelic acid as diagnostic diamino acid and arabinose as whole-cell sugar. The polar lipid pattern consisted of diphosphatidylglycerol, phosphatidylglycerol, phosphatidylcholine and phosphatidylinositol. It synthesized cellular fatty acids of anteiso and iso-branched types, anteiso-C17 : 0, iso-C17:0, iso-C15:0, iso-C16 : 0. The major respiratory quinone was MK-9(H4). The G+C content of its genomic DNA was 72.1 mol%. Phylogenetic analysis based on 16S rRNA gene sequence comparison revealed that strain Miq-12 belongs to the family Pseudonocardiaceae, constituted a separate clade, and showed the closest phylogenetic similarity to Saccharopolyspora aidingensis TRM 46074 (96.99 %) and Saccharopolyspora ghardaiensis CCUG 63370 (96.92 %). On the basis of phylogenetic analysis, phenotypic and chemotaxonomic characteristics, a novel genus and species of the family Pseudonocardiaceae, Salinifilum proteinilyticum gen. nov., sp. nov., are proposed. The type strain is Miq-12 (=IBRCM 11033 =LMG 28390 ). We also propose that S. aidingensis and S. ghardaiensis should be transferred to this new genus and be named Salinifilum aidingensis comb. nov. and Salinifilum ghardaiensis comb. nov., respectively. The type strain of Salinifilum aidingensis comb. nov. is TRM 46074 (=CCTCCAA 2012014 =JCM 30185 ) and the type strain of Salinifilum ghardaiensis comb. nov. is CCUG 63370 (=DSM 45606 =CECT 8304 ).
[Mh] Termos MeSH primário: Actinobacteria/classificação
Filogenia
Saccharopolyspora/classificação
Zonas Úmidas
[Mh] Termos MeSH secundário: Actinobacteria/genética
Actinobacteria/isolamento & purificação
Técnicas de Tipagem Bacteriana
Composição de Bases
DNA Bacteriano/genética
Ácido Diaminopimélico/química
Ácidos Graxos/química
Halobacteriales/classificação
Irã (Geográfico)
Fosfolipídeos/química
RNA Ribossômico 16S/genética
Análise de Sequência de DNA
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 (Phospholipids); 0 (RNA, Ribosomal, 16S); 11032-49-8 (Vitamin K 2); 523-39-7 (menaquinone 9); 583-93-7 (Diaminopimelic Acid)
[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:170919
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.002286


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[PMID]:28760847
[Au] Autor:Xu Z; Wang M; Ye BC
[Ad] Endereço:Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
[Ti] Título:TetR Family Transcriptional Regulator PccD Negatively Controls Propionyl Coenzyme A Assimilation in Saccharopolyspora erythraea.
[So] Source:J Bacteriol;199(20), 2017 Oct 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Propanol stimulates erythromycin biosynthesis by increasing the supply of propionyl coenzyme A (propionyl-CoA), a starter unit of erythromycin production in Propionyl-CoA is assimilated via propionyl-CoA carboxylase to methylmalonyl-CoA, an extender unit of erythromycin. We found that the addition of -propanol or propionate caused a 4- to 16-fold increase in the transcriptional levels of the SACE_3398-3400 locus encoding propionyl-CoA carboxylase, a key enzyme in propionate metabolism. The regulator PccD was proved to be directly involved in the transcription regulation of the SACE_3398-3400 locus by EMSA and DNase I footprint analysis. The transcriptional levels of SACE_3398-3400 were upregulated 15- to 37-fold in the gene deletion strain (Δ ) and downregulated 3-fold in the overexpression strain (WT/pIB- ), indicating that PccD was a negative transcriptional regulator of SACE_3398-3400. The Δ strain has a higher growth rate than that of the wild-type strain (WT) on Evans medium with propionate as the sole carbon source, whereas the growth of the WT/pIB- strain was repressed. As a possible metabolite of propionate metabolism, methylmalonic acid was identified as an effector molecule of PccD and repressed its regulatory activity. A higher level of erythromycin in the Δ strain was observed compared with that in the wild-type strain. Our study reveals a regulatory mechanism in propionate metabolism and suggests new possibilities for designing metabolic engineering to increase erythromycin yield. Our work has identified the novel regulator PccD that controls the expression of the gene for propionyl-CoA carboxylase, a key enzyme in propionyl-CoA assimilation in PccD represses the generation of methylmalonyl-CoA through carboxylation of propionyl-CoA and reveals an effect on biosynthesis of erythromycin. This finding provides novel insight into propionyl-CoA assimilation, and extends our understanding of the regulatory mechanisms underlying the biosynthesis of erythromycin.
[Mh] Termos MeSH primário: Acil Coenzima A/biossíntese
Proteínas de Bactérias/metabolismo
Regulação Bacteriana da Expressão Gênica
Proteínas Repressoras/metabolismo
Saccharopolyspora/genética
[Mh] Termos MeSH secundário: 1-Propanol/metabolismo
Proteínas de Bactérias/genética
Pegada de DNA
DNA Bacteriano/metabolismo
Ensaio de Desvio de Mobilidade Eletroforética
Deleção de Genes
Expressão Gênica
Perfilação da Expressão Gênica
Propionatos/metabolismo
Ligação Proteica
Proteínas Repressoras/genética
Saccharopolyspora/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Propionates); 0 (Repressor Proteins); 317-66-8 (propionyl-coenzyme A); 96F264O9SV (1-Propanol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171015
[Lr] Data última revisão:
171015
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE


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[PMID]:28632117
[Au] Autor:Souza DT; Silva FSPD; Silva LJD; Crevelin EJ; Moraes LAB; Zucchi TD; Melo IS
[Ad] Endereço:2​College of Agriculture 'Luiz de Queiroz', University of São Paulo, Av. Pádua Dias, 11, 13418900, Piracicaba, SP, Brazil 1​Environmental Microbiology Laboratory, Embrapa Environment, Rodovia SP 340 - Km 127,5, 13820-000, Jaguariúna, SP, Brazil.
[Ti] Título:Saccharopolyspora spongiae sp. nov., a novel actinomycete isolated from the marine sponge Scopalina ruetzleri (Wiedenmayer, 1977).
[So] Source:Int J Syst Evol Microbiol;67(6):2019-2025, 2017 Jun.
[Is] ISSN:1466-5034
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A novel marine actinomycete, designated strain CMAA 1452T, was isolated from the sponge Scopalina ruetzleri collected from Saint Peter and Saint Paul Archipelago, in Brazil, and subjected to a polyphasic taxonomic investigation. The organism formed a distinct phyletic line in the Saccharopolyspora 16S rRNA gene tree and had chemotaxonomic and morphological properties consistent with its classification in this genus. It was found to be closely related to Saccharopolyspora dendranthemae KLBMP 1305T (99.5% 16S rRNA gene sequence similarity) and shared similarities of 99.3, 99.2 and 99.0 % with 'Saccharopolyspora endophytica' YIM 61095, Saccharopolyspora tripterygii YIM 65359T and 'Saccharopolyspora pathumthaniensis' S582, respectively. DNA-DNA relatedness values between the isolate and its closest phylogenetic neighbours, namely S. dendranthemae KLBMP 1305T, 'S. endophytica' YIM 61095 and S. tripterygii YIM 65359T, were 53.5, 25.8 and 53.2 %, respectively. Strain CMAA 1452T was also distinguished from the type strains of these species using a range of phenotypic features. On the basis of these results, it is proposed that strain CMAA 1452T (=DSM 103218T=NRRL B-65384T) merits recognition as the type strain of a novel Saccharopolyspora species, Saccharopolyspora spongiae sp. nov.
[Mh] Termos MeSH primário: Filogenia
Poríferos/microbiologia
Saccharopolyspora/classificação
[Mh] Termos MeSH secundário: Animais
Técnicas de Tipagem Bacteriana
Composição de Bases
Brasil
DNA Bacteriano/genética
Hibridização de Ácido Nucleico
RNA Ribossômico 16S/genética
Saccharopolyspora/genética
Saccharopolyspora/isolamento & purificação
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Bacterial); 0 (RNA, Ribosomal, 16S)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE
[do] DOI:10.1099/ijsem.0.001912


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[PMID]:28628641
[Au] Autor:Bernatchez E; Langlois A; Brassard J; Flamand N; Marsolais D; Blanchet MR
[Ad] Endereço:Institut Universitaire de Cardiologie et de Pneumologie de Québec, Université Laval, Quebec, Quebec, Canada.
[Ti] Título:Hypersensitivity pneumonitis onset and severity is regulated by CD103 dendritic cell expression.
[So] Source:PLoS One;12(6):e0179678, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pulmonary dendritic cells drive lung responses to foreign antigens, including Saccharopolyspora rectivirgula, a causative agent of hypersensitivity pneumonitis. While the airway inflammatory mechanisms involved in hypersensitivity pneumonitis are well described, the mechanisms leading to the break in homeostasis and hypersensitivity pneumonitis onset are not well-described, and could involve CD103+ dendritic cells, which are found at baseline and during inflammatory responses in the lung. However, recent demonstration of the ability of CD103+ dendritic cells to induce inflammatory responses starkly contrasts with their classically described role as regulatory cells. These discrepancies may be attributable to the lack of current information on the importance of CD103 expression and modulation on these cells during inflammatory episodes. METHODS: To verify the importance of CD103 expression in the regulation of hypersensitivity pneumonitis, wild-type and Cd103-/- mice were exposed intranasally to S. rectivirgula and airway inflammation was quantified. Surface expression of CD103 in response to S. rectivirgula exposure was studied and cell transfers were used to determine the relative importance of CD103 expression on dendritic cells and T cells in regulating the inflammation in hypersensitivity pneumonitis. RESULTS: Cd103-/- mice developed an exacerbated inflammatory response as early as 18h following S. rectivirgula exposure. CD103 expression on dendritic cells was downregulated quickly following S. rectivirgula exposure, and cell transfers demonstrated that CD103 expression on dendritic cells specifically (and not T cells) regulates the onset and severity of this response. CONCLUSION: All in all, we demonstrate that CD103 expression by dendritic cells, but not T cells, is crucial for homeostasis maintenance and the regulation of the TH17 airway inflammatory response in hypersensitivity pneumonitis.
[Mh] Termos MeSH primário: Alveolite Alérgica Extrínseca/patologia
Antígenos CD/metabolismo
Células Dendríticas/metabolismo
Cadeias alfa de Integrinas/metabolismo
[Mh] Termos MeSH secundário: Alveolite Alérgica Extrínseca/imunologia
Alveolite Alérgica Extrínseca/microbiologia
Animais
Antígenos de Bactérias/imunologia
Antígenos CD/genética
Líquido da Lavagem Broncoalveolar/citologia
Linfócitos T CD4-Positivos/citologia
Linfócitos T CD4-Positivos/imunologia
Linfócitos T CD4-Positivos/metabolismo
Linfócitos T CD8-Positivos/citologia
Linfócitos T CD8-Positivos/imunologia
Linfócitos T CD8-Positivos/metabolismo
Citocinas/metabolismo
Células Dendríticas/citologia
Células Dendríticas/imunologia
Modelos Animais de Doenças
Regulação para Baixo
Imunoglobulina G/sangue
Imunoglobulina G/imunologia
Cadeias alfa de Integrinas/deficiência
Cadeias alfa de Integrinas/genética
Leucócitos/citologia
Pulmão/citologia
Pulmão/imunologia
Pulmão/patologia
Camundongos
Camundongos Knockout
Saccharopolyspora/metabolismo
Saccharopolyspora/patogenicidade
Índice de Gravidade de Doença
Baço/citologia
Baço/imunologia
Células Th17/citologia
Células Th17/imunologia
Células Th17/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Antigens, CD); 0 (Cytokines); 0 (Immunoglobulin G); 0 (Integrin alpha Chains); 0 (alpha E integrins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179678


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[PMID]:28399278
[Au] Autor:Zhao L; Alto BW; Duguma D
[Ad] Endereço:Florida Medical Entomology Laboratory, University of Florida, 200 9th St. South East, Vero Beach, FL 32962.
[Ti] Título:Transcriptional Profile for Detoxification Enzymes AeaGGT1 and AaeGGT2 From Aedes aegypti (Diptera: Culicidae) in Response to Larvicides.
[So] Source:J Med Entomol;54(4):878-887, 2017 Jul 01.
[Is] ISSN:1938-2928
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aedes aegypti (L.) is the vector responsible for transmitting dengue, chikungunya, yellow fever, and Zika viruses, as well as other pathogens. Microbial larvicides based on Bacillus thuringiensis Berliner israelensis (Bti) and Saccharopolyspora spinosa Mertz and Yao, such as VectoBac 12AS and Natular 2EC, have been shown to be effective in reducing larval populations of Ae. aegypti. We examined the gene expression of two detoxification enzymes, glucosyl and glucuronosyl transferases (AaeGGT1 and AaeGGT2), through developmental stages and a time course study in response to larvicide exposure using qualitative real-time polymerase chain reaction (qPCR). AaeGGT1 and AaeGGT2 gene expressions were differentially regulated during development of the immature stages. We also found that male adults had higher expression than female adults after controlling for age effects. AaeGGT1 and AaeGGT2 gene expression were both upregulated in response to VectoBac 12AS and Natular 2EC treatments with the maximum level of expression occurring 24 h after treatment applications. This information sheds light on larvicide-induced changes in the physiology of Ae. aegypti with implications for development of mosquito control strategies.
[Mh] Termos MeSH primário: Aedes/genética
Regulação da Expressão Gênica
Glucosiltransferases/genética
Glucuronosiltransferase/genética
Proteínas de Insetos/genética
Inseticidas/farmacologia
[Mh] Termos MeSH secundário: Aedes/efeitos dos fármacos
Aedes/crescimento & desenvolvimento
Animais
Bacillus thuringiensis/química
Feminino
Glucosiltransferases/metabolismo
Glucuronosiltransferase/metabolismo
Proteínas de Insetos/metabolismo
Larva/efeitos dos fármacos
Larva/genética
Larva/crescimento & desenvolvimento
Masculino
Óvulo/efeitos dos fármacos
Óvulo/crescimento & desenvolvimento
Pupa/efeitos dos fármacos
Pupa/genética
Pupa/crescimento & desenvolvimento
Reação em Cadeia da Polimerase em Tempo Real
Saccharopolyspora/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insect Proteins); 0 (Insecticides); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.17 (Glucuronosyltransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE
[do] DOI:10.1093/jme/tjw244


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[PMID]:28166382
[Au] Autor:Dhakal D; Pokhrel AR; Jha AK; Thuan NH; Sohng JK
[Ad] Endereço:Department of Life Science and Biochemical Engineering, Sun Moon University, Chungnam, Republic of Korea.
[Ti] Título:Saccharopolyspora Species: Laboratory Maintenance and Enhanced Production of Secondary Metabolites.
[So] Source:Curr Protoc Microbiol;44:10H.1.1-10H.1.13, 2017 Feb 06.
[Is] ISSN:1934-8533
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Saccharopolyspora spp. are aerobic, Gram-positive, non-acid-fast, and non-motile actinomycetes. Various species of the genus Saccharopolyspora have been reported with an ability to produce various bioactive compounds for pharmaceutical and agricultural uses. This unit includes general protocols for the laboratory maintenance of Saccharopolyspora species, including growth in liquid medium, growth on solid agar, long-term storage, and generation of a higher producer strain by mutagenesis. Saccharopolyspora spinosa ATCC 49460 is used as a prototype for explaining the considerations for efficient laboratory maintenance of Saccharopolyspora spp. Saccharopolyspora spinosa is a producer of spinosad, a prominent insecticide with selective activity against various insects. © 2017 by John Wiley & Sons, Inc.
[Mh] Termos MeSH primário: Técnicas Bacteriológicas/métodos
Produtos Biológicos/metabolismo
Engenharia Metabólica/métodos
Saccharopolyspora/crescimento & desenvolvimento
Saccharopolyspora/metabolismo
[Mh] Termos MeSH secundário: Meios de Cultura/química
Mutagênese
Preservação Biológica/métodos
Saccharopolyspora/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biological Products); 0 (Culture Media)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170207
[St] Status:MEDLINE
[do] DOI:10.1002/cpmc.21


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[PMID]:28154945
[Au] Autor:Lu C; Yin J; Zhao F; Li F; Lu W
[Ad] Endereço:School of Chemical Engineering and Technology, Tianjin University, Tianjin, 300072, People's Republic of China.
[Ti] Título:Metabolomics analysis of the effect of dissolved oxygen on spinosad production by Saccharopolyspora spinosa.
[So] Source:Antonie Van Leeuwenhoek;110(5):677-685, 2017 May.
[Is] ISSN:1572-9699
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Spinosad, a universal bio-pesticide, is obtained from the soil actinomycete Saccharopolyspora spinosa. Dissolved oxygen, an important contributing factor in aerobic microbial fermentation, however, is not always available in sufficient amounts. To alleviate oxygen limitation in spinosad production, three different oxygen vectors, namely oleic acid, toluene, and n-dodecane, were added into early fermentation. Results indicated that n-dodecane was the optimal oxygen vector. Spinosad yield was increased by 44.2% compared to that in the control group in the presence of 0.5% n-dodecane, added after 120 h of incubation. Yields of the test group reached 6.52 mg/g dry cell weight (DCW), while that of the control group was limited to 4.52 mg/g DCW. Metabolomics analysis by gas chromatography coupled to mass spectrometry was performed to demonstrate the metabolism mechanism in the presence and absence of oxygen vector. In total, 78 principal intracellular metabolites in S. spinosa were detected and quantified in the presence and absence of n-dodecane. Levels of some metabolites that were related to the tricarboxylic acid cycle and pentose phosphate pathway varied significantly. Aspartic acid and glucose-1-phosphate levels varied significantly and contributed most in the distinction of the fermentation conditions and phases. The above findings give new insights into the improvement and the metabolomic characteristics of industrial spinosad production.
[Mh] Termos MeSH primário: Macrolídeos/metabolismo
Metabolômica
Oxigênio/metabolismo
Saccharopolyspora/efeitos dos fármacos
Saccharopolyspora/metabolismo
[Mh] Termos MeSH secundário: Aerobiose
Alcanos/metabolismo
Combinação de Medicamentos
Fermentação
Cromatografia Gasosa-Espectrometria de Massas
Ácido Oleico/metabolismo
Fatores de Tempo
Tolueno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alkanes); 0 (Drug Combinations); 0 (Macrolides); 11A386X1QH (n-dodecane); 2UMI9U37CP (Oleic Acid); 3FPU23BG52 (Toluene); S88TT14065 (Oxygen); XPA88EAP6V (spinosad)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170414
[Lr] Data última revisão:
170414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170204
[St] Status:MEDLINE
[do] DOI:10.1007/s10482-017-0835-5


  9 / 419 MEDLINE  
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[PMID]:28103677
[Au] Autor:Koryakina I; Kasey C; McArthur JB; Lowell AN; Chemler JA; Li S; Hansen DA; Sherman DH; Williams GJ
[Ad] Endereço:Department of Chemistry, NC State University , Raleigh, North Carolina 27695-8204, United States.
[Ti] Título:Inversion of Extender Unit Selectivity in the Erythromycin Polyketide Synthase by Acyltransferase Domain Engineering.
[So] Source:ACS Chem Biol;12(1):114-123, 2017 01 20.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acyltransferase (AT) domains of polyketide synthases (PKSs) select extender units for incorporation into polyketides and dictate large portions of the structures of clinically relevant natural products. Accordingly, there is significant interest in engineering the substrate specificity of PKS ATs in order to site-selectively manipulate polyketide structure. However, previous attempts to engineer ATs have yielded mutant PKSs with relaxed extender unit specificity, rather than an inversion of selectivity from one substrate to another. Here, by directly screening the extender unit selectivity of mutants from active site saturation libraries of an AT from the prototypical PKS, 6-deoxyerythronolide B synthase, a set of single amino acid substitutions was discovered that dramatically impact the selectivity of the PKS with only modest reductions of product yields. One particular substitution (Tyr189Arg) inverted the selectivity of the wild-type PKS from its natural substrate toward a non-natural alkynyl-modified extender unit while maintaining more than twice the activity of the wild-type PKS with its natural substrate. The strategy and mutations described herein form a platform for combinatorial biosynthesis of site-selectively modified polyketide analogues that are modified with non-natural and non-native chemical functionality.
[Mh] Termos MeSH primário: Aciltransferases/metabolismo
Eritromicina/metabolismo
Mutagênese Sítio-Dirigida
Policetídeo Sintases/metabolismo
Policetídeos/metabolismo
Saccharopolyspora/enzimologia
[Mh] Termos MeSH secundário: Aciltransferases/química
Aciltransferases/genética
Eritromicina/química
Macrolídeos/química
Macrolídeos/metabolismo
Mutagênese Sítio-Dirigida/métodos
Mutação Puntual
Policetídeo Sintases/química
Policetídeo Sintases/genética
Policetídeos/química
Domínios Proteicos
Saccharopolyspora/genética
Saccharopolyspora/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Macrolides); 0 (Polyketides); 63937KV33D (Erythromycin); 79956-01-7 (Polyketide Synthases); 81644-19-1 (10-deoxymethynolide); EC 2.3.- (Acyltransferases)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170414
[Lr] Data última revisão:
170414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.6b00732


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[PMID]:27987242
[Au] Autor:You D; Wang MM; Ye BC
[Ad] Endereço:Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Meilong RD 130, Shanghai, 200237, China.
[Ti] Título:Acetyl-CoA synthetases of Saccharopolyspora erythraea are regulated by the nitrogen response regulator GlnR at both transcriptional and post-translational levels.
[So] Source:Mol Microbiol;103(5):845-859, 2017 Mar.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Saccharopolyspora erythraea has three AMP-forming acetyl-CoA synthetases (Acs) encoded by acsA1, acsA2, and acsA3. In this work, we found that nitrogen response regulator GlnR can directly interact with the promoter regions of all three genes and can activate their transcription in response to nitrogen availability. The typical GlnR-binding boxes were identified in the promoter regions. Moreover, the activities of three Acs enzymes were modulated by the reversible lysine acetylation (RLA) with acetyltransferase AcuA and NAD -dependent deacetylase SrtN. Interestingly, GlnR controlled the RLA by directly activating the expression of acuA and srtN. A glnR-deleted mutant (ΔglnR) caused a growth defect in 10 mM acetate minimal medium, a condition under which RLA function is critical to control Acs activity. Overexpression of acuA reversed the growth defect of ΔglnR mutant. Total activity of Acs in cell-free extracts from ΔglnR strain had a 4-fold increase relative to that of wildtype strain. Western Blotting showed that in vivo acetylation levels of Acs were influenced by nitrogen availability and lack of glnR. These results demonstrated that GlnR regulated acetyl-CoA synthetases at transcriptional and post-translational levels, and mediated the interplay between nitrogen and carbon metabolisms by integrating nitrogen signals to modulate the acetate metabolism.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/genética
Aminoacil-tRNA Sintetases/genética
Regulação Bacteriana da Expressão Gênica
Nitrogênio/metabolismo
Processamento de Proteína Pós-Traducional
Saccharopolyspora/enzimologia
Transcrição Genética
[Mh] Termos MeSH secundário: Acetato-CoA Ligase/metabolismo
Acetilação
Aminoacil-tRNA Sintetases/metabolismo
Proteínas de Bactérias/metabolismo
Carbono/metabolismo
Lisina/metabolismo
Saccharopolyspora/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 7440-44-0 (Carbon); EC 6.1.1.- (Amino Acyl-tRNA Synthetases); EC 6.1.1.18 (glutaminyl-tRNA synthetase); EC 6.2.1.1 (Acetate-CoA Ligase); K3Z4F929H6 (Lysine); N762921K75 (Nitrogen)
[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:161218
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13595



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