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  1 / 1501 MEDLINE  
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[PMID]:28465214
[Au] Autor:Guo J; Wang Y; Li B; Huang S; Chen Y; Guo X; Xiao D
[Ad] Endereço:Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education College of Biotechnology, Tianjin University of Science Technology, Tianjin, 300457, China.
[Ti] Título:Development of a one-step gene knock-out and knock-in method for metabolic engineering of Aureobasidium pullulans.
[So] Source:J Biotechnol;251:145-150, 2017 Jun 10.
[Is] ISSN:1873-4863
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Aureobasidium pullulans is an increasingly attractive host for bio-production of pullulan, heavy oil, polymalic acid, and a large spectrum of extracellular enzymes. To date, genetic manipulation of A. pullulans mainly relies on time-consuming conventional restriction enzyme digestion and ligation methods. In this study, we present a one-step homologous recombination-based method for rapid genetic manipulation in A. pullulans. Overlaps measuring >40bp length and 10µg DNA segments for homologous recombination provided maximum benefits to transformation of A. pullulans. This optimized method was successfully applied to PKSIII gene (encodes polyketide synthase) knock-out and gltP gene (encodes glycolipid transfer protein) knock-in. After disruption of PKSIII gene, secretion of melanin decreased slightly. The melanin purified from disruptant showed lower reducing capacity compared with that of the parent strain, leading to a decrease in exopolysaccharide production. Knock-in of gltP gene resulted in at least 4.68-fold increase in heavy oil production depending on the carbon source used, indicating that gltP can regulate heavy oil synthesis in A. pullulans.
[Mh] Termos MeSH primário: Ascomicetos/genética
Ascomicetos/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Transporte/genética
Fermentação
Proteínas Fúngicas/metabolismo
Técnicas de Introdução de Genes
Técnicas de Inativação de Genes
Genes Fúngicos
Glucose/metabolismo
Melaninas/metabolismo
Engenharia Metabólica
Policetídeo Sintases/genética
Recombinação Genética
Xilose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Fungal Proteins); 0 (Melanins); 0 (lipid transfer protein); 79956-01-7 (Polyketide Synthases); A1TA934AKO (Xylose); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  2 / 1501 MEDLINE  
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[PMID]:28448715
[Au] Autor:Thiele GAR; Friedman CP; Tsai KJS; Beld J; Londergan CH; Charkoudian LK
[Ad] Endereço:Department of Chemistry, Haverford College , Haverford, Pennsylvania 19041-1392, United States.
[Ti] Título:Acyl Carrier Protein Cyanylation Delivers a Ketoacyl Synthase-Carrier Protein Cross-Link.
[So] Source:Biochemistry;56(20):2533-2536, 2017 05 23.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acyl carrier proteins (ACPs) are central hubs in polyketide and fatty acid biosynthetic pathways, but the fast motions of the ACP's phosphopantetheine (Ppant) arm make its conformational dynamics difficult to capture using traditional spectroscopic approaches. Here we report that converting the terminal thiol of Escherichia coli ACP's Ppant arm into a thiocyanate activates this site to form a selective cross-link with the active site cysteine of its partner ketoacyl synthase (FabF). The reaction releases a cyanide anion, which can be detected by infrared spectroscopy. This represents a practical and generalizable method for obtaining and visualizing ACP-protein complexes relevant to biocatalysis and will be valuable in future structural and engineering studies.
[Mh] Termos MeSH primário: Proteína de Transporte de Acila/química
Cianetos/química
Policetídeo Sintases/química
[Mh] Termos MeSH secundário: Cromatografia em Gel
Proteínas de Escherichia coli/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Cyanides); 0 (Escherichia coli Proteins); 79956-01-7 (Polyketide Synthases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171205
[Lr] Data última revisão:
171205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00219


  3 / 1501 MEDLINE  
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[PMID]:28985565
[Au] Autor:Cooke TF; Fischer CR; Wu P; Jiang TX; Xie KT; Kuo J; Doctorov E; Zehnder A; Khosla C; Chuong CM; Bustamante CD
[Ad] Endereço:Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305, USA.
[Ti] Título:Genetic Mapping and Biochemical Basis of Yellow Feather Pigmentation in Budgerigars.
[So] Source:Cell;171(2):427-439.e21, 2017 Oct 05.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Parrot feathers contain red, orange, and yellow polyene pigments called psittacofulvins. Budgerigars are parrots that have been extensively bred for plumage traits during the last century, but the underlying genes are unknown. Here we use genome-wide association mapping and gene-expression analysis to map the Mendelian blue locus, which abolishes yellow pigmentation in the budgerigar. We find that the blue trait maps to a single amino acid substitution (R644W) in an uncharacterized polyketide synthase (MuPKS). When we expressed MuPKS heterologously in yeast, yellow pigments accumulated. Mass spectrometry confirmed that these yellow pigments match those found in feathers. The R644W substitution abolished MuPKS activity. Furthermore, gene-expression data from feathers of different bird species suggest that parrots acquired their colors through regulatory changes that drive high expression of MuPKS in feather epithelia. Our data also help formulate biochemical models that may explain natural color variation in parrots. VIDEO ABSTRACT.
[Mh] Termos MeSH primário: Proteínas Aviárias/genética
Plumas/fisiologia
Melopsittacus/genética
Pigmentos Biológicos/biossíntese
Polienos/metabolismo
Policetídeo Sintases/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas Aviárias/metabolismo
Plumas/anatomia & histologia
Plumas/química
Expressão Gênica
Genoma
Estudo de Associação Genômica Ampla
Melopsittacus/anatomia & histologia
Melopsittacus/fisiologia
Pigmentação
Policetídeo Sintases/metabolismo
Polimorfismo de Nucleotídeo Único
Regeneração
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Avian Proteins); 0 (Pigments, Biological); 0 (Polyenes); 79956-01-7 (Polyketide Synthases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171007
[St] Status:MEDLINE


  4 / 1501 MEDLINE  
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[PMID]:28832129
[Au] Autor:Mathews II; Allison K; Robbins T; Lyubimov AY; Uervirojnangkoorn M; Brunger AT; Khosla C; DeMirci H; McPhillips SE; Hollenbeck M; Soltis M; Cohen AE
[Ad] Endereço:Stanford Synchrotron Radiation Lightsource , 2575 Sand Hill Road, Menlo Park, California 94025, United States.
[Ti] Título:The Conformational Flexibility of the Acyltransferase from the Disorazole Polyketide Synthase Is Revealed by an X-ray Free-Electron Laser Using a Room-Temperature Sample Delivery Method for Serial Crystallography.
[So] Source:Biochemistry;56(36):4751-4756, 2017 Sep 12.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The crystal structure of the trans-acyltransferase (AT) from the disorazole polyketide synthase (PKS) was determined at room temperature to a resolution of 2.5 Å using a new method for the direct delivery of the sample into an X-ray free-electron laser. A novel sample extractor efficiently delivered limited quantities of microcrystals directly from the native crystallization solution into the X-ray beam at room temperature. The AT structure revealed important catalytic features of this core PKS enzyme, including the occurrence of conformational changes around the active site. The implications of these conformational changes for polyketide synthase reaction dynamics are discussed.
[Mh] Termos MeSH primário: Aciltransferases/metabolismo
Cristalografia por Raios X/métodos
Lasers
Policetídeo Sintases/química
Conformação Proteica
[Mh] Termos MeSH secundário: Aciltransferases/química
Subunidades Proteicas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 79956-01-7 (Polyketide Synthases); EC 2.3.- (Acyltransferases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00711


  5 / 1501 MEDLINE  
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[PMID]:28719729
[Au] Autor:Andersen-Ranberg J; Kongstad KT; Nafisi M; Staerk D; Okkels FT; Mortensen UH; Lindberg Møller B; Frandsen RJN; Kannangara R
[Ad] Endereço:Plant Biochemistry Laboratory, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, 1871, Frederiksberg, Denmark.
[Ti] Título:Synthesis of C-Glucosylated Octaketide Anthraquinones in Nicotiana benthamiana by Using a Multispecies-Based Biosynthetic Pathway.
[So] Source:Chembiochem;18(19):1893-1897, 2017 Oct 05.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Carminic acid is a C-glucosylated octaketide anthraquinone and the main constituent of the natural dye carmine (E120), possessing unique coloring, stability, and solubility properties. Despite being used since ancient times, longstanding efforts to elucidate its route of biosynthesis have been unsuccessful. Herein, a novel combination of enzymes derived from a plant (Aloe arborescens, Aa), a bacterium (Streptomyces sp. R1128, St), and an insect (Dactylopius coccus, Dc) that allows for the biosynthesis of the C-glucosylated anthraquinone, dcII, a precursor for carminic acid, is reported. The pathway, which consists of AaOKS, StZhuI, StZhuJ, and DcUGT2, presents an alternative biosynthetic approach for the production of polyketides by using a type III polyketide synthase (PKS) and tailoring enzymes originating from a type II PKS system. The current study showcases the power of using transient expression in Nicotiana benthamiana for efficient and rapid identification of functional biosynthetic pathways, including both soluble and membrane-bound enzymes.
[Mh] Termos MeSH primário: Antraquinonas/química
Antraquinonas/metabolismo
Vias Biossintéticas
Policetídeo Sintases/metabolismo
Tabaco/metabolismo
[Mh] Termos MeSH secundário: Glicosilação
Tabaco/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anthraquinones); 79956-01-7 (Polyketide Synthases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170719
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700331


  6 / 1501 MEDLINE  
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[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


  7 / 1501 MEDLINE  
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[PMID]:28704687
[Au] Autor:Chakraborty K; Thilakan B; Raola VK
[Ad] Endereço:Marine Bioprospecting Section of Biotechnology Division, Central Marine Fisheries Research Institute, Ernakulam North, P.B. No. 1603, Cochin, 682018, Kerala, India. Electronic address: kajal_cmfri@yahoo.com.
[Ti] Título:Antimicrobial polyketide furanoterpenoids from seaweed-associated heterotrophic bacterium Bacillus subtilis MTCC 10403.
[So] Source:Phytochemistry;142:112-125, 2017 Oct.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Brown seaweed Anthophycus longifolius (Turner) Kützing (family Sargassaceae) associated heterotrophic bacterium Bacillus subtilis MTCC 10403 was found to be a potent isolate with broad range of antibacterial activity against important perceptive food pathogens Vibrio parahaemolyticus, V. vulnificus, and Aeromonas hydrophila. This bacterium was positive for polyketide synthetase gene (KC589397), and therefore, was selected to bioprospect specialized metabolites bearing polyketide backbone. Bioactivity-guided chromatographic fractionation of the ethyl acetate extract of the seaweed-associated bacterium segregated four homologous polyketide furanoterpenoids with potential antibacterial activities against clinically important pathogens. The minimum inhibitory concentration (MIC) assay showed that the referral antibiotics tetracycline and ampicillin were active at 25 µg/mL against the test pathogens, whereas the previously undescribed (4E)-methyl 13-((16-(furan-2-yl) ethyl)-octahydro-7-hydroxy-4-((E)-23-methylbut-21-enyl)-2H-chromen-6-yl)-4-methylpent-4-enoate (compound 1) and methyl 3-(hexahydro-9-((E)-3-methylpent-1-enyl)-4H-furo[3,2-g]isochromen-6-yl) propanoate (compound 3) displayed antibacterial activities against the test pathogens at a lesser concentration (MIC < 7 µg/mL). The title compounds were characterized by comprehensive nuclear magnetic resonance and mass spectroscopic experiments. Polyketide synthase catalyzed putative biosynthetic mechanism additionally corroborated the structural ascriptions of the hitherto undescribed furanoterpenoids from seaweed-associated bacterial symbiont. The electronic and hydrophobic parameters appeared to hold a conspicuous part in directing the antibacterial properties of the compounds. Seaweed-associated B. subtilis MTCC 10403 demonstrated to represent a potential source of antimicrobial polyketides for pharmaceutical applications.
[Mh] Termos MeSH primário: Anti-Infecciosos/isolamento & purificação
Anti-Infecciosos/farmacologia
Policetídeos/farmacologia
Terpenos/isolamento & purificação
Terpenos/farmacologia
[Mh] Termos MeSH secundário: Antibacterianos/química
Anti-Infecciosos/química
Bacillus subtilis/metabolismo
Processos Heterotróficos
Testes de Sensibilidade Microbiana
Feófitas/química
Policetídeo Sintases/metabolismo
Policetídeos/química
Policetídeos/isolamento & purificação
Alga Marinha/metabolismo
Terpenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Anti-Infective Agents); 0 (Polyketides); 0 (Terpenes); 79956-01-7 (Polyketide Synthases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE


  8 / 1501 MEDLINE  
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[PMID]:28696720
[Au] Autor:Schleissner C; Cañedo LM; Rodríguez P; Crespo C; Zúñiga P; Peñalver A; de la Calle F; Cuevas C
[Ad] Endereço:Research and Development Department, PharmaMar S.A. , Avenida de los Reyes, 1, Colmenar Viejo 28770, Madrid, Spain.
[Ti] Título:Bacterial Production of a Pederin Analogue by a Free-Living Marine Alphaproteobacterium.
[So] Source:J Nat Prod;80(7):2170-2173, 2017 Jul 28.
[Is] ISSN:1520-6025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The polyketide pederin family are cytotoxic compounds isolated from insects, lichen, and marine sponges. During the past decade, different uncultivable bacteria symbionts have been proposed as the real producers of these compounds, such as those found in insects, lichen, and marine sponges, and their trans-AT polyketide synthase gene clusters have been identified. Herein we report the isolation and biological activities of a new analogue of the pederin family, compound 1, from the culture of a marine heterotrophic alphaproteobacterium, Labrenzia sp. PHM005. This is the first report of the production of a pederin-type compound by a free-living marine bacteria that could be cultured in the laboratory.
[Mh] Termos MeSH primário: Piranos/metabolismo
[Mh] Termos MeSH secundário: Alphaproteobacteria
Animais
Bactérias/metabolismo
Coleópteros/metabolismo
Líquens
Biologia Marinha
Estrutura Molecular
Família Multigênica
Policetídeo Sintases/metabolismo
Poríferos/microbiologia
Piranos/química
Análise de Sequência de DNA
Simbiose
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyrans); 79956-01-7 (Polyketide Synthases); B8F7J348GJ (pederin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jnatprod.7b00408


  9 / 1501 MEDLINE  
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[PMID]:28545544
[Au] Autor:Losada AA; Méndez C; Salas JA; Olano C
[Ad] Endereço:Departamento de Biología Funcional e Instituto Universitario de Oncología del Principado de Asturias (I.U.O.P.A), Universidad de Oviedo, C/Julian Claveria s/n, 33006, Oviedo, Asturias, Spain.
[Ti] Título:Exploring the biocombinatorial potential of benzoxazoles: generation of novel caboxamycin derivatives.
[So] Source:Microb Cell Fact;16(1):93, 2017 May 25.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The biosynthesis pathway of benzoxazole compounds caboxamycin and nataxazole have been recently elucidated. Both compounds share one of their precursors, 3-hydroxyanthranilate (two units in the case of nataxazole). In addition, caboxamycin structure includes a salicylate moiety while 6-methylsalycilate is the third scaffold in nataxazole. Pathways cross-talk has been identified in caboxamycin producer Streptomyces sp. NTK937, between caboxamycin and enterobactin pathways, and nataxazole producer Streptomyces sp. Tü6176, between nataxazole and coelibactin pathways. These events represent a natural form of combinatorial biosynthesis. RESULTS: Eleven novel caboxamycin derivatives, and five putative novel derivatives, bearing distinct substitutions in the aryl ring have been generated. These compounds were produced by heterologous expression of several caboxamycin biosynthesis genes in Streptomyces albus J1074 (two compounds), by combinatorial biosynthesis in Streptomyces sp. NTK937 expressing nataxazole iterative polyketide synthase (two compounds) and by mutasynthesis using a nonproducing mutant of Streptomyces sp. NTK937 (12 compounds). Some of the compounds showed improved bioactive properties in comparison with caboxamycin. CONCLUSIONS: In addition to the benzoxazoles naturally biosynthesized by the caboxamycin and nataxazole producers, a greater structural diversity can be generated by mutasynthesis and heterologous expression of benzoxazole biosynthesis genes, not only in the respective producer strains but also in non-benzoxazole producers such as S. albus strains. These results show that the production of a wide variety of benzoxazoles could be potentially achieved by the sole expression of cbxBCDE genes (or orthologs thereof), supplying an external source of salicylate-like compounds, or with the concomitant expression of other genes capable of synthesizing salicylates, such as cbxA or natPK.
[Mh] Termos MeSH primário: Benzoxazóis/metabolismo
Policetídeo Sintases/metabolismo
Streptomyces/metabolismo
[Mh] Termos MeSH secundário: Benzoxazóis/química
Vias Biossintéticas
Streptomyces/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoxazoles); 0 (caboxamycin); 79956-01-7 (Polyketide Synthases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-017-0709-6


  10 / 1501 MEDLINE  
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[PMID]:28475838
[Au] Autor:Song TY; Xu ZF; Chen YH; Ding QY; Sun YR; Miao Y; Zhang KQ; Niu XM
[Ad] Endereço:State Key Laboratory for Conservation and Utilization of Bio-Resources and Key Laboratory for Microbial Resources of the Ministry of Education, School of Life Science, Yunnan University , Kunming, Yunnan 650091, People's Republic of China.
[Ti] Título:Potent Nematicidal Activity and New Hybrid Metabolite Production by Disruption of a Cytochrome P450 Gene Involved in the Biosynthesis of Morphological Regulatory Arthrosporols in Nematode-Trapping Fungus Arthrobotrys oligospora.
[So] Source:J Agric Food Chem;65(20):4111-4120, 2017 May 24.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Types of polyketide synthase-terpenoid synthase (PKS-TPS) hybrid metabolites, including arthrosporols with significant morphological regulatory activity, have been elucidated from nematode-trapping fungus Arthrobotrys oligospora. A previous study suggested that the gene cluster AOL_s00215 in A. oligospora was involved in the production of arthrosporols. Here, we report that disruption of one cytochrome P450 monooxygenase gene AOL_s00215g280 in the cluster resulted in significant phenotypic difference and much aerial hyphae. A further bioassay indicated that the mutant showed a dramatic decrease in the conidial formation but developed numerous traps and killed 85% nematodes within 6 h in contact with prey, in sharp contrast to the wild-type strain with no obvious response. Chemical investigation revealed huge accumulation of three new PKS-TPS epoxycyclohexone derivatives with different oxygenated patterns around the epoxycyclohexone moiety and the absence of arthrosporols in the cultural broth of the mutant ΔAOL_s00215g280. These findings suggested that a study on the biosynthetic pathway for morphological regulatory metabolites in nematode-trapping fungus would provide an efficient way to develop new fungal biocontrol agents.
[Mh] Termos MeSH primário: Antinematódeos/metabolismo
Ascomicetos/enzimologia
Sistema Enzimático do Citocromo P-450/metabolismo
Proteínas Fúngicas/metabolismo
Nematoides/microbiologia
[Mh] Termos MeSH secundário: Animais
Antinematódeos/química
Ascomicetos/genética
Ascomicetos/crescimento & desenvolvimento
Ascomicetos/metabolismo
Vias Biossintéticas
Sistema Enzimático do Citocromo P-450/genética
Mutação
Nematoides/crescimento & desenvolvimento
Controle Biológico de Vetores
Policetídeo Sintases/genética
Policetídeo Sintases/metabolismo
Esporos Fúngicos/enzimologia
Esporos Fúngicos/genética
Esporos Fúngicos/crescimento & desenvolvimento
Esporos Fúngicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antinematodal Agents); 0 (Fungal Proteins); 79956-01-7 (Polyketide Synthases); 9035-51-2 (Cytochrome P-450 Enzyme System)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170622
[Lr] Data última revisão:
170622
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b01290



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