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[PMID]:28800422
[Au] Autor:Tohtahon Z; Xue J; Han J; Liu Y; Hua H; Yuan T
[Ad] Endereço:The Key Laboratory of Plant Resources and Chemistry of Arid Zone, and State Key Laboratory of Xinjiang Indigenous Medicinal Plants Resource Utilization, Xinjiang Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Urumqi 830011, China; University of Chinese Academy of Sciences
[Ti] Título:Cytotoxic lanostane triterpenoids from the fruiting bodies of Piptoporus betulinus.
[So] Source:Phytochemistry;143:98-103, 2017 Nov.
[Is] ISSN:1873-3700
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Chemical investigation of a bioactive methanolic extract of the fruiting bodies of Piptoporus betulinus led to the isolation of five previously undescribed lanostane triterpenoids named piptolinic acids A-E, as well as five known lanostane triterpenoids. Their structures were elucidated on the basis of 1D and 2D NMR spectroscopic and HRESIMS analysis. Piptolinic acid A with an unusual moiety (3-hydroxy-4-methoxycarbonyl-3-methylbutyryloxy) at C-3 exhibited comparable cytotoxic activity against human promyelocytic leukemia cell line HL-60 (IC = 1.77 µM) and human acute monocytic leukemia cell line THP-1 (IC = 8.21 µM) to those of positive control, fluorouracil (IC = 6.38 and 4.41 µM, respectively).
[Mh] Termos MeSH primário: Antineoplásicos/isolamento & purificação
Antineoplásicos/farmacologia
Ganoderma/química
Triterpenos/isolamento & purificação
Triterpenos/farmacologia
[Mh] Termos MeSH secundário: Antineoplásicos/química
Coriolaceae/química
Ensaios de Seleção de Medicamentos Antitumorais
Carpóforos/química
Células HL-60
Seres Humanos
Estrutura Molecular
Ressonância Magnética Nuclear Biomolecular
Triterpenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Triterpenes)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE


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[PMID]:28602730
[Au] Autor:Avelar M; Olvera C; Aceves-Zamudio D; Folch JL; Ayala M
[Ad] Endereço:Departamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología UNAM, Av. Universidad 2001 Chamilpa, 62210 Cuernavaca, Morelos, Mexico.
[Ti] Título:Recombinant expression of a laccase from Coriolopsis gallica in Pichia pastoris using a modified α-factor preproleader.
[So] Source:Protein Expr Purif;136:14-19, 2017 Aug.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this work we communicate the heterologous expression of a laccase from Coriolopsis gallica in Pichia pastoris. This enzyme has been reported to efficiently degrade a variety of pollutants such as industrial dyes. The expression strategy included using a previously reported modified α-factor preproleader for enhanced secretion and pAOX1, a methanol-responsive promoter. Methanol concentration, copper salts concentration and temperature were varied in order to enhance laccase expression in this heterologous system. A volumetric activity of 250 U/L was achieved after 12-day culture in Fernbach flasks. The protein was recovered from the supernatant and purified, obtaining a preparation with 90% electrophoretic purity. The catalytic constants of the recombinant enzyme are almost identical to the fungal enzyme, thus rendering this system a useful tool for protein engineering of laccase from C. gallica.
[Mh] Termos MeSH primário: Coriolaceae/genética
Proteínas Fúngicas
Expressão Gênica
Lacase
[Mh] Termos MeSH secundário: Coriolaceae/enzimologia
Proteínas Fúngicas/biossíntese
Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Lacase/biossíntese
Lacase/química
Lacase/genética
Pichia/genética
Pichia/metabolismo
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Recombinant Proteins); EC 1.10.3.2 (Laccase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE


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[PMID]:28486485
[Au] Autor:Goodwin JM; Rana H; Ndungu J; Chakrabarti G; Moomaw EW
[Ad] Endereço:Department of Chemistry and Biochemistry, Kennesaw State University, Kennesaw, GA, United States of America.
[Ti] Título:Hydrogen peroxide inhibition of bicupin oxalate oxidase.
[So] Source:PLoS One;12(5):e0177164, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oxalate oxidase is a manganese containing enzyme that catalyzes the oxidation of oxalate to carbon dioxide in a reaction that is coupled with the reduction of oxygen to hydrogen peroxide. Oxalate oxidase from Ceriporiopsis subvermispora (CsOxOx) is the first fungal and bicupin enzyme identified that catalyzes this reaction. Potential applications of oxalate oxidase for use in pancreatic cancer treatment, to prevent scaling in paper pulping, and in biofuel cells have highlighted the need to understand the extent of the hydrogen peroxide inhibition of the CsOxOx catalyzed oxidation of oxalate. We apply a membrane inlet mass spectrometry (MIMS) assay to directly measure initial rates of carbon dioxide formation and oxygen consumption in the presence and absence of hydrogen peroxide. This work demonstrates that hydrogen peroxide is both a reversible noncompetitive inhibitor of the CsOxOx catalyzed oxidation of oxalate and an irreversible inactivator. The build-up of the turnover-generated hydrogen peroxide product leads to the inactivation of the enzyme. The introduction of catalase to reaction mixtures protects the enzyme from inactivation allowing reactions to proceed to completion. Circular dichroism spectra indicate that no changes in global protein structure take place in the presence of hydrogen peroxide. Additionally, we show that the CsOxOx catalyzed reaction with the three carbon substrate mesoxalate consumes oxygen which is in contrast to previous proposals that it catalyzed a non-oxidative decarboxylation with this substrate.
[Mh] Termos MeSH primário: Coriolaceae/enzimologia
Peróxido de Hidrogênio/farmacologia
Oxirredutases/antagonistas & inibidores
[Mh] Termos MeSH secundário: Catálise
Cromatografia Líquida de Alta Pressão
Cinética
Espectrometria de Massas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
BBX060AN9V (Hydrogen Peroxide); EC 1.- (Oxidoreductases); EC 1.2.3.4 (oxalate oxidase)
[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:170510
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177164


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[PMID]:28391562
[Au] Autor:Rizqi HD; Purnomo AS
[Ad] Endereço:Department of Chemistry, Faculty of Mathematics and Natural Science, Institut Teknologi Sepuluh Nopember (ITS), Kampus ITS Sukolilo, Surabaya, 60111, Indonesia.
[Ti] Título:The ability of brown-rot fungus Daedalea dickinsii to decolorize and transform methylene blue dye.
[So] Source:World J Microbiol Biotechnol;33(5):92, 2017 May.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The ability of Daedalea dickinsii to decolorize and transform methylene blue (MB) dye was investigated. MB was decolorized in potato dextrose agar medium after adding MB at concentrations of 50, 75, and 100 mg L . D. dickinsii decolorized MB with decolorization index values of 0.92, 0.90, and 0.88 at MB concentrations of 50, 75, and 100 mg L , respectively. The 100 mg L MB concentration was selected for biotransformation in liquid potato dextrose broth medium. D. dickinsii transformed approximately 54% of the MB after a 14-day incubation. 3-(Dimethylamino)-7-(methylamino) phenothiazine (C H N S), 3,7-bis(dimethylamino)-4aH-phenothiazin-5-one (C H N SO), and 4-(dimethylamino)-2-[m(dimethylamino) phenylsulfinyl] benzenamine (C H N SO) were detected as MB metabolic products. This is the first report of MB transformation by the brown-rot fungi D. dickinsii. These results indicate that D. dickinsii can be used to decolorize and biotransform MB dye.
[Mh] Termos MeSH primário: Coriolaceae/fisiologia
Azul de Metileno/química
Poluentes Químicos da Água/química
[Mh] Termos MeSH secundário: Biodegradação Ambiental
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Water Pollutants, Chemical); T42P99266K (Methylene Blue)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170410
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-017-2256-z


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[PMID]:28378220
[Au] Autor:Pleszczynska M; Lemieszek MK; Siwulski M; Wiater A; Rzeski W; Szczodrak J
[Ad] Endereço:Department of Industrial Microbiology, Maria Curie-Sklodowska University, Akademicka 19, 20-033, Lublin, Poland. m.pleszczynska@poczta.umcs.lublin.pl.
[Ti] Título:Fomitopsis betulina (formerly Piptoporus betulinus): the Iceman's polypore fungus with modern biotechnological potential.
[So] Source:World J Microbiol Biotechnol;33(5):83, 2017 May.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Higher Basidiomycota have been used in natural medicine throughout the world for centuries. One of such fungi is Fomitopsis betulina (formerly Piptoporus betulinus), which causes brown rot of birch wood. Annual white to brownish fruiting bodies of the species can be found on trees in the northern hemisphere but F. betulina can also be cultured as a mycelium and fruiting body. The fungus has a long tradition of being applied in folk medicine as an antimicrobial, anticancer, and anti-inflammatory agent. Probably due to the curative properties, pieces of its fruiting body were carried by Ötzi the Iceman. Modern research confirms the health-promoting benefits of F. betulina. Pharmacological studies have provided evidence supporting the antibacterial, anti-parasitic, antiviral, anti-inflammatory, anticancer, neuroprotective, and immunomodulating activities of F. betulina preparations. Biologically active compounds such as triterpenoids have been isolated. The mushroom is also a reservoir of valuable enzymes and other substances such as cell wall (1→3)-α-D-glucan which can be used for induction of microbial enzymes degrading cariogenic dental biofilm. In conclusion, F. betulina can be considered as a promising source for the development of new products for healthcare and other biotechnological uses.
[Mh] Termos MeSH primário: Coriolaceae/química
Carpóforos/química
[Mh] Termos MeSH secundário: Biotecnologia
Indústria Farmacêutica
Medicina Tradicional
Terpenos/isolamento & purificação
Terpenos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Terpenes)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170419
[Lr] Data última revisão:
170419
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-017-2247-0


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[PMID]:28213299
[Au] Autor:Liu X; Hiligsmann S; Gourdon R; Bayard R
[Ad] Endereço:Univ. Lyon, INSA-Lyon, DEEP Laboratory, EA4126, Bldg. S. Carnot, 20 Avenue A. Einstein, F-69621 Villeurbanne, France.
[Ti] Título:Anaerobic digestion of lignocellulosic biomasses pretreated with Ceriporiopsis subvermispora.
[So] Source:J Environ Manage;193:154-162, 2017 May 15.
[Is] ISSN:1095-8630
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Fungal pretreatment by Ceriporiopsis subvermispora of two forest residues (hazel and acacia branches) and two agricultural lignocellulosic residues (barley straw and sugarcane bagasse) were studied as a pretreatment to improve their subsequent anaerobic digestion for methane production. Biomass samples were grinded to 2 ranges of particle sizes (<4 or 1 mm), autoclaved, inoculated with two strains of C. subvermispora (ATCC 90467 and ATCC 96608) and incubated at 28 °C for 28 days. The effects of fungal pretreatment were assessed by analyzing the samples before and after incubations for dry solids mass, biochemical composition, bio-methane production (BMP) and availability of cellulose to hydrolysis. The production of ligninolytic enzymes MnP and/or laccase was observed with both strains during incubation on most of the samples tested. It almost doubled the hazel branches BMP per unit mass of dry solids but did not improve however the BMP of the agricultural residues and acacia branches. These observations were explained by the fact that although both strains were able to degrade 20-25% of lignin in <1 mm and <4 mm hazel branches samples, none of them was successful however to significantly degrade lignin in the other samples, except for sugarcane bagasse.
[Mh] Termos MeSH primário: Biomassa
Coriolaceae/metabolismo
[Mh] Termos MeSH secundário: Hidrólise
Lignina/química
Saccharum/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9005-53-2 (Lignin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170219
[St] Status:MEDLINE


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[PMID]:28130302
[Au] Autor:Presley GN; Schilling JS
[Ad] Endereço:University of Minnesota Department of Bioproducts and Biosystems Engineering, St. Paul, Minnesota, USA.
[Ti] Título:Distinct Growth and Secretome Strategies for Two Taxonomically Divergent Brown Rot Fungi.
[So] Source:Appl Environ Microbiol;83(7), 2017 Apr 01.
[Is] ISSN:1098-5336
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Brown rot fungi are wood-degrading fungi that employ both oxidative and hydrolytic mechanisms to degrade wood. Hydroxyl radicals that facilitate the oxidative component are powerful nonselective oxidants and are incompatible with hydrolytic enzymes unless they are spatially segregated in wood. Differential gene expression has been implicated in the segregation of these reactions in , but it is unclear if this two-step mechanism varies in other brown rot fungi with different traits and life history strategies that occupy different niches in nature. We employed proteomics to analyze a progression of wood decay on thin wafers, using brown rot fungi with significant taxonomic and niche distances: (Boletales; "dry rot" lumber decay) and (order Gloeophyllales; slash, downed wood). Both fungi produced greater oxidoreductase diversity upon wood colonization and greater glycoside hydrolase activity later, consistent with a two-step mechanism. The two fungi invested very differently, however, in terms of growth (infrastructure) versus protein secretion (resource capture), with the ergosterol/extracted protein ratio being 7-fold higher with than with In line with the native substrate associations of these fungi, hemicellulase-specific activities were dominated by mannanase in and by xylanase in Consistent with previous observations, did not produce glycoside hydrolase 6 (GH6) cellobiohydrolases (CBHs) in this study, despite taxonomically belonging to the order Boletales, which is distinguished among brown rot fungi by having CBH genes. This work suggests that distantly related brown rot fungi employ staggered mechanisms to degrade wood, but the underlying strategies vary among taxa. Wood-degrading fungi are important in forest nutrient cycling and offer promise in biotechnological applications. Brown rot fungi are unique among these fungi in that they use a nonenzymatic oxidative pretreatment before enzymatic carbohydrate hydrolysis, enabling selective removal of carbohydrates from lignin. This capacity has independently evolved multiple times, but it is unclear if different mechanisms underpin similar outcomes. Here, we grew fungi directionally on wood wafers and we found similar two-step mechanisms in taxonomically divergent brown rot fungi. The results, however, revealed strikingly different growth strategies, with investing more in biomass production than secretion of proteins and showing the opposite pattern, with a high diversity of uncharacterized proteins. The "simplified" secretomic system could help narrow gene targets central to oxidative brown rot pretreatments, and a comparison of its distinctions with and other brown rot fungi (e.g., ) might offer similar traction in noncatabolic genes.
[Mh] Termos MeSH primário: Basidiomycota/crescimento & desenvolvimento
Basidiomycota/metabolismo
Coriolaceae/crescimento & desenvolvimento
Coriolaceae/metabolismo
Proteínas Fúngicas/metabolismo
Madeira/microbiologia
[Mh] Termos MeSH secundário: Basidiomycota/classificação
Basidiomycota/genética
Biomassa
Celulose 1,4-beta-Celobiosidase/metabolismo
Coriolaceae/classificação
Coriolaceae/genética
Glicosídeo Hidrolases/biossíntese
Glicosídeo Hidrolases/metabolismo
Hidrólise
Lignina/metabolismo
Oxirredução
Proteômica
Madeira/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 9005-53-2 (Lignin); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.- (hemicellulase); EC 3.2.1.91 (Cellulose 1,4-beta-Cellobiosidase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE


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[PMID]:28065548
[Au] Autor:Voberková S; Vaverková MD; Buresová A; Adamcová D; Vrsanská M; Kynický J; Brtnický M; Adam V
[Ad] Endereço:Department of Chemistry and Biochemistry, Faculty of Agronomy, Mendel University in Brno, Zemedelská 1/1665, 613 00, Czech Republic. Electronic address: stanislava.voberkova@mendelu.cz.
[Ti] Título:Effect of inoculation with white-rot fungi and fungal consortium on the composting efficiency of municipal solid waste.
[So] Source:Waste Manag;61:157-164, 2017 Mar.
[Is] ISSN:1879-2456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:An investigation was carried out on the effect of inoculation methods on the compost of an organic fraction of municipal solid waste. Three types of white-rot fungi (Phanerochaete chrysosporium, Trametes versicolor and Fomes fomentarius), and a consortium of these fungi, were used. The study assessed their influence on microbial enzymatic activities and the quality of the finished compost. It was found that the addition of white-rot fungi to municipal solid waste (after 37days of composting) could be a useful strategy for enhancing the properties of the final compost product. In comparison with the control sample (compost without inoculation), it accelerates degradation of solid waste as indicated by changes in C/N, electrical conductivity and pH. However, the effectiveness of waste degradation and compost maturation depends on the type of microorganism used for inoculation. The presence of inoculants, such as Trametes versicolor and Fomes fomentarius, led to a higher degrading ratio and a better degree of maturity. This resulted in an increase of enzymatic activities (especially dehydrogenase and protease) and a germination index in comparison with inoculation using Phanerochaete chrysosporium or a consortium of fungi.
[Mh] Termos MeSH primário: Fungos/metabolismo
Eliminação de Resíduos/métodos
Microbiologia do Solo
Solo
Resíduos Sólidos
[Mh] Termos MeSH secundário: Biodegradação Ambiental
Carbono/metabolismo
Coriolaceae/metabolismo
Enzimas/metabolismo
Concentração de Íons de Hidrogênio
Nitrogênio/metabolismo
Phanerochaete/metabolismo
Trametes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes); 0 (Soil); 0 (Solid Waste); 7440-44-0 (Carbon); N762921K75 (Nitrogen)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170110
[St] Status:MEDLINE


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[PMID]:28062355
[Au] Autor:Nishimura H; Yamaguchi D; Watanabe T
[Ad] Endereço:Laboratory of Biomass Conversion, Research Institute for Sustainable Humanosphere (RISH), Kyoto University, Gokasho, Uji, Kyoto, Japan. Electronic address: hiroshi_nishimura@rish.kyoto-u.ac.jp.
[Ti] Título:Cerebrosides, extracellular glycolipids secreted by the selective lignin-degrading fungus Ceriporiopsis subvermispora.
[So] Source:Chem Phys Lipids;203:1-11, 2017 Mar.
[Is] ISSN:1873-2941
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Ceriporiopsis subvermispora is a selective white-rot fungus that degrades lignin at a site far from the hyphae and extracellular enzymes, without intensive damage to the cellulose. In selective ligninolysis, low molecular mass metabolites play a principal role and amphipathic substances are involved to control the degradation and transport of hydrophobic aromatic molecules, including lignin and lipids; however, secretion of the amphipathic substances by this fungus has not been well understood, except for alk(en)yl itaconates called ceriporic acids, which have a weak amphiphilicity. Herein, we report for the first time that the fungus secretes cerebrosides that are classified as glycosphingolipids. By using liquid chromatography electron spray ionization mass spectrometry (LC-ESI-MS) and nuclear magnetic resonance (NMR) spectroscopy coupled with stable isotope feeding experiments with C-glucose and N-ammonium sulfate, the cerebrosides were determined to be N-hydroxyoctadecanoyl-1-O-ß-d-glucopyranosyl-4E,8E-sphingadienine, N-hydroxyoctadecanoyl-1-O-ß-d-glucopyranosyl-4E,8Z-sphingadienine, and N-hydroxyoctadecanoyl-1-O-ß-d-glucopyranosyl-9-methyl-4E,8E-sphingadienine. The cerebrosides are strong amphipathic substances and potential metabolites for regulating difference and symbiosis within the microbial community.
[Mh] Termos MeSH primário: Cerebrosídeos/metabolismo
Coriolaceae/metabolismo
Lignina/metabolismo
[Mh] Termos MeSH secundário: Cerebrosídeos/química
Lignina/química
Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cerebrosides); 9005-53-2 (Lignin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170502
[Lr] Data última revisão:
170502
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170108
[St] Status:MEDLINE


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[PMID]:27875934
[Au] Autor:Chen Y; Cao Q; Tao X; Shao H; Zhang K; Zhang Y; Tan X
[Ad] Endereço:a The Key Laboratory for Bio-Resources and Eco-Environment of Ministry of Education, Sichuan Key Laboratory of Molecular Biology and Biotechnology , College of Life Sciences, Sichuan University , Chengdu , China.
[Ti] Título:Analysis of de novo sequencing and transcriptome assembly and lignocellulolytic enzymes gene expression of Coriolopsis gallica HTC.
[So] Source:Biosci Biotechnol Biochem;81(3):460-468, 2017 Mar.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:White-rot basidiomycete Coriolopsis gallica HTC is one of the main biodegraders of poplar. In our previous study, we have shown the strong capacity of C. gallica HTC to degrade lignocellulose. In this study, equal amounts of total RNA fromC. Gallica HTC cultures grown in different conditions were pooled together. Illumina paired-end RNA sequencing was performed, and 13.2 million 90-bp paired-end reads were generated. We chose the Merged Assembly of Oases data-set for the following blast searches and gene ontology analyses. The reads were assembled de novo into 28,034 transcripts (≥ 100 bp) using combined assembly strategy MAO. The transcripts were annotated using Blast2GO. In all, 18,810 transcripts (≥100 bp) achieved BLASTX hits, of which, 7048 transcripts had GO term and 2074 had ECs. The expression level of 11 lignocellulolytic enzyme genes from the assembled C. gallica HTC transcriptome were detected by real-time quantitative polymerase chain reaction. The results showed that expression levels of these genes were affected by carbon source and nitrogen source at the level of transcription. The current abundant transcriptome data allowed the identification of many new transcripts in C. gallica HTC. Data provided here represent the most comprehensive and integrated genomic resources for cloning and identifying genes of interest from C. gallica HTC. Characterization of C. gallica HTC transcriptome provides an effective tool to understand mechanisms underlying cellular and molecular functions of C. gallica HTC.
[Mh] Termos MeSH primário: Coriolaceae/enzimologia
Coriolaceae/genética
Enzimas/genética
Perfilação da Expressão Gênica/métodos
Regulação Fúngica da Expressão Gênica
Lignina/metabolismo
[Mh] Termos MeSH secundário: Enzimas/metabolismo
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Ontologia Genética
Sequenciamento de Nucleotídeos em Larga Escala/métodos
Lignina/genética
Fases de Leitura Aberta
Reação em Cadeia da Polimerase em Tempo Real
Transcriptoma
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes); 0 (Fungal Proteins); 11132-73-3 (lignocellulose); 9005-53-2 (Lignin)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170306
[Lr] Data última revisão:
170306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161124
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2016.1182418



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