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[PMID]:29293326
[Au] Autor:Ide M; Okumura M; Koizumi K; Kumagai M; Yoshida I; Yoshida M; Mishima T; Nakamura M
[Ad] Endereço:Japan Food Research Laboratories , Osaka 567-0085, Japan.
[Ti] Título:Novel Method to Quantify ß-Glucan in Processed Foods: Sodium Hypochlorite Extracting and Enzymatic Digesting (SEED) Assay.
[So] Source:J Agric Food Chem;66(4):1033-1038, 2018 Jan 31.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Some ß-glucans have attracted attention due to their functionality as an immunostimulant and have been used in processed foods. However, accurately measuring the ß-glucan content of processed foods using existing methods is difficult. We demonstrate a new method, the Sodium hypochlorite Extracting and Enzymatic Digesting (SEED) assay, in which ß-glucan is extracted using sodium hypochlorite, dimethyl sulfoxide, and 5 mol/L sodium hydroxide and then digested into ß-glucan fragments using Westase which is an enzyme having ß-1,6- and ß-1,3 glucanase activity. The ß-glucan fragments are further digested into glucose using exo-1,3-ß-d-glucanase and ß-glucosidase. We measured ß-glucan comprising ß-1,3-, -1,6-, and -1,(3),4- bonds in various polysaccharide reagents and processed foods using our novel method. The SEED assay was able to quantify ß-glucan with good reproducibility, and the recovery rate was >90% for food containing ß-glucan. Therefore, the SEED assay is capable of accurately measuring the ß-glucan content of processed foods.
[Mh] Termos MeSH primário: Análise de Alimentos/métodos
Hipoclorito de Sódio
beta-Glucanas/análise
[Mh] Termos MeSH secundário: Manipulação de Alimentos
Glucana 1,3-beta-Glucosidase/metabolismo
Glucanos/química
Hordeum/química
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucans); 0 (beta-Glucans); 9008-22-4 (laminaran); DY38VHM5OD (Sodium Hypochlorite); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase); EC 3.2.1.58 (beta-1,3-exoglucanase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05044


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[PMID]:28827308
[Au] Autor:Hettle A; Fillo A; Abe K; Massel P; Pluvinage B; Langelaan DN; Smith SP; Boraston AB
[Ad] Endereço:From the Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada and.
[Ti] Título:Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of ß-1,3-glucan.
[So] Source:J Biol Chem;292(41):16955-16968, 2017 Oct 13.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BH0236 from is a multimodular ß-1,3-glucanase comprising an N-terminal family 81 glycoside hydrolase catalytic module, an internal family 6 carbohydrate-binding module (CBM) that binds the nonreducing end of ß-1,3-glucan chains, and an uncharacterized C-terminal module classified into CBM family 56. Here, we determined that this latter CBM, BhCBM56, bound the soluble ß-1,3-glucan laminarin with a dissociation constant ( ) of ∼26 µm and displayed higher affinity for insoluble ß-1,3-glucans with values of ∼2-10 µm but lacked affinity for ß-1,3-glucooligosaccharides. The X-ray crystal structure of BhCBM56 and NMR-derived chemical shift mapping of the binding site revealed a ß-sandwich fold, with the face of one ß-sheet possessing the ß-1,3-glucan-binding surface. On the basis of the functional and structural properties of BhCBM56, we propose that it binds a quaternary polysaccharide structure, most likely the triple helix adopted by polymerized ß-1,3-glucans. Consistent with the BhCBM56 and BhCBM6/56 binding profiles, deletion of the CBM56 from BH0236 decreased activity of the enzyme on the insoluble ß-1,3-glucan curdlan but not on soluble laminarin; additional deletion of the CBM6 also did not affect laminarin degradation but further decreased curdlan hydrolysis. The pseudo-atomic solution structure of BH0236 determined by small-angle X-ray scattering revealed structural insights into the nature of avid binding by the BhCBM6/56 pair and how the orientation of the active site in the catalytic module factors into recognition and degradation of ß-1,3-glucans. Our findings reinforce the notion that catalytic modules and their cognate CBMs have complementary specificities, including targeting of polysaccharide quaternary structure.
[Mh] Termos MeSH primário: Bacillus/enzimologia
Proteínas de Bactérias/química
Glucana 1,3-beta-Glucosidase/química
[Mh] Termos MeSH secundário: Bacillus/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Cristalografia por Raios X
Glucana 1,3-beta-Glucosidase/genética
Glucana 1,3-beta-Glucosidase/metabolismo
Polissacarídeos/química
Polissacarídeos/metabolismo
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Polysaccharides); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.806711


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[PMID]:28658312
[Au] Autor:Nayyar S; Sharma BK; Kaur A; Kalia A; Sanghera GS; Thind KS; Yadav IS; Sandhu JS
[Ad] Endereço:School of Agricultural Biotechnology, Punjab Agricultural University, Ludhiana, India.
[Ti] Título:Red rot resistant transgenic sugarcane developed through expression of ß-1,3-glucanase gene.
[So] Source:PLoS One;12(6):e0179723, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sugarcane (Saccharum spp.) is a commercially important crop, vulnerable to fungal disease red rot caused by Colletotrichum falcatum Went. The pathogen attacks sucrose accumulating parenchyma cells of cane stalk leading to severe losses in cane yield and sugar recovery. We report development of red rot resistant transgenic sugarcane through expression of ß-1,3-glucanase gene from Trichoderma spp. The transgene integration and its expression were confirmed by quantitative reverse transcription-PCR in first clonal generation raised from T0 plants revealing up to 4.4-fold higher expression, in comparison to non-transgenic sugarcane. Bioassay of transgenic plants with two virulent C. falcatum pathotypes, Cf 08 and Cf 09 causing red rot disease demonstrated that some plants were resistant to Cf 08 and moderately resistant to Cf 09. The electron micrographs of sucrose storing stalk parenchyma cells from these plants displayed characteristic sucrose-filled cells inhibiting Cf 08 hyphae and lysis of Cf 09 hyphae; in contrast, the cells of susceptible plants were sucrose depleted and prone to both the pathotypes. The transgene expression was up-regulated (up to 2.0-fold in leaves and 5.0-fold in roots) after infection, as compared to before infection in resistant plants. The transgene was successfully transmitted to second clonal generation raised from resistant transgenic plants. ß-1,3-glucanase protein structural model revealed that active sites Glutamate 628 and Aspartate 569 of the catalytic domain acted as proton donor and nucleophile having role in cleaving ß-1,3-glycosidic bonds and pathogen hyphal lysis.
[Mh] Termos MeSH primário: Resistência à Doença/genética
Glucana 1,3-beta-Glucosidase/genética
Doenças das Plantas/prevenção & controle
Plantas Geneticamente Modificadas/genética
Saccharum/genética
[Mh] Termos MeSH secundário: Colletotrichum/patogenicidade
Regulação da Expressão Gênica de Plantas/genética
Genes de Plantas/genética
Glucana 1,3-beta-Glucosidase/metabolismo
Doenças das Plantas/genética
Plantas Geneticamente Modificadas/enzimologia
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Saccharum/enzimologia
Trichoderma/enzimologia
Trichoderma/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179723


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[PMID]:28154008
[Au] Autor:Garfoot AL; Dearing KL; VanSchoiack AD; Wysocki VH; Rappleye CA
[Ad] Endereço:From the Departments of Microbiology, Microbial Infection, and Immunity and.
[Ti] Título:Eng1 and Exg8 Are the Major ß-Glucanases Secreted by the Fungal Pathogen .
[So] Source:J Biol Chem;292(12):4801-4810, 2017 Mar 24.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fungal cell walls contain ß-glucan polysaccharides that stimulate immune responses when recognized by host immune cells. The fungal pathogen minimizes detection of ß-glucan by host cells through at least two mechanisms: concealment of ß-glucans beneath α-glucans and enzymatic removal of any exposed ß-glucan polysaccharides by the secreted glucanase Eng1. yeasts also secrete the putative glucanase Exg8, which may serve a similar role as Eng1 in removing exposed ß-glucans from the yeast cell surface. Here, we characterize the enzymatic specificity of the Eng1 and Exg8 proteins and show that Exg8 is an exo-ß1,3-glucanase and Eng1 is an endo-ß1,3-glucanase. Together, Eng1 and Exg8 account for nearly all of the total secreted glucanase activity of yeasts. Both Eng1 and Exg8 proteins are secreted through a conventional secretion signal and are modified post-translationally by -linked glycosylation. Both glucanases have near maximal activity at temperature and pH conditions experienced during infection of host cells, supporting roles in pathogenesis. Exg8 has a higher specific activity than Eng1 for ß1,3-glucans; yet despite this, Exg8 does not reduce detection of yeasts by the host ß-glucan receptor Dectin-1. Exg8 is largely dispensable for virulence , in contrast to Eng1. These results show that yeasts secrete two ß1,3-glucanases and that Eng1 endoglucanase activity is the predominant factor responsible for removal of exposed cell wall ß-glucans to minimize host detection of yeasts.
[Mh] Termos MeSH primário: Glucana 1,3-beta-Glucosidase/metabolismo
Glucana Endo-1,3-beta-D-Glucosidase/metabolismo
Histoplasma/enzimologia
Histoplasmose/microbiologia
[Mh] Termos MeSH secundário: Histoplasma/metabolismo
Histoplasma/patogenicidade
Seres Humanos
Especificidade por Substrato
beta-Glucanas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta-Glucans); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase); EC 3.2.1.58 (beta-1,3-exoglucanase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170204
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.762104


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[PMID]:27894990
[Au] Autor:Ribeiro TC; Weiblen C; de Azevedo MI; de Avila Botton S; Robe LJ; Pereira DI; Monteiro DU; Lorensetti DM; Santurio JM
[Ad] Endereço:Laboratório de Pesquisas Micológicas, Departamento de Microbiologia e Parasitologia, Centro de Ciências da Saúde, Programa de Pós-graduação em Farmacologia (PPGF), Universidade Federal de Santa Maria (UFSM), Santa Maria, RS, Brazil.
[Ti] Título:Microevolutionary analyses of Pythium insidiosum isolates of Brazil and Thailand based on exo-1,3-ß-glucanase gene.
[So] Source:Infect Genet Evol;48:58-63, 2017 Mar.
[Is] ISSN:1567-7257
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pythium insidiosum is an important oomycete due to its ability to infect humans and animals. It causes pythiosis, a disease of difficult treatment that occurs more frequently in humans in Thailand and in horses in Brazil. Since cell-wall components are frequently related to host shifts, we decided here to use sequences from the exo-1,3-ß-glucanase gene (exo1), which encodes an immunodominant protein putatively involved in cell wall remodeling, to investigate the microevolutionary relationships of Brazilian and Thai isolates of P. insidiosum. After neutrality ratification, the phylogenetic analyses performed through Maximum parsimony (MP), Neighbor-joining (NJ), Maximum likelihood (ML), and Bayesian analysis (BA) strongly supported Thai isolates being paraphyletic in relation to those from Brazil. The structure recovered by these analyses, as well as by Spatial Analysis of Molecular Variance (SAMOVA), suggests the subdivision of P. insidiosum into three clades or population groups, which are able to explain almost 81% of the variation encountered for exo1. Moreover, the two identified Thai clades were almost as strongly differentiated between each other, as they were from the Brazilian clade, suggesting an ancient Asian subdivision. The derived positioning in the phylogenetic tree, linked to the lower diversity values and the recent expansion signs detected for the Brazilian clade, further support this clade as derived in relation to the Asian populations. Thus, although some patterns presented here are compatible with those recovered with different molecular markers, exo1 was revealed to be a good marker for studying evolution in Pythium, providing robust and strongly supported results with regard to the patterns of origin and diversification of P. insidiosum.
[Mh] Termos MeSH primário: Glucana 1,3-beta-Glucosidase/genética
Pythium/genética
[Mh] Termos MeSH secundário: Brasil
Evolução Molecular
Variação Genética
Filogenia
Pythium/enzimologia
Tailândia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161130
[St] Status:MEDLINE


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[PMID]:27854040
[Au] Autor:Jiang C; Song J; Cong H; Zhang J; Yang Q
[Ad] Endereço:School of Life Science and Technology, Harbin Institute of Technology, Nangang District, Harbin, People's Republic of China.
[Ti] Título:Expression and Characterization of a Novel Antifungal Exo-ß-1,3-glucanase from Chaetomium cupreum.
[So] Source:Appl Biochem Biotechnol;182(1):261-275, 2017 May.
[Is] ISSN:1559-0291
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A novel ß-1,3-glucanase gene, designated Ccglu17A, was cloned from the biological control fungus Chaetomium cupreum Ame. Its 1626-bp open reading frame encoded 541 amino acids. The corresponding amino acid sequence showed highest identity (67 %) with a glycoside hydrolase family 17 ß-1,3-glucanase from Chaetomium globosum. The recombinant protein Ccglu17A was successfully expressed in Pichia pastoris, and the enzyme was purified to homogeneity with 10.1-fold purification and 47.8 % recovery yield. The protein's molecular mass was approximately 65 kDa, and its maximum activity appeared at pH 5.0 and temperature 45 °C. Heavy metal ions Fe , Mn , Cu , Co , Ag , and Hg had inhibitory effects on Ccglu17A, but Ba promoted the enzyme's activity. Ccglu17A exhibited high substrate specificity, almost exclusively catalyzing ß-1,3-glycosidic bond cleavage in various polysaccharoses to liberate glucose. The enzyme had a Km of 2.84 mg/mL and Vmax of 10.7 µmol glucose/min/mg protein for laminarin degradation under optimal conditions. Ccglu17A was an exoglucanase with transglycosylation activity based on its hydrolytic properties. It showed potential antifungal activity with a degradative effect on cell walls and inhibitory action against the germination of pathogenic fungus. In conclusion, Ccglu17A is the first functional exo-1,3-ß-glucanase to be identified from C. cupreum and has potential applicability in industry and agriculture.
[Mh] Termos MeSH primário: Antifúngicos/química
Chaetomium/enzimologia
Proteínas Fúngicas/metabolismo
Glucana 1,3-beta-Glucosidase/metabolismo
Glucanos/metabolismo
[Mh] Termos MeSH secundário: Antifúngicos/metabolismo
Antifúngicos/farmacologia
Cátions Bivalentes
Chaetomium/química
Chaetomium/classificação
Clonagem Molecular
Proteínas Fúngicas/genética
Proteínas Fúngicas/farmacologia
Fusarium/efeitos dos fármacos
Fusarium/crescimento & desenvolvimento
Expressão Gênica
Glucana 1,3-beta-Glucosidase/genética
Glucana 1,3-beta-Glucosidase/farmacologia
Glucanos/química
Concentração de Íons de Hidrogênio
Cinética
Metais Pesados/química
Peso Molecular
Fases de Leitura Aberta
Filogenia
Pichia/genética
Pichia/metabolismo
Plasmídeos/química
Plasmídeos/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteínas Recombinantes/farmacologia
Esporos Fúngicos/efeitos dos fármacos
Esporos Fúngicos/crescimento & desenvolvimento
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Cations, Divalent); 0 (Fungal Proteins); 0 (Glucans); 0 (Metals, Heavy); 0 (Recombinant Proteins); 9008-22-4 (laminaran); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161118
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-016-2325-z


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[PMID]:27580619
[Au] Autor:Michalko J; Renner T; Mészáros P; Socha P; Moravcíková J; Blehová A; Libantová J; Polóniová Z; Matusíková I
[Ad] Endereço:Institute of Plant Genetics and Biotechnology, Slovak Academy of Sciences, Akademická 2, P.O. Box 39A, 950 07, Nitra, Slovak Republic.
[Ti] Título:Molecular characterization and evolution of carnivorous sundew (Drosera rotundifolia L.) class V ß-1,3-glucanase.
[So] Source:Planta;245(1):77-91, 2017 Jan.
[Is] ISSN:1432-2048
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:MAIN CONCLUSION: A gene for ß-1,3-glucanase was isolated from carnivorous sundew. It is active in leaves and roots, but not in digestive glands. Analyses in transgenic tobacco suggest its function in germination. Ancestral plant ß-1,3-glucanases (EC 3.2.1.39) played a role in cell division and cell wall remodelling, but divergent evolution has extended their roles in plant defense against stresses to decomposition of prey in carnivorous plants. As available gene sequences from carnivorous plants are rare, we isolated a glucanase gene from roundleaf sundew (Drosera rotundifolia L.) by a genome walking approach. Computational predictions recognized typical gene features and protein motifs described for other plant ß-1,3-glucanases. Phylogenetic reconstructions suggest strong support for evolutionary relatedness to class V ß-1,3-glucanases, including homologs that are active in the traps of related carnivorous species. The gene is expressed in sundew vegetative tissues but not in flowers and digestive glands, and encodes for a functional enzyme when expressed in transgenic tobacco. Detailed analyses of the supposed promoter both in silico and in transgenic tobacco suggest that this glucanase plays a role in development. Specific spatiotemporal activity was observed during transgenic seed germination. Later during growth, the sundew promoter was active in marginal and sub-marginal areas of apical true leaf meristems of young tobacco plants. These results suggest that the isolated glucanase gene is regulated endogenously, possibly by auxin. This is the first report on a nuclear gene study from sundew.
[Mh] Termos MeSH primário: Drosera/enzimologia
Evolução Molecular
Glucana 1,3-beta-Glucosidase/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Simulação por Computador
Drosera/genética
Genes de Plantas
Glucana 1,3-beta-Glucosidase/química
Glucana 1,3-beta-Glucosidase/metabolismo
Glucuronidase/metabolismo
Motivos de Nucleotídeos
Filogenia
Plantas Geneticamente Modificadas
Regiões Promotoras Genéticas/genética
Alinhamento de Sequência
Estresse Fisiológico/genética
Tabaco/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Transcription Factors); EC 3.2.1.31 (Glucuronidase); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160902
[St] Status:MEDLINE
[do] DOI:10.1007/s00425-016-2592-5


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[PMID]:27733120
[Au] Autor:Su Y; Xu L; Wang Z; Peng Q; Yang Y; Chen Y; Que Y
[Ad] Endereço:Key Laboratory of Sugarcane Biology and Genetic Breeding, Ministry of Agriculture, Fujian Agriculture and Forestry University, Fuzhou, 350002, China.
[Ti] Título:Comparative proteomics reveals that central metabolism changes are associated with resistance against Sporisorium scitamineum in sugarcane.
[So] Source:BMC Genomics;17(1):800, 2016 10 12.
[Is] ISSN:1471-2164
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Sugarcane smut, which is caused by Sporisorium scitamineum, has been threatening global sugarcane production. Breeding smut resistant sugarcane varieties has been proven to be the most effective method of controlling this particular disease. However, a lack of genome information of sugarcane has hindered the development of genome-assisted resistance breeding programs. Furthermore, the molecular basis of sugarcane response to S. scitamineum infection at the proteome level was incomplete and combining proteomic and transcriptional analysis has not yet been conducted. RESULTS: We identified 273 and 341 differentially expressed proteins in sugarcane smut-resistant (Yacheng05-179) and susceptible (ROC22) genotypes at 48 h after inoculation with S. scitamineum by employing an isobaric tag for relative and absolute quantification (iTRAQ). The proteome quantitative data were then validated by multiple reaction monitoring (MRM). The integrative analysis showed that the correlations between the quantitative proteins and the corresponding genes that was obtained in our previous transcriptome study were poor, which were 0.1502 and 0.2466 in Yacheng05-179 and ROC22, respectively, thereby revealing a post-transcriptional event during Yacheng05-179-S. scitamineum incompatible interaction and ROC22-S. scitamineum compatible interaction. Most differentially expressed proteins were closely related to sugarcane smut resistance such as beta-1,3-glucanase, peroxidase, pathogenesis-related protein 1 (PR1), endo-1,4-beta-xylanase, heat shock protein, and lectin. Ethylene and gibberellic acid pathways, phenylpropanoid metabolism and PRs, such as PR1, PR2, PR5 and PR14, were more active in Yacheng05-179, which suggested of their possible roles in sugarcane smut resistance. However, calcium signaling, reactive oxygen species, nitric oxide, and abscisic acid pathways in Yacheng05-179 were repressed by S. scitamineum and might not be crucial for defense against this particular pathogen. CONCLUSIONS: These results indicated complex resistance-related events in sugarcane-S. scitamineum interaction, and provided novel insights into the molecular mechanism underlying the response of sugarcane to S. scitamineum infection.
[Mh] Termos MeSH primário: Resistência à Doença
Metabolismo Energético
Proteoma
Proteômica
Saccharum/metabolismo
Saccharum/microbiologia
[Mh] Termos MeSH secundário: Basidiomycota
Sinalização do Cálcio
Regulação da Expressão Gênica de Plantas
Glucana 1,3-beta-Glucosidase/metabolismo
Interações Hospedeiro-Patógeno
Metabolômica/métodos
Óxido Nítrico/metabolismo
Doenças das Plantas
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Proteome); 0 (Reactive Oxygen Species); 31C4KY9ESH (Nitric Oxide); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161014
[St] Status:MEDLINE


  9 / 684 MEDLINE  
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[PMID]:27697786
[Au] Autor:Rinne PL; Paul LK; Vahala J; Kangasjärvi J; van der Schoot C
[Ad] Endereço:Department of Plant Sciences, Norwegian University of Life Sciences, N-1432 Ås, Norway.
[Ti] Título:Axillary buds are dwarfed shoots that tightly regulate GA pathway and GA-inducible 1,3-ß-glucanase genes during branching in hybrid aspen.
[So] Source:J Exp Bot;67(21):5975-5991, 2016 Nov.
[Is] ISSN:1460-2431
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Axillary buds (AXBs) of hybrid aspen (Populus tremula×P. tremuloides) contain a developing dwarfed shoot that becomes para-dormant at the bud maturation point. Para-dormant AXBs can grow out after stem decapitation, while dormant AXBs pre-require long-term chilling to release them from dormancy. The latter is mediated by gibberellin (GA)-regulated 1,3-ß-glucanases, but it is unknown if GA is also important in the development, activation, and outgrowth of para-dormant AXBs. The present data show that para-dormant AXBs up-regulate GA receptor genes during their maturation, but curtail GA biosynthesis by down-regulating the rate-limiting GIBBERELLIN 3-OXIDASE2 (GA3ox2), which is characteristically expressed in the growing apex. However, decapitation significantly up-regulated GA3ox2 and GA -responsive 1,3-ß-glucanases (GH17-family; α-clade). In contrast, decapitation down-regulated γ-clade 1,3-ß-glucanases, which were strongly up-regulated in maturing AXBs concomitant with lipid body accumulation. Overexpression of selected GH17 members in hybrid aspen resulted in characteristic branching patterns. The α-clade member induced an acropetal branching pattern, whereas the γ-clade member activated AXBs in recurrent flushes during transient cessation of apex proliferation. The results support a model in which curtailing the final step in GA biosynthesis dwarfs the embryonic shoot, while high levels of GA precursors and GA receptors keep AXBs poised for growth. GA signaling, induced by decapitation, reinvigorates symplasmic supply routes through GA-inducible 1,3-ß-glucanases that hydrolyze callose at sieve plates and plasmodesmata.
[Mh] Termos MeSH primário: Giberelinas/fisiologia
Glucana 1,3-beta-Glucosidase/metabolismo
Brotos de Planta/metabolismo
Populus/metabolismo
[Mh] Termos MeSH secundário: Indução Enzimática/fisiologia
Giberelinas/metabolismo
Glucana 1,3-beta-Glucosidase/biossíntese
Glucana 1,3-beta-Glucosidase/genética
Redes e Vias Metabólicas/fisiologia
Dormência de Plantas/fisiologia
Brotos de Planta/enzimologia
Brotos de Planta/crescimento & desenvolvimento
Populus/enzimologia
Populus/crescimento & desenvolvimento
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gibberellins); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161005
[St] Status:MEDLINE


  10 / 684 MEDLINE  
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[PMID]:27626400
[Au] Autor:Jhan MH; Yeh CH; Tsai CC; Kao CT; Chang CK; Hsieh CW
[Ad] Endereço:Department of Medicinal Botanicals and Health Applications, Da-Yeh University, No.168, Xuefu Rd., Dacun Township, Chang-Hua 51591, Taiwan. mickey810514@gmail.com.
[Ti] Título:Enhancing the Antioxidant Ability of Trametes versicolor Polysaccharopeptides by an Enzymatic Hydrolysis Process.
[So] Source:Molecules;21(9), 2016 Sep 10.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Polysaccharopeptides (PSPs) are among the main bioactive constituents of Trametes versicolor (T. versicolor). The purpose of this research was to investigate the antioxidant activities of enzymatic hydrolysates obtained from T. versicolor polysaccharopeptides by 80 U/mL ß-1,3-glucanase (PSPs-EH80). The half-inhibitory concentration (IC50) of PSPs-EH80 in metal chelating assay, ABTS and DPPH radical scavenging test results were 0.83 mg/mL, 0.14 mg/mL and 0.52 mg/mL, respectively, which were lower than that of PSPs-EH 20 U/mL. The molecular weights of the PSPs-EH80 hydrolysates were 300, 190, 140 and 50 kDa, respectively, and the hydrolysis of polysaccharides by ß-1,3-glucanase did not change the original functional group. PSPs-EH80 reduced the reactive oxygen species (ROS) content at least twice that of treatment without PSPs-EH80. In addition, an oxidative damage test showed that PSPs-EH80 can improve HaCaT cell survival. According to our results, PSP demonstrates the potential of anti-oxidative damage; besides, enzyme hydrolysis can improve the ability of the PSP.
[Mh] Termos MeSH primário: Antioxidantes
Glucana 1,3-beta-Glucosidase/química
Proteoglicanas
Espécies Reativas de Oxigênio/metabolismo
Trametes/química
[Mh] Termos MeSH secundário: Antioxidantes/química
Antioxidantes/farmacologia
Linhagem Celular
Seres Humanos
Hidrólise
Proteoglicanas/química
Proteoglicanas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Proteoglycans); 0 (Reactive Oxygen Species); 0 (polysaccharide peptide); EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160915
[St] Status:MEDLINE



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