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Pesquisa : D08.811.277.450.420.200.600 [Categoria DeCS]
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  1 / 369 MEDLINE  
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[PMID]:28507000
[Au] Autor:Vaddepalli P; Fulton L; Wieland J; Wassmer K; Schaeffer M; Ranf S; Schneitz K
[Ad] Endereço:Entwicklungsbiologie der Pflanzen, Wissenschaftszentrum Weihenstephan, Technische Universität München, 85354 Freising, Germany.
[Ti] Título:The cell wall-localized atypical ß-1,3 glucanase ZERZAUST controls tissue morphogenesis in .
[So] Source:Development;144(12):2259-2269, 2017 06 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Orchestration of cellular behavior in plant organogenesis requires integration of intercellular communication and cell wall dynamics. The underlying signaling mechanisms are poorly understood. Tissue morphogenesis in depends on the receptor-like kinase STRUBBELIG. Mutations in were previously shown to result in a -like mutant phenotype. Here, we report on the molecular identification and functional characterization of We show that encodes a putative GPI-anchored ß-1,3 glucanase suggested to degrade the cell wall polymer callose. However, a combination of , cell biological and genetic experiments indicate that ZERZAUST is not involved in the regulation of callose accumulation. Nonetheless, Fourier-transformed infrared-spectroscopy revealed that mutants show defects in cell wall composition. Furthermore, the results indicate that ZERZAUST represents a mobile apoplastic protein, and that its carbohydrate-binding module family 43 domain is required for proper subcellular localization and function whereas its GPI anchor is dispensable. Our collective data reveal that the atypical ß-1,3 glucanase ZERZAUST acts in a non-cell-autonomous manner and is required for cell wall organization during tissue morphogenesis.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/crescimento & desenvolvimento
Arabidopsis/metabolismo
Glucana Endo-1,3-beta-D-Glucosidase/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Parede Celular/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Regulação da Expressão Gênica de Plantas
Genes de Plantas
Glucana Endo-1,3-beta-D-Glucosidase/genética
Morfogênese/genética
Morfogênese/fisiologia
Mutação
Plantas Geneticamente Modificadas
Receptores Proteína Tirosina Quinases/genética
Receptores Proteína Tirosina Quinases/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (QUIRKY protein, Arabidopsis); 0 (ZERZAUST protein, Arabidopsis); EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases); EC 2.7.10.1 (SUB protein, Arabidopsis); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170517
[St] Status:MEDLINE
[do] DOI:10.1242/dev.152231


  2 / 369 MEDLINE  
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[PMID]:28388361
[Au] Autor:Miki A; Inaba S; Maruno T; Kobayashi Y; Oda M
[Ad] Endereço:a Graduate School of Life and Environmental Sciences, Kyoto Prefectural University , Kyoto , Japan.
[Ti] Título:Tryptophan introduction can change ß-glucan binding ability of the carbohydrate-binding module of endo-1,3-ß-glucanase.
[So] Source:Biosci Biotechnol Biochem;81(5):951-957, 2017 May.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Endo-1,3-ß-glucanase from Cellulosimicrobium cellulans DK-1 has a carbohydrate-binding module (CBM-DK) at the C-terminal side of a catalytic domain. Out of the imperfect tandem α-, ß-, and γ-repeats in CBM-DK, the α-repeat primarily contributes to ß-glucan binding. This unique feature is derived from Trp273 in α-repeat, whose corresponding residues in ß- and γ-repeats are Asp314 and Gly358, respectively. In this study, we generated Trp-switched mutants, W273A/D314W, D270A/W273A/D314W, W273A/G358W, and D270A/W273A/G358W, and analyzed their binding abilities toward laminarioligosaccharides and laminarin. While the binding affinities of D270A/W273A and W273A mutants were either lost or much lower than that of the wild-type, those of Trp-switched mutants recovered, indicating that a Trp introduction in ß- or γ-repeat can substitute the α-repeat by primarily contributing to ß-glucan binding. Thus, we have successfully engineered a CBM-DK that binds to laminarin by a mechanism different from that of the wild-type, but with similar affinity.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Glucana Endo-1,3-beta-D-Glucosidase/química
Glucana Endo-1,3-beta-D-Glucosidase/metabolismo
Triptofano
beta-Glucanas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Glucana Endo-1,3-beta-D-Glucosidase/genética
Laminaria/enzimologia
Mutação
Ligação Proteica
Sequências Repetitivas de Ácido Nucleico
Wolfiporia/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta-Glucans); 8DUH1N11BX (Tryptophan); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase)
[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:170408
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1285687


  3 / 369 MEDLINE  
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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


  4 / 369 MEDLINE  
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[PMID]:28120311
[Au] Autor:Kusaykin MI; Belik AA; Kovalchuk SN; Dmitrenok PS; Rasskazov VA; Isakov VV; Zvyagintseva TN
[Ad] Endereço:G.B. Elyakov Pacific Institute of Bioorganic Chemistry FEB RAS, pr.100 let Vladivostoku 159, Vladivostok, Russia, 690022. mikvil@gmail.com.
[Ti] Título:A new recombinant endo-1,3-ß-D-glucanase from the marine bacterium Formosa algae KMM 3553: enzyme characteristics and transglycosylation products analysis.
[So] Source:World J Microbiol Biotechnol;33(2):40, 2017 Feb.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A specific endo-1,3-ß-D-glucanase (GFA) gene was found in genome of marine bacterium Formosa algae KMM 3553. For today this is the only characterized endo-1,3-ß-D-glucanase (EC 3.2.1.39) in Formosa genus and the only bacterial EC 3.2.1.39 GH16 endo-1,3-ß-D-glucanase with described transglycosylation activity. It was expressed in E. coli and isolated in homogeneous state. Investigating the products of polysaccharides digestion with GFA allowed to establish it's substrate specificity and classify this enzyme as glucan endo-1,3-ß-D-glucosidase (EC 3.2.1.39). The amino-acid sequence of GFA consists of 556 residues and shows sequence similarity of 45-85% to ß-1,3-glucanases of bacteria belonging to the CAZy 16th structural family of glycoside hydrolases GH16. Enzyme has molecular weight 61 kDa, exhibits maximum of catalytic activity at 45 °C, pH 5.5. Half-life period at 45 °Ð¡ is 20 min, complete inactivation happens at 55 °C within 10 min. K for hydrolysis of laminarin is 0.388 mM. GFA glucanase from marine bacteria F. algae is one of rare enzymes capable to catalyze reactions of transglycosylation. It catalyzed transfer of glyconic part of substrate molecule on methyl-ß-D-xylopyranoside, glycerol and methyl-α-D-glucopyranoside. The enzyme can be used in structure determination of ß-1,3-glucans (or mixed 1,3;1,4- and 1,3;1,6-ß-D-glucans) and enzymatic synthesis of new carbohydrate-containing compounds.
[Mh] Termos MeSH primário: Flavobacterium/enzimologia
Glucana Endo-1,3-beta-D-Glucosidase/genética
Glucana Endo-1,3-beta-D-Glucosidase/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Clonagem Molecular
Flavobacterium/genética
Glicosilação
Hidrólise
Peso Molecular
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170126
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-017-2213-x


  5 / 369 MEDLINE  
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[PMID]:28081530
[Au] Autor:Hirpara DG; Gajera HP; Hirpara HZ; Golakiya BA
[Ad] Endereço:Department of Biotechnology, College of Agriculture, Junagadh Agricultural University, Junagadh, India.
[Ti] Título:Antipathy of Trichoderma against Sclerotium rolfsii Sacc.: Evaluation of Cell Wall-Degrading Enzymatic Activities and Molecular Diversity Analysis of Antagonists.
[So] Source:J Mol Microbiol Biotechnol;27(1):22-28, 2017.
[Is] ISSN:1660-2412
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The fungus Trichoderma is a teleomorph of the Hypocrea genus and associated with biological control of plant diseases. The microscopic, biochemical, and molecular characterization of Trichoderma was carried out and evaluated for in vitro antagonistic activity against the fungal pathogen Sclerotium rolfsii causing stem rot disease in groundnut. In total, 11 isolates of Trichoderma were examined for antagonism at 6 and 12 days after inoculation (DAI). Out of 11, T. virens NBAII Tvs12 evidenced the highest (87.91%) growth inhibition of the test pathogen followed by T. koningii MTCC 796 (67.03%), T. viride NBAII Tv23 (63.74%), and T. harzianum NBAII Th1 (60.44%). Strong mycoparasitism was observed in the best antagonist Tvs12 strain during 6-12 DAI. The specific activity of cell wall-degrading enzymes - chitinase and ß-1,3-glucanase - was positively correlated with growth inhibition of the test pathogen. In total, 18 simple sequence repeat (SSR) polymorphisms were reported to amplify 202 alleles across 11 Trichoderma isolates. The average polymorphism information content for SSR markers was found to be 0.80. The best antagonist Tvs 12 was identified with 7 unique SSR alleles amplified by 5 SSR markers. Clustering patterns of 11 Trichoderma strains showed the best antagonist T. virens NBAII Tvs 12 outgrouped with a minimum 3% similarity from the rest of Trichoderma.
[Mh] Termos MeSH primário: Antibiose
Basidiomycota/crescimento & desenvolvimento
Parede Celular/metabolismo
Quitinases/metabolismo
Glucana Endo-1,3-beta-D-Glucosidase/metabolismo
Trichoderma/enzimologia
Trichoderma/fisiologia
[Mh] Termos MeSH secundário: Alelos
Arachis/microbiologia
Quitinases/genética
Glucana Endo-1,3-beta-D-Glucosidase/genética
Doenças das Plantas/microbiologia
Polimorfismo Genético
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.2.1.14 (Chitinases); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE
[do] DOI:10.1159/000452997


  6 / 369 MEDLINE  
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[PMID]:27811341
[Au] Autor:Bolouri Moghaddam MR; Vilcinskas A; Rahnamaeian M
[Ti] Título:The insect-derived antimicrobial peptide metchnikowin targets Fusarium graminearum ß(1,3)glucanosyltransferase Gel1, which is required for the maintenance of cell wall integrity.
[So] Source:Biol Chem;398(4):491-498, 2017 Apr 01.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Antimicrobial peptides (AMPs) are essential components of the insect innate immune system. Their diversity provides protection against a broad spectrum of microbes and they have several distinct modes of action. Insect-derived AMPs are currently being developed for both medical and agricultural applications, and their expression in transgenic crops confers resistance against numerous plant pathogens. The antifungal peptide metchnikowin (Mtk), which was originally discovered in the fruit fly Drosophila melanogaster, is of particular interest because it has potent activity against economically important phytopathogenic fungi of the phylum Ascomycota, such as Fusarium graminearum, but it does not harm beneficial fungi such as the mycorrhizal basidiomycete Piriformospora indica. To investigate the specificity of Mtk, we used the peptide to screen a F. graminearum yeast two-hybrid library. This revealed that Mtk interacts with the fungal enzyme ß(1,3)-glucanosyltransferase Gel1 (FgBGT), which is one of the enzymes responsible for fungal cell wall synthesis. The interaction was independently confirmed in a second interaction screen using mammalian cells. FgBGT is required for the viability of filamentous fungi by maintaining cell wall integrity. Our study therefore paves the way for further applications of Mtk in formulation of bio fungicides or as a supplement in food preservation.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/farmacologia
Parede Celular/efeitos dos fármacos
Proteínas de Drosophila/farmacologia
Fusarium/efeitos dos fármacos
Glucana Endo-1,3-beta-D-Glucosidase/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Anti-Infecciosos/farmacologia
Bioensaio
Linhagem Celular
Drosophila melanogaster/química
Fusarium/genética
Biblioteca Gênica
Modelos Biológicos
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Antimicrobial Cationic Peptides); 0 (Drosophila Proteins); 175280-86-1 (Metchnikowin protein, Drosophila); EC 3.2.1.- (1,3-beta-glucanosyltransferase); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE


  7 / 369 MEDLINE  
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[PMID]:27597232
[Au] Autor:Chen X; Zhang R; Takada A; Iwatani S; Oka C; Kitamoto T; Kajiwara S
[Ad] Endereço:School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
[Ti] Título:The role of Bgl2p in the transition to filamentous cells during biofilm formation by Candida albicans.
[So] Source:Mycoses;60(2):96-103, 2017 Feb.
[Is] ISSN:1439-0507
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The fungal pathogen Candida albicans undergoes a transition from yeast cells to filamentous cells that is related to its pathogenicity. The complex multicellular processes involved in biofilm formation by this fungus also include this transition. In this work, we investigated the morphological role of the Bgl2 protein (Bgl2p) in the transition to filamentous cells during biofilm formation by C. albicans. Bgl2p has been identified as a ß-1, 3-glucosyltransferase, and transcription of the CaBGL2 gene is upregulated during biofilm formation. We used scanning electron microscopy to observe the microstructure of a bgl2 null mutant during biofilm formation and found a delay in the transition to filamentous cells in the premature phase (24 hours) of biofilm formation. Deletion of the CaBGL2 gene led to a decrease in the expression of CPH2 and TEC1, which encode transcription factors required for the transition to the filamentous form. These findings indicate that Bgl2p plays a role in the transition to filamentous cells during biofilm formation by C. albicans.
[Mh] Termos MeSH primário: Biofilmes/crescimento & desenvolvimento
Candida albicans/genética
Candida albicans/fisiologia
Glucana Endo-1,3-beta-D-Glucosidase/genética
[Mh] Termos MeSH secundário: Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Candida albicans/enzimologia
Candida albicans/ultraestrutura
Candidíase
Proteínas de Ligação a DNA/genética
Proteínas Fúngicas/genética
Deleção de Genes
Glucana Endo-1,3-beta-D-Glucosidase/química
Glucana Endo-1,3-beta-D-Glucosidase/metabolismo
Hifas/genética
Hifas/ultraestrutura
Microscopia Eletrônica de Varredura
Mutação
Reação em Cadeia da Polimerase
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (CPH2 protein, Candida albicans); 0 (DNA-Binding Proteins); 0 (Fungal Proteins); 0 (TEC1 protein, Candida albicans); 0 (Transcription Factors); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170323
[Lr] Data última revisão:
170323
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160907
[St] Status:MEDLINE
[do] DOI:10.1111/myc.12554


  8 / 369 MEDLINE  
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[PMID]:27568483
[Au] Autor:Samalova M; Mélida H; Vilaplana F; Bulone V; Soanes DM; Talbot NJ; Gurr SJ
[Ad] Endereço:Department of Plant Sciences, University of Oxford, Oxford, UK.
[Ti] Título:The ß-1,3-glucanosyltransferases (Gels) affect the structure of the rice blast fungal cell wall during appressorium-mediated plant infection.
[So] Source:Cell Microbiol;19(3), 2017 Mar.
[Is] ISSN:1462-5822
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The fungal wall is pivotal for cell shape and function, and in interfacial protection during host infection and environmental challenge. Here, we provide the first description of the carbohydrate composition and structure of the cell wall of the rice blast fungus Magnaporthe oryzae. We focus on the family of glucan elongation proteins (Gels) and characterize five putative ß-1,3-glucan glucanosyltransferases that each carry the Glycoside Hydrolase 72 signature. We generated targeted deletion mutants of all Gel isoforms, that is, the GH72 , which carry a putative carbohydrate-binding module, and the GH72 Gels, without this motif. We reveal that M. oryzae GH72 GELs are expressed in spores and during both infective and vegetative growth, but each individual Gel enzymes are dispensable for pathogenicity. Further, we demonstrated that a Δgel1Δgel3Δgel4 null mutant has a modified cell wall in which 1,3-glucans have a higher degree of polymerization and are less branched than the wild-type strain. The mutant showed significant differences in global patterns of gene expression, a hyper-branching phenotype and no sporulation, and thus was unable to cause rice blast lesions (except via wounded tissues). We conclude that Gel proteins play significant roles in structural modification of the fungal cell wall during appressorium-mediated plant infection.
[Mh] Termos MeSH primário: Parede Celular/química
Glucana Endo-1,3-beta-D-Glucosidase/metabolismo
Magnaporthe/enzimologia
Magnaporthe/metabolismo
beta-Glucanas/análise
[Mh] Termos MeSH secundário: Deleção de Genes
Glucana Endo-1,3-beta-D-Glucosidase/genética
Magnaporthe/genética
Magnaporthe/patogenicidade
Oryza/microbiologia
Doenças das Plantas/microbiologia
Esporos Fúngicos/enzimologia
Esporos Fúngicos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta-1,3-D-glucan); 0 (beta-Glucans); EC 3.2.1.- (1,3-beta-glucanosyltransferase); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160830
[St] Status:MEDLINE
[do] DOI:10.1111/cmi.12659


  9 / 369 MEDLINE  
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[PMID]:27559035
[Au] Autor:Zavaliev R; Dong X; Epel BL
[Ad] Endereço:Department of Molecular Biology and Ecology of Plants, Tel Aviv University, Tel Aviv 69978, Israel (R.Z., B.L.E.); andDepartment of Biology, Duke University, Durham, North Carolina 27708 (R.Z., X.D.) raul.zavaliev@duke.edu.
[Ti] Título:Glycosylphosphatidylinositol (GPI) Modification Serves as a Primary Plasmodesmal Sorting Signal.
[So] Source:Plant Physiol;172(2):1061-1073, 2016 Oct.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plasmodesmata (Pd) are membranous channels that serve as a major conduit for cell-to-cell communication in plants. The Pd-associated ß-1,3-glucanase (BG_pap) and CALLOSE BINDING PROTEIN1 (PDCB1) were identified as key regulators of Pd conductivity. Both are predicted glycosylphosphatidylinositol-anchored proteins (GPI-APs) carrying a conserved GPI modification signal. However, the subcellular targeting mechanism of these proteins is unknown, particularly in the context of other GPI-APs not associated with Pd Here, we conducted a comparative analysis of the subcellular targeting of the two Pd-resident and two unrelated non-Pd GPI-APs in Arabidopsis (Arabidopsis thaliana). We show that GPI modification is necessary and sufficient for delivering both BG_pap and PDCB1 to Pd Moreover, the GPI modification signal from both Pd- and non-Pd GPI-APs is able to target a reporter protein to Pd, likely to plasma membrane microdomains enriched at Pd As such, the GPI modification serves as a primary Pd sorting signal in plant cells. Interestingly, the ectodomain, a region that carries the functional domain in GPI-APs, in Pd-resident proteins further enhances Pd accumulation. However, in non-Pd GPI-APs, the ectodomain overrides the Pd targeting function of the GPI signal and determines a specific GPI-dependent non-Pd localization of these proteins at the plasma membrane and cell wall. Domain-swap analysis showed that the non-Pd localization is also dominant over the Pd-enhancing function mediated by a Pd ectodomain. In conclusion, our results indicate that segregation between Pd- and non-Pd GPI-APs occurs prior to Pd targeting, providing, to our knowledge, the first evidence of the mechanism of GPI-AP sorting in plants.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/metabolismo
Glucana Endo-1,3-beta-D-Glucosidase/metabolismo
Glicosilfosfatidilinositóis/metabolismo
Glicoproteínas de Membrana/metabolismo
Plasmodesmos/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Membrana Celular/metabolismo
Parede Celular/metabolismo
Glucana Endo-1,3-beta-D-Glucosidase/genética
Immunoblotting
Proteínas Ligadas a Lipídeos/genética
Proteínas Ligadas a Lipídeos/metabolismo
Glicoproteínas de Membrana/genética
Microdomínios da Membrana/metabolismo
Microscopia Confocal
Modelos Biológicos
Plantas Geneticamente Modificadas
Plasmodesmos/genética
Transporte Proteico/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Glycosylphosphatidylinositols); 0 (Lipid-Linked Proteins); 0 (Membrane Glycoproteins); 0 (PDCB1 protein, Arabidopsis); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160826
[St] Status:MEDLINE


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[PMID]:27500912
[Au] Autor:Selivanova OM; Glyakina AV; Gorbunova EY; Mustaeva LG; Suvorina MY; Grigorashvili EI; Nikulin AD; Dovidchenko NV; Rekstina VV; Kalebina TS; Surin AK; Galzitskaya OV
[Ad] Endereço:Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russia.
[Ti] Título:Structural model of amyloid fibrils for amyloidogenic peptide from Bgl2p-glucantransferase of S. cerevisiae cell wall and its modifying analog. New morphology of amyloid fibrils.
[So] Source:Biochim Biophys Acta;1864(11):1489-99, 2016 11.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:We performed a comparative study of the process of amyloid formation by short homologous peptides with a substitution of aspartate for glutamate in position 2 - VDSWNVLVAG (AspNB) and VESWNVLVAG (GluNB) - with unblocked termini. Peptide AspNB (residues 166-175) corresponded to the predicted amyloidogenic region of the protein glucantransferase Bgl2 from the Saccharomyces cerevisiae cell wall. The process of amyloid formation was monitored by fluorescence spectroscopy (FS), electron microscopy (EM), tandem mass spectrometry (TMS), and X-ray diffraction (XD) methods. The experimental study at pH3.0 revealed formation of amyloid fibrils with similar morphology for both peptides. Moreover, we found that the morphology of fibrils made of untreated ammonia peptide is not mentioned in the literature. This morphology resembles snakes lying side by side in the form of a wave without intertwining. Irrespective of the way of the peptide preparation, the rate of fibril formation is higher for AspNB than for GluNB. However, preliminary treatment with ammonia highly affected fibril morphology especially for AspNB. Such treatment allowed us to obtain a lag period during the process of amyloid formation. It showed that the process was nucleation-dependent. With or without treatment, amyloid fibrils consisted of ring-like oligomers with the diameter of about 6nm packed either directly ring-to-ring or ring-on-ring with a slight shift. We also proposed the molecular structure of amyloid fibrils for two studied peptides.
[Mh] Termos MeSH primário: Amiloide/ultraestrutura
Proteínas Amiloidogênicas/ultraestrutura
Ácido Aspártico/química
Glucana Endo-1,3-beta-D-Glucosidase/química
Ácido Glutâmico/química
Proteínas de Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Substituição de Aminoácidos
Amônia/química
Amiloide/química
Proteínas Amiloidogênicas/química
Parede Celular/química
Cristalografia por Raios X
Concentração de Íons de Hidrogênio
Modelos Moleculares
Estrutura Molecular
Fragmentos de Peptídeos/química
Técnicas de Síntese em Fase Sólida
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amyloid); 0 (Amyloidogenic Proteins); 0 (Peptide Fragments); 0 (Saccharomyces cerevisiae Proteins); 30KYC7MIAI (Aspartic Acid); 3KX376GY7L (Glutamic Acid); 7664-41-7 (Ammonia); EC 3.2.1.39 (BGL2 protein, S cerevisiae); EC 3.2.1.39 (Glucan Endo-1,3-beta-D-Glucosidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160809
[St] Status:MEDLINE



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