Base de dados : MEDLINE
Pesquisa : D08.811.277.450 [Categoria DeCS]
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  1 / 14571 MEDLINE  
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[PMID]:29324789
[Au] Autor:Choi JH; Shin KC; Oh DK
[Ad] Endereço:Department of Bioscience and Biotechnology, Konkuk University, Seoul, Republic of Korea.
[Ti] Título:An L213A variant of ß-glycosidase from Sulfolobus solfataricus with increased α-L-arabinofuranosidase activity converts ginsenoside Rc to compound K.
[So] Source:PLoS One;13(1):e0191018, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Compound K (C-K) is a crucial pharmaceutical and cosmetic component because of disease prevention and skin anti-aging effects. For industrial application of this active compound, the protopanaxadiol (PPD)-type ginsenosides should be transformed to C-K. ß-Glycosidase from Sulfolobus solfataricus has been reported as an efficient C-K-producing enzyme, using glycosylated PPD-type ginsenosides as substrates. ß-Glycosidase from S. solfataricus can hydrolyze ß-d-glucopyranoside in ginsenosides Rc, C-Mc1, and C-Mc, but not α-l-arabinofuranoside in these ginsenosides. To determine candidate residues involved in α-l-arabinofuranosidase activity, compound Mc (C-Mc) was docking to ß-glycosidase from S. solfataricus in homology model and sequence was aligned with ß-glycosidase from Pyrococcus furiosus that has α-l-arabinofuranosidase activity. A L213A variant ß-glycosidase with increased α-l-arabinofuranosidase activity was selected by substitution of other amino acids for candidate residues. The increased α-l-arabinofuranosidase activity of the L213A variant was confirmed through the determination of substrate specificity, change in binding energy, transformation pathway, and C-K production from ginsenosides Rc and C-Mc. The L213A variant ß-glycosidase catalyzed the conversion of Rc to Rd by hydrolyzing α-l-arabinofuranoside linked to Rc, whereas the wild-type ß-glycosidase did not. The variant enzyme converted ginsenosides Rc and C-Mc into C-K with molar conversions of 97%, which were 1.5- and 2-fold higher, respectively, than those of the wild-type enzyme. Therefore, protein engineering is a useful tool for enhancing the hydrolytic activity on specific glycoside linked to ginsenosides.
[Mh] Termos MeSH primário: Ginsenosídeos/metabolismo
Glicosídeo Hidrolases/metabolismo
Sulfolobus solfataricus/enzimologia
beta-Glucosidase/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Genes Bacterianos
Mutagênese Sítio-Dirigida
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
beta-Glucosidase/química
beta-Glucosidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ginsenosides); 0 (ginsenoside M1); 0K83B0L786 (ginsenoside Rc); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.21 (beta-Glucosidase); EC 3.2.1.55 (alpha-N-arabinofuranosidase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191018


  2 / 14571 MEDLINE  
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[PMID]:29334729
[Au] Autor:Huang R; Jiang BG; Li XN; Wang YT; Liu SS; Zheng KX; He J; Wu SH
[Ad] Endereço:School of Chemical Science and Technology, Yunnan University , Kunming 650091, China.
[Ti] Título:Polyoxygenated Cyclohexenoids with Promising α-Glycosidase Inhibitory Activity Produced by Phomopsis sp. YE3250, an Endophytic Fungus Derived from Paeonia delavayi.
[So] Source:J Agric Food Chem;66(5):1140-1146, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Seven new polyoxygenated cyclohexenoids, namely, phomopoxides A-G (1-7), were isolated from the fermentation broth extract of an endophytic fungal strain Phomopsis sp. YE3250 from the medicinal plant Paeonia delavayi Franch. The structures of these compounds were established by spectroscopic interpretation. The absolute configurations of compounds 1 and 4 were confirmed by X-ray crystallographic analysis and chemical derivative approach. All isolated compounds showed weak cytotoxic activities toward three human tumor cell lines (Hela, MCF-7, and NCI-H460) and weak antifungal activities against five pathogenic fungi (Candida albicans, Aspergillus niger, Pyricularia oryzae, Fusarium avenaceum, and Hormodendrum compactum). In addition, compounds 1-7 showed a promising α-glycosidase inhibitory activity with IC values of 1.47, 1.55, 1.83, 2.76, 2.88, 3.16, and 2.94 mM, respectively, as compared with a positive control of acarbose (IC = 1.22 mM).
[Mh] Termos MeSH primário: Ascomicetos/metabolismo
Cicloexanos/farmacologia
Inibidores Enzimáticos
Glicosídeo Hidrolases/antagonistas & inibidores
Paeonia/microbiologia
[Mh] Termos MeSH secundário: Antifúngicos
Antineoplásicos
Linhagem Celular Tumoral
Cicloexanos/química
Endófitos/metabolismo
Células HeLa
Seres Humanos
Células MCF-7
Oxigênio/química
Plantas Medicinais/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Antineoplastic Agents); 0 (Cyclohexanes); 0 (Enzyme Inhibitors); EC 3.2.1.- (Glycoside Hydrolases); S88TT14065 (Oxygen)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04998


  3 / 14571 MEDLINE  
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[PMID]:29334221
[Au] Autor:Liu L; Gong W; Sun X; Chen G; Wang L
[Ad] Endereço:State Key Laboratory of Microbial Technology, Shandong University , 27 Shandanan Road, Jinan 250100, China.
[Ti] Título:Extracellular Enzyme Composition and Functional Characteristics of Aspergillus niger An-76 Induced by Food Processing Byproducts and Based on Integrated Functional Omics.
[So] Source:J Agric Food Chem;66(5):1285-1295, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Byproducts of food processing can be utilized for the production of high-value-added enzyme cocktails. In this study, we utilized integrated functional omics technology to analyze composition and functional characteristics of extracellular enzymes produced by Aspergillus niger grown on food processing byproducts. The results showed that oligosaccharides constituted by arabinose, xylose, and glucose in wheat bran were able to efficiently induce the production of extracellular enzymes of A. niger. Compared with other substrates, wheat bran was more effective at inducing the secretion of ß-glucosidases from GH1 and GH3 families, as well as >50% of proteases from A1-family aspartic proteases. Compared with proteins induced by single wheat bran or soybean dregs, the protein yield induced by their mixture was doubled, and the time required to reach peak enzyme activity was shortened by 25%. This study provided a technical platform for the complex formulation of various substrates and functional analysis of extracellular enzymes.
[Mh] Termos MeSH primário: Aspergillus niger/enzimologia
Aspergillus niger/crescimento & desenvolvimento
Indução Enzimática/efeitos dos fármacos
Manipulação de Alimentos
Oligossacarídeos/farmacologia
Resíduos
[Mh] Termos MeSH secundário: Arabinose/farmacologia
Ácido Aspártico Proteases/biossíntese
Celulases/biossíntese
Fibras na Dieta/análise
Grãos Comestíveis/química
Fermentação
Glucose/farmacologia
Glicosídeo Hidrolases/biossíntese
Peptídeo Hidrolases/biossíntese
Xilose/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dietary Fiber); 0 (Oligosaccharides); 0 (Waste Products); A1TA934AKO (Xylose); B40ROO395Z (Arabinose); EC 3.2.1.- (Cellulases); EC 3.2.1.- (Glycoside Hydrolases); EC 3.4.- (Aspartic Acid Proteases); EC 3.4.- (Peptide Hydrolases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180116
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05164


  4 / 14571 MEDLINE  
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[PMID]:29346402
[Au] Autor:Schabort DTWP; Kilian SG; du Preez JC
[Ad] Endereço:Department of Microbial, Biochemical and Food Biotechnology, University of the Free State, Bloemfontein, South Africa.
[Ti] Título:Gene regulation in Kluyveromyces marxianus in the context of chromosomes.
[So] Source:PLoS One;13(1):e0190913, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotes, including the unicellular eukaryotes such as yeasts, employ multiple levels of gene regulation. Regulation of chromatin structure through chromatin compaction cascades, and influenced by transcriptional insulators, might play a role in the coordinated regulation of genes situated at adjacent loci and expressed as a co-regulated cluster. Subtelomeric gene silencing, which has previously been described in the yeast Saccharomyces cerevisiae, is an example of this phenomenon. Transcription from a common regulatory element located around a shared intergenic region is another factor that could coordinate the transcription of genes at adjacent loci. Additionally, the presence of DNA binding sites for the same transcription factor may coordinate expression of multiple genes. Yeasts such as the industrially important Kluyveromyces marxianus may also display these modes of regulation, but this has not been explored to date. An exploration was done using a complete genome and RNA-seq data from a previous study of the transcriptional response to glucose or xylose as the carbon source in a defined culture medium, and investigating whether the species displays clusters of co-localised differentially expressed genes. Regions of possible subtelomeric silencing were evident, but were non-responsive to the carbon sources tested here. Additionally, glucose or xylose responsive clusters were discovered far from telomeres which contained some of the most significantly differentially expressed genes, encoding enzymes involved in the utilisation of alternative carbon sources such as the industrially important inulinase gene INU1. These clusters contained putative binding sites for the carbon source responsive transcription factors Mig1 and Adr1. Additionally, we investigated the potential contribution of common intergenic regions in co-regulation. Some observations were also made in terms of the evolutionary conservation of these clusters among yeast species and the presence of potential transcriptional insulators at the periphery of these clusters.
[Mh] Termos MeSH primário: Cromossomos Bacterianos
Regulação Bacteriana da Expressão Gênica
Kluyveromyces/genética
[Mh] Termos MeSH secundário: Evolução Molecular
Genes Bacterianos
Glicosídeo Hidrolases/genética
Família Multigênica
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.7 (inulinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190913


  5 / 14571 MEDLINE  
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[PMID]:28461332
[Au] Autor:Temple MJ; Cuskin F; Baslé A; Hickey N; Speciale G; Williams SJ; Gilbert HJ; Lowe EC
[Ad] Endereço:From the Institute of Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE4 2HH, United Kingdom and.
[Ti] Título:A Bacteroidetes locus dedicated to fungal 1,6-ß-glucan degradation: Unique substrate conformation drives specificity of the key endo-1,6-ß-glucanase.
[So] Source:J Biol Chem;292(25):10639-10650, 2017 06 23.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycans are major nutrients available to the human gut microbiota. The are generalist glycan degraders, and this function is mediated largely by polysaccharide utilization loci (PULs). The genomes of several species contain a PUL, PUL , that was predicted to target mixed linked plant 1,3;1,4-ß-glucans. To test this hypothesis we characterized the proteins encoded by this locus in , a member of the human gut microbiota. We show here that PUL does not orchestrate the degradation of a plant polysaccharide but targets a fungal cell wall glycan, 1,6-ß-glucan, which is a growth substrate for the bacterium. The locus is up-regulated by 1,6-ß-glucan and encodes two enzymes, a surface endo-1,6-ß-glucanase, BT3312, and a periplasmic ß-glucosidase that targets primarily 1,6-ß-glucans. The non-catalytic proteins encoded by PUL target 1,6-ß-glucans and comprise a surface glycan-binding protein and a SusD homologue that delivers glycans to the outer membrane transporter. We identified the central role of the endo-1,6-ß-glucanase in 1,6-ß-glucan depolymerization by deleting , which prevented the growth of on 1,6-ß-glucan. The crystal structure of BT3312 in complex with ß-glucosyl-1,6-deoxynojirimycin revealed a TIM barrel catalytic domain that contains a deep substrate-binding cleft tailored to accommodate the hook-like structure adopted by 1,6-ß-glucan. Specificity is driven by the complementarity of the enzyme active site cleft and the conformation of the substrate. We also noted that PUL is syntenic to many PULs from other Bacteroidetes, suggesting that utilization of yeast and fungal cell wall 1,6-ß-glucans is a widespread adaptation within the human microbiota.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Bacteroidetes/enzimologia
Polissacarídeos Fúngicos/química
Glicosídeo Hidrolases/química
beta-Glucanas/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Bacteroidetes/genética
Configuração de Carboidratos
Cristalografia por Raios X
Loci Gênicos
Glicosídeo Hidrolases/genética
Seres Humanos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Fungal Polysaccharides); 0 (beta-Glucans); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.75 (endo-1,6-beta-glucanase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.787606


  6 / 14571 MEDLINE  
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[PMID]:28946280
[Au] Autor:Xu XQ; Su BM; Xie JS; Li RK; Yang J; Lin J; Ye XY
[Ad] Endereço:Fujian Key Laboratory of Marine Enzyme Engineering, College of Biological Sciences and Technology, Fuzhou University, Fuzhou, Fujian 350116, China.
[Ti] Título:Preparation of bioactive neoagaroligosaccharides through hydrolysis of Gracilaria lemaneiformis agar: A comparative study.
[So] Source:Food Chem;240:330-337, 2018 Feb 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Hydrolysis of Gracilaria lemaneiformis agar by ß-agarase was compared with HCl hydrolysis. The results showed that optimum catalysis conditions for the ß-agarase were pH 7.0 at 45°C. Mass spectroscopy, thin-layer chromatography and GPC results showed that the polymerization degrees of the hydrolysis products by the ß-agarase were mainly four, six and eight (more specific than the hydrolysate by HCl). The enzymatic degradation products of agar were distinctly different from those of HCl hydrolysis in the ratios among galactose and 3,6-anhydro-galactose and sulfate group contents. The NMR spectrometry proved that the products of ß-agarase were neoagaroligosaccharides, which was not found in the agarolytic products by HCl. The neoagarotetraose inhibited tyrosinase activity competitively with the K value of 16.0mg/ml. Hydroxyl radical-scavenging ability of neoagaroligosaccharides was much greater than that of agar HCl hydrolysate. This work suggests that neoagaroligosaccharide products produced by our ß-agarase could be more effective in function than products from acid hydrolysis.
[Mh] Termos MeSH primário: Gracilaria
[Mh] Termos MeSH secundário: Ágar
Glicosídeo Hidrolases
Hidrólise
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
9002-18-0 (Agar); EC 3.2.1.- (Glycoside Hydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE


  7 / 14571 MEDLINE  
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[PMID]:28873570
[Au] Autor:Long J; Zhang B; Li X; Zhan X; Xu X; Xie Z; Jin Z
[Ad] Endereço:School of Food Science and Technology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China; The State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Ji
[Ti] Título:Effective production of resistant starch using pullulanase immobilized onto magnetic chitosan/Fe O nanoparticles.
[So] Source:Food Chem;239:276-286, 2018 Jan 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this study, pullulanase was firstly immobilized by covalent bonding onto chitosan/Fe O nanoparticles or encapsulation in sol-gel after bonding onto chitosan/Fe O nanoparticles, and then the immobilized pullulanase was used for the effective production of resistant starch (RS). The highest RS content (35.1%) was obtained under the optimized condition of pH 4.4, enzyme concentration of 10ASPU/g and hydrolysis time of 12h when debranched by free pullulsanase, indicating that RS content was significantly (p<0.05) increased when compared to native starch (4.3%) and autoclaved starch (12.5%). Under these conditions, the immobilized pullulanase (10ASPU/g dry starch) yielded higher RS content compared to free enzyme (10ASPU/g dry starch), especially, the pullulanse immobilized by sol-gel encapsulation yielded the highest RS content (43.4%). Moreover, compared to starches hydrolyzed by free pullulanase, starches hydrolyzed by immobilized pullulanase showed a different saccharide profile of starch hydrolysate, including a stronger peak C (MW=5.0×10 ), as well as exhibited an additional absorption peak around 140°C. Reusability results demonstrated that pullulanase immobilized by sol-gel encapsulation had the advantages of producing higher RS content as well as better operational stability compared to pullulanase immobilized by cross-linking. The resulting enhanced RS content generated by the process described in this work could be used as an adjunct in food processing industries.
[Mh] Termos MeSH primário: Quitosana/metabolismo
[Mh] Termos MeSH secundário: Enzimas Imobilizadas
Compostos Férricos
Glicosídeo Hidrolases
Magnetismo
Nanopartículas Metálicas
Amido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Ferric Compounds); 1K09F3G675 (ferric oxide); 9005-25-8 (Starch); 9012-76-4 (Chitosan); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.41 (pullulanase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE


  8 / 14571 MEDLINE  
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[PMID]:28741461
[Au] Autor:Griffin LS; Gloster TM
[Ad] Endereço:Biomedical Sciences Research Complex, North Haugh, University of St. Andrews, St. Andrews, KY16 9ST. United Kingdom.
[Ti] Título:The Enzymatic Degradation of Heparan Sulfate.
[So] Source:Protein Pept Lett;24(8):710-722, 2017.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Glycosaminoglycans (GAGs) such as heparan sulfate (HS) interact with a number of factors in the extracellular matrix (ECM) and as a consequence play a key role in the metabolic processes occurring within the cell. The dynamic synthesis and degradation of HS (and all GAGs) are necessary for ensuring that optimal chains are present for these functions. The degradation of HS begins at the cell surface and finishes in the lysosome, after which components can be recycled. Deficiencies or mutations in the lysosomal enzymes that process GAGs result in rare Mucopolysaccharidoses disorders (MPSs). There are few treatments available for these genetically inherited diseases and those that are available often do not treat the neurological symptoms of the disease. In this review, we discuss the enzymes involved in the degradation of HS and their related diseases, with emphasis on those located in the lysosome.
[Mh] Termos MeSH primário: Matriz Extracelular/enzimologia
Heparitina Sulfato/metabolismo
Lisossomos/enzimologia
Mucopolissacaridoses/enzimologia
[Mh] Termos MeSH secundário: Sequência de Carboidratos
Expressão Gênica
Glicosídeo Hidrolases/deficiência
Glicosídeo Hidrolases/genética
Seres Humanos
Lisossomos/patologia
Mucopolissacaridoses/genética
Mucopolissacaridoses/patologia
Sulfatases/deficiência
Sulfatases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
9050-30-0 (Heparitin Sulfate); EC 3.1.6.- (Sulfatases); EC 3.2.1.- (Glycoside Hydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.2174/0929866524666170724113452


  9 / 14571 MEDLINE  
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[PMID]:28934471
[Au] Autor:Kaufmann T; Grishkovskaya I; Polyansky AA; Kostrhon S; Kukolj E; Olek KM; Herbert S; Beltzung E; Mechtler K; Peterbauer T; Gotzmann J; Zhang L; Hartl M; Zagrovic B; Elsayad K; Djinovic-Carugo K; Slade D
[Ad] Endereço:Department of Biochemistry, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter (VBC), Dr. Bohr-Gasse 9, 1030 Vienna, Austria.
[Ti] Título:A novel non-canonical PIP-box mediates PARG interaction with PCNA.
[So] Source:Nucleic Acids Res;45(16):9741-9759, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Poly(ADP-ribose) glycohydrolase (PARG) regulates cellular poly(ADP-ribose) (PAR) levels by rapidly cleaving glycosidic bonds between ADP-ribose units. PARG interacts with proliferating cell nuclear antigen (PCNA) and is strongly recruited to DNA damage sites in a PAR- and PCNA-dependent fashion. Here we identified PARG acetylation site K409 that is essential for its interaction with PCNA, its localization within replication foci and its recruitment to DNA damage sites. We found K409 to be part of a non-canonical PIP-box within the PARG disordered regulatory region. The previously identified putative N-terminal PIP-box does not bind PCNA directly but contributes to PARG localization within replication foci. X-ray structure and MD simulations reveal that the PARG non-canonical PIP-box binds PCNA in a manner similar to other canonical PIP-boxes and may represent a new type of PIP-box. While the binding of previously described PIP-boxes is based on hydrophobic interactions, PARG PIP-box binds PCNA via both stabilizing hydrophobic and fine-tuning electrostatic interactions. Our data explain the mechanism of PARG-PCNA interaction through a new PARG PIP-box that exhibits non-canonical sequence properties but a canonical mode of PCNA binding.
[Mh] Termos MeSH primário: Glicosídeo Hidrolases/metabolismo
Antígeno Nuclear de Célula em Proliferação/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Calorimetria/métodos
Cromatina/metabolismo
Cristalografia por Raios X
Dano ao DNA
Transferência Ressonante de Energia de Fluorescência
Glicosídeo Hidrolases/química
Glicosídeo Hidrolases/genética
Células HeLa
Seres Humanos
Imunoprecipitação
Lasers
Lisina/genética
Lisina/metabolismo
Simulação de Dinâmica Molecular
Antígeno Nuclear de Célula em Proliferação/química
Conformação Proteica
Fase S/genética
Eletricidade Estática
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Proliferating Cell Nuclear Antigen); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.143 (poly ADP-ribose glycohydrolase); K3Z4F929H6 (Lysine)
[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:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx604


  10 / 14571 MEDLINE  
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[PMID]:28886130
[Au] Autor:Ramos-Morales E; de la Fuente G; Nash RJ; Braganca R; Duval S; Bouillon ME; Lahmann M; Newbold CJ
[Ad] Endereço:Institute of Biological, Environmental and Rural Sciences, Aberystwyth University, Aberystwyth, United Kingdom.
[Ti] Título:Improving the antiprotozoal effect of saponins in the rumen by combination with glycosidase inhibiting iminosugars or by modification of their chemical structure.
[So] Source:PLoS One;12(9):e0184517, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The antiprotozoal effect of saponins is transitory, as when saponins are deglycosylated to sapogenins by rumen microorganisms they become inactive. We hypothesised that the combination of saponins with glycosidase-inhibiting iminosugars might potentially increase the effectiveness of saponins over time by preventing their deglycosylation in the rumen. Alternatively, modifying the structure of the saponins by substituting the sugar moiety with other small polar residues might maintain their activity as the sugar substitute would not be enzymatically cleaved. The aim of this in vitro study was to evaluate the acute antiprotozoal effect and the stability of this effect over a 24 h incubation period using ivy saponins, a stevia extract rich in iminosugars, ivy saponins with stevia extract, and a chemically modified ivy saponin, hederagenin bis-succinate (HBS). The effects on fermentation parameters and rumen bacterial communities were also studied. Ivy saponins with stevia and HBS had a greater antiprotozoal effect than ivy saponins, and this effect was maintained after 24 h of incubation (P<0.001). The combination of ivy and stevia extracts was more effective in shifting the fermentation pattern towards higher propionate (+39%) and lower butyrate (-32%) and lower ammonia concentration (-64%) than the extracts incubated separately. HBS caused a decrease in butyrate (-45%) and an increase in propionate (+43%) molar proportions. However, the decrease in ammonia concentration (-42%) observed in the presence of HBS was less than that caused by ivy saponins, either alone or with stevia. Whereas HBS and stevia impacted on bacterial population in terms of community structure, only HBS had an effect in terms of biodiversity (P<0.05). It was concluded that ivy saponins with stevia and the modified saponin HBS had a strong antiprotozoal effect, although they differed in their effects on fermentation parameters and bacteria communities. Ivy saponins combined with an iminosugar-rich stevia extract and/or HBS should be evaluated to determine their antiprotozoal effect in vivo.
[Mh] Termos MeSH primário: Antiprotozoários/farmacologia
Glicosídeo Hidrolases/antagonistas & inibidores
Extratos Vegetais/farmacologia
Rúmen/efeitos dos fármacos
Rúmen/parasitologia
Saponinas/farmacologia
[Mh] Termos MeSH secundário: Animais
Bactérias/efeitos dos fármacos
Estabilidade de Medicamentos
Fermentação/efeitos dos fármacos
Microbiota/efeitos dos fármacos
Extratos Vegetais/química
Rúmen/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiprotozoal Agents); 0 (Plant Extracts); 0 (Saponins); EC 3.2.1.- (Glycoside Hydrolases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184517



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