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Pesquisa : D08.811.913.555.500.350.700 [Categoria DeCS]
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[PMID]:28661661
[Au] Autor:Woodcock CB; Yakubov AB; Reich NO
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California , Santa Barbara, California 93106, United States.
[Ti] Título:Caulobacter crescentus Cell Cycle-Regulated DNA Methyltransferase Uses a Novel Mechanism for Substrate Recognition.
[So] Source:Biochemistry;56(30):3913-3922, 2017 Aug 01.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Caulobacter crescentus relies on DNA methylation by the cell cycle-regulated methyltransferase (CcrM) in addition to key transcription factors to control the cell cycle and direct cellular differentiation. CcrM is shown here to efficiently methylate its cognate recognition site 5'-GANTC-3' in single-stranded and hemimethylated double-stranded DNA. We report the K , k , k , and K for single-stranded and hemimethylated substrates, revealing discrimination of 10 -fold for noncognate sequences. The enzyme also shows a similar discrimination against single-stranded RNA. Two independent assays clearly show that CcrM is highly processive with single-stranded and hemimethylated DNA. Collectively, the data provide evidence that CcrM and other DNA-modifying enzymes may use a new mechanism to recognize DNA in a key epigenetic process.
[Mh] Termos MeSH primário: Caulobacter crescentus/enzimologia
Metilação de DNA
DNA de Cadeia Simples/metabolismo
DNA/metabolismo
DNA Metiltransferases Sítio Específica (Adenina-Específica)/metabolismo
[Mh] Termos MeSH secundário: Caulobacter crescentus/citologia
Ciclo Celular
Coenzimas/metabolismo
DNA/química
DNA de Cadeia Simples/química
Ensaio de Desvio de Mobilidade Eletroforética
Fluoresceínas/análise
Corantes Fluorescentes/análise
Cinética
Motivos de Nucleotídeos
RNA/química
RNA/metabolismo
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/metabolismo
S-Adenosilmetionina/metabolismo
DNA Metiltransferases Sítio Específica (Adenina-Específica)/genética
Especificidade por Substrato
Termodinâmica
Trítio
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (DNA, Single-Stranded); 0 (Fluoresceins); 0 (Fluorescent Dyes); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 10028-17-8 (Tritium); 63231-63-0 (RNA); 7LP2MPO46S (S-Adenosylmethionine); 9007-49-2 (DNA); EC 2.1.1.- (DNA modification methylase CcrM); EC 2.1.1.- (DNA modification methylase HindII); EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific))
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00378


  2 / 1006 MEDLINE  
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[PMID]:28640505
[Au] Autor:de la Rosa R; Steinmaus C; Akers NK; Conde L; Ferreccio C; Kalman D; Zhang KR; Skibola CF; Smith AH; Zhang L; Smith MT
[Ad] Endereço:Superfund Research Program, Divisions of Environmental Health Sciences and Epidemiology, School of Public Health, University of California, Berkeley, California.
[Ti] Título:Associations between arsenic (+3 oxidation state) methyltransferase (AS3MT) and N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) polymorphisms, arsenic metabolism, and cancer risk in a chilean population.
[So] Source:Environ Mol Mutagen;58(6):411-422, 2017 Jul.
[Is] ISSN:1098-2280
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inter-individual differences in arsenic metabolism have been linked to arsenic-related disease risks. Arsenic (+3) methyltransferase (AS3MT) is the primary enzyme involved in arsenic metabolism, and we previously demonstrated in vitro that N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) also methylates the toxic inorganic arsenic (iAs) metabolite, monomethylarsonous acid (MMA), to the less toxic dimethylarsonic acid (DMA). Here, we evaluated whether AS3MT and N6AMT1 gene polymorphisms alter arsenic methylation and impact iAs-related cancer risks. We assessed AS3MT and N6AMT1 polymorphisms and urinary arsenic metabolites (%iAs, %MMA, %DMA) in 722 subjects from an arsenic-cancer case-control study in a uniquely exposed area in northern Chile. Polymorphisms were genotyped using a custom designed multiplex, ligation-dependent probe amplification (MLPA) assay for 6 AS3MT SNPs and 14 tag SNPs in the N6AMT1 gene. We found several AS3MT polymorphisms associated with both urinary arsenic metabolite profiles and cancer risk. For example, compared to wildtypes, individuals carrying minor alleles in AS3MT rs3740393 had lower %MMA (mean difference = -1.9%, 95% CI: -3.3, -0.4), higher %DMA (mean difference = 4.0%, 95% CI: 1.5, 6.5), and lower odds ratios for bladder (OR = 0.3; 95% CI: 0.1-0.6) and lung cancer (OR = 0.6; 95% CI: 0.2-1.1). Evidence of interaction was also observed for both lung and bladder cancer between these polymorphisms and elevated historical arsenic exposures. Clear associations were not seen for N6AMT1. These results are the first to demonstrate a direct association between AS3MT polymorphisms and arsenic-related internal cancer risk. This research could help identify subpopulations that are particularly vulnerable to arsenic-related disease. Environ. Mol. Mutagen. 58:411-422, 2017. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Arsênico/metabolismo
Predisposição Genética para Doença
Metiltransferases/genética
Neoplasias/enzimologia
Neoplasias/genética
Polimorfismo Genético
DNA Metiltransferases Sítio Específica (Adenina-Específica)/genética
[Mh] Termos MeSH secundário: Idoso
Arsênico/urina
Chile
Feminino
Frequência do Gene/genética
Seres Humanos
Desequilíbrio de Ligação/genética
Masculino
Meia-Idade
Neoplasias/urina
Oxirredução
Fatores de Risco
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.1.1.- (Methyltransferases); EC 2.1.1.137 (AS3MT protein, human); EC 2.1.1.72 (N6AMT1 protein, human); EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific)); N712M78A8G (Arsenic)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1002/em.22104


  3 / 1006 MEDLINE  
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[PMID]:28586322
[Au] Autor:Luo GZ; He C
[Ad] Endereço:Department of Chemistry and Institute for Biophysical Dynamics, University of Chicago, Chicago, Illinois, USA. Howard Hughes Medical Institute, University of Chicago, Chicago, Illinois, USA. Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
[Ti] Título:DNA N -methyladenine in metazoans: functional epigenetic mark or bystander?
[So] Source:Nat Struct Mol Biol;24(6):503-506, 2017 Jun 06.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The DNA-adenine modification N -methyladenine (6mA), initially thought to be mainly restricted to prokaryotes and certain unicellular eukaryotes, has recently been found in metazoans. Proposed functions vary from gene activation to transposon suppression. However, since most metazoan genomes possess 5-methylcytosine (5mC) as a dominant epigenetic mark, it raises the question of why 6mA is required. This Perspective summarizes the latest discoveries and suggests potential functional roles for 6mA in metazoan genomes.
[Mh] Termos MeSH primário: Adenina/análogos & derivados
DNA/metabolismo
Epigênese Genética
[Mh] Termos MeSH secundário: Adenina/metabolismo
Animais
Regulação da Expressão Gênica no Desenvolvimento
DNA Metiltransferases Sítio Específica (Adenina-Específica)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9007-49-2 (DNA); EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific)); JAC85A2161 (Adenine); W7IBY2BGAX (6-methyladenine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170607
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3412


  4 / 1006 MEDLINE  
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[PMID]:28421443
[Au] Autor:Pindyurin AV
[Ad] Endereço:Netherlands Cancer Institute, Amsterdam, 1066 CX, the Netherlands. a.pindyurin@mcb.nsc.ru.
[Ti] Título:Genomic mapping of chromatin proteins by using Dam modification of an FLP-dependent DamID approach.
[So] Source:Dokl Biochem Biophys;472(1):15-18, 2017 Jan.
[Is] ISSN:1608-3091
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:To identify interactions of chromatin proteins with the genome of the cell type of interest that is a part of heterologous tissues and organs of Drosophila, an FLP-dependent DamID approach was recently developed [4], which does not require sorting of cells or nuclei. Here, a modification of this approach, Dam , is described. The modified approach was validated by generating the binding pattern of the LAM protein, a component of the inner membrane of the nuclear envelope, with the genome of glial cells of the Drosophila larval central brains.
[Mh] Termos MeSH primário: Cromatina/genética
Mapeamento Cromossômico/métodos
Drosophila/genética
Proteínas de Escherichia coli/genética
DNA Metiltransferases Sítio Específica (Adenina-Específica)/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Drosophila/genética
Proteínas de Escherichia coli/metabolismo
Laminas/genética
Neuroglia/metabolismo
Neurônios/metabolismo
DNA Metiltransferases Sítio Específica (Adenina-Específica)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Drosophila Proteins); 0 (Escherichia coli Proteins); 0 (Lamin protein, Drosophila); 0 (Lamins); EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific)); EC 2.1.1.72 (dam protein, E coli)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1134/S1607672917010057


  5 / 1006 MEDLINE  
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[PMID]:28223461
[Au] Autor:Doberenz S; Eckweiler D; Reichert O; Jensen V; Bunk B; Spröer C; Kordes A; Frangipani E; Luong K; Korlach J; Heeb S; Overmann J; Kaever V; Häussler S
[Ad] Endereço:Institute for Molecular Bacteriology, Twincore GmbH, Center for Clinical and Experimental Infection Research, Hannover, Germany.
[Ti] Título:Identification of a PAO1 DNA Methyltransferase, Its Targets, and Physiological Roles.
[So] Source:MBio;8(1), 2017 Feb 21.
[Is] ISSN:2150-7511
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA methylation is widespread among prokaryotes, and most DNA methylation reactions are catalyzed by adenine DNA methyltransferases, which are part of restriction-modification (R-M) systems. R-M systems are known for their role in the defense against foreign DNA; however, DNA methyltransferases also play functional roles in gene regulation. In this study, we used single-molecule real-time (SMRT) sequencing to uncover the genome-wide DNA methylation pattern in the opportunistic pathogen PAO1. We identified a conserved sequence motif targeted by an adenine methyltransferase of a type I R-M system and quantified the presence of N -methyladenine using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Changes in the PAO1 methylation status were dependent on growth conditions and affected pathogenicity in a infection model. Furthermore, we found that methylated motifs in promoter regions led to shifts in sense and antisense gene expression, emphasizing the role of enzymatic DNA methylation as an epigenetic control of phenotypic traits in Since the DNA methylation enzymes are not encoded in the core genome, our findings illustrate how the acquisition of accessory genes can shape the global transcriptome and thus may facilitate adaptation to new and challenging habitats. With the introduction of advanced technologies, epigenetic regulation by DNA methyltransferases in bacteria has become a subject of intense studies. Here we identified an adenosine DNA methyltransferase in the opportunistic pathogen PAO1, which is responsible for DNA methylation of a conserved sequence motif. The methylation level of all target sequences throughout the PAO1 genome was approximated to be in the range of 65 to 85% and was dependent on growth conditions. Inactivation of the methyltransferase revealed an attenuated-virulence phenotype in the infection model. Furthermore, differential expression of more than 90 genes was detected, including the small regulatory RNA , which contributes to a global iron-sparing response via the repression of a set of gene targets. Our finding of a methylation-dependent repression of the antisense transcript of the small regulatory RNA significantly expands our understanding of the regulatory mechanisms underlying active DNA methylation in bacteria.
[Mh] Termos MeSH primário: Adenina/análogos & derivados
Metilação de DNA
Pseudomonas aeruginosa/enzimologia
Pseudomonas aeruginosa/metabolismo
DNA Metiltransferases Sítio Específica (Adenina-Específica)/metabolismo
[Mh] Termos MeSH secundário: Adenina/análise
Animais
Cromatografia Líquida
Modelos Animais de Doenças
Epigênese Genética
Regulação Bacteriana da Expressão Gênica
Lepidópteros/microbiologia
Espectrometria de Massas
Regiões Promotoras Genéticas
Infecções por Pseudomonas/microbiologia
Pseudomonas aeruginosa/crescimento & desenvolvimento
Análise de Sequência de DNA
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific)); JAC85A2161 (Adenine); W7IBY2BGAX (6-methyladenine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170626
[Lr] Data última revisão:
170626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE


  6 / 1006 MEDLINE  
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[PMID]:28189763
[Au] Autor:Ramialison M; Waardenberg AJ; Schonrock N; Doan T; de Jong D; Bouveret R; Harvey RP
[Ad] Endereço:Victor Chang Cardiac Research Institute, Darlinghurst, NSW 2010, Australia; Australian Regenerative Medicine Institute, Monash University, Clayton, VIC 3800, Australia; Systems Biology Institute, Australia.
[Ti] Título:Analysis of steric effects in DamID profiling of transcription factor target genes.
[So] Source:Genomics;109(2):75-82, 2017 Mar.
[Is] ISSN:1089-8646
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA adenine methyltransferase identification (DamID) is an enzymatic technology for detecting DNA regions targeted by chromatin-associated proteins. Proteins are fused to bacterial DNA adenine methyltransferase (Dam) and expressed in cultured cells or whole organisms. Here, we used DamID to detect DNA regions bound by the cardiac-restricted transcription factors (TFs) NKX2-5 and SRF, and ubiquitously-expressed co-factors ELK1 and ELK4. We compared targets bound by these TFs as N- and C-terminal fusions with Dam, for both wild type (WT) NKX2-5 and mutant proteins mimicking those found in congenital heart disease. Overall, DamID is highly robust: while the orientation of WT Dam fusions can affect the size of the target sets, their signatures remained largely reproducible. Furthermore, a severe NKX2-5 mutant lacking the homeodomain showed strong steric effects negatively impacting target discovery. The extent of steric effect is likely to be dependent on the protein in question and the orientation of Dam fusion.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Regulação da Expressão Gênica
Técnicas Genéticas
Cardiopatias Congênitas/metabolismo
DNA Metiltransferases Sítio Específica (Adenina-Específica)
[Mh] Termos MeSH secundário: Animais
DNA/metabolismo
Cardiopatias Congênitas/genética
Proteína Homeobox Nkx-2.5/metabolismo
Seres Humanos
Camundongos
Fator de Resposta Sérica/metabolismo
Proteínas Elk-1 do Domínio ets/metabolismo
Proteínas Elk-4 do Domínio ets/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Elk1 protein, mouse); 0 (Elk4 protein, mouse); 0 (Homeobox Protein Nkx-2.5); 0 (Nkx2-5 protein, mouse); 0 (Serum Response Factor); 0 (ets-Domain Protein Elk-1); 146481-62-1 (ets-Domain Protein Elk-4); 9007-49-2 (DNA); EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific))
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170213
[St] Status:MEDLINE


  7 / 1006 MEDLINE  
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[PMID]:27981573
[Au] Autor:Zhong WP; Wu H; Chen JY; Li XX; Lin HM; Zhang B; Zhang ZW; Ma DL; Sun S; Li HP; Mai LP; He GD; Wang XP; Lei HP; Zhou HK; Tang L; Liu SW; Zhong SL
[Ad] Endereço:Guangdong Provincial Key Laboratory of Coronary Heart Disease Prevention, Guangdong Cardiovascular Institute, Guangzhou, China.
[Ti] Título:Genomewide Association Study Identifies Novel Genetic Loci That Modify Antiplatelet Effects and Pharmacokinetics of Clopidogrel.
[So] Source:Clin Pharmacol Ther;101(6):791-802, 2017 Jun.
[Is] ISSN:1532-6535
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genetic variants in the pharmacokinetic (PK) mechanism are the main underlying factors affecting the antiplatelet response to clopidogrel. Using a genomewide association study (GWAS) to identify new genetic loci that modify antiplatelet effects in Chinese patients with coronary heart disease, we identified novel variants in two transporter genes (SLC14A2 rs12456693, ATP-binding cassette [ABC]A1 rs2487032) and in N6AMT1 (rs2254638) associated with P2Y12 reaction unit (PRU) and plasma active metabolite (H4) concentration. These new variants dramatically improved the predictability of PRU variability to 37.7%. The associations between these loci and PK parameters of clopidogrel and H4 were observed in additional patients, and its function on the activation of clopidogrel was validated in liver S9 fractions (P < 0.05). Rs2254638 was further identified to exert a marginal risk effect for major adverse cardiac events in an independent cohort. In conclusion, new genetic variants were systematically identified as risk factors for the reduced efficacy of clopidogrel treatment.
[Mh] Termos MeSH primário: Transportador 1 de Cassete de Ligação de ATP/genética
Doença das Coronárias/tratamento farmacológico
Loci Gênicos
Variantes Farmacogenômicos
Inibidores da Agregação de Plaquetas/farmacocinética
Polimorfismo de Nucleotídeo Único
Antagonistas do Receptor Purinérgico P2Y/farmacocinética
DNA Metiltransferases Sítio Específica (Adenina-Específica)/genética
Ticlopidina/análogos & derivados
[Mh] Termos MeSH secundário: Transportador 1 de Cassete de Ligação de ATP/metabolismo
Idoso
Biotransformação
China
Doença das Coronárias/diagnóstico
Doença das Coronárias/genética
Feminino
Estudo de Associação Genômica Ampla
Seres Humanos
Masculino
Microssomos Hepáticos/metabolismo
Meia-Idade
Modelos Biológicos
Dinâmica não Linear
Inibidores da Agregação de Plaquetas/administração & dosagem
Inibidores da Agregação de Plaquetas/efeitos adversos
Testes de Função Plaquetária
Antagonistas do Receptor Purinérgico P2Y/administração & dosagem
Antagonistas do Receptor Purinérgico P2Y/efeitos adversos
Receptores Purinérgicos P2Y12/sangue
Receptores Purinérgicos P2Y12/efeitos dos fármacos
Medição de Risco
Fatores de Risco
DNA Metiltransferases Sítio Específica (Adenina-Específica)/metabolismo
Ticlopidina/administração & dosagem
Ticlopidina/efeitos adversos
Ticlopidina/farmacocinética
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCA1 protein, human); 0 (ATP Binding Cassette Transporter 1); 0 (P2RY12 protein, human); 0 (Platelet Aggregation Inhibitors); 0 (Purinergic P2Y Receptor Antagonists); 0 (Receptors, Purinergic P2Y12); A74586SNO7 (clopidogrel); EC 2.1.1.72 (N6AMT1 protein, human); EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific)); OM90ZUW7M1 (Ticlopidine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE
[do] DOI:10.1002/cpt.589


  8 / 1006 MEDLINE  
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[PMID]:27611472
[Au] Autor:Zhang Y; Xue Q; Liu J; Wang H
[Ad] Endereço:Department of Chemistry, Liaocheng University, Liaocheng, Shandong 252059, China.
[Ti] Título:Magnetic bead-liposome hybrids enable sensitive and portable detection of DNA methyltransferase activity using personal glucose meter.
[So] Source:Biosens Bioelectron;87:537-544, 2017 Jan 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:DNA methyltransferase (MTase) plays a critical role in maintaining genome methylation patterns, which has a close relationship to cancer and bacterial diseases. This encouraged the need to develop highly sensitive, simple, and robust assays for DNA MTase detection and inhibitor screening. Herein, a simple, sensitive, and specific DNA MTase activity assay was developed based on magnetic beads-liposome hybrids combined with personal glucose meter (PGM) for quantitative detection of DNA MTase and inhibitor screening. First, a magnetic beads-liposome hybrid probe is designed by the hybridization of p DNA-functionalized magnetic bead with p DNA-functionalized glucoamylase-encapsulated liposome (GEL). It integrates target recognition, magnetic separation and signal amplification within one multifunctional design. Then, in the presence of Dam MTase, the hybrids probe was methylated, and cleaved by methylation-sensitive restriction endonuclease Dpn I, making liposome separated from magnetic bead by magnetic separation. Finally, the separated liposome was decomposed, liberating the encapsulated glucoamylase to catalyze the hydrolysis of the signal substrate amylose with multiple turnovers, producing a large amount of glucose for quantitative readout by the PGM. In the proposed assay, the magnetic beads-liposome hybrids offered excellent sensitivity due to primary amplification via releasing numerous glucoamylase from a liposome followed by a secondary enzymatic amplification. The use of portable quantitative device PGM bypasses the requirement of complicated instruments and sophisticated operations, making the method simple and feasible for on-site detection. Moreover, the proposed assay was successfully applied in complex biological matrix and screen suitable inhibitor drugs for DAM for disease(s) treatment. The results reveal that the approach provides a simple, sensitive, and robust platform for DNA MTases detection and screening potential drugs in medical research and early clinical diagnostics.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Automonitorização da Glicemia/métodos
Lipossomos/química
Imãs/química
DNA Metiltransferases Sítio Específica (Adenina-Específica)/sangue
DNA Metiltransferases Sítio Específica (Adenina-Específica)/metabolismo
[Mh] Termos MeSH secundário: Amilose/metabolismo
Avaliação Pré-Clínica de Medicamentos/métodos
Enzimas Imobilizadas/metabolismo
Glucana 1,4-alfa-Glucosidase/metabolismo
Glucose/análise
Glucose/metabolismo
Seres Humanos
DNA Metiltransferases Sítio Específica (Adenina-Específica)/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzymes, Immobilized); 0 (Liposomes); 9005-82-7 (Amylose); EC 2.1.1.72 (Dam methyltransferase); EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific)); EC 3.2.1.3 (Glucan 1,4-alpha-Glucosidase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160910
[St] Status:MEDLINE


  9 / 1006 MEDLINE  
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[PMID]:27399961
[Au] Autor:Park YS; Suh KT; Shin JK; Lee JS
[Ad] Endereço:a Department of Orthopaedic Surgery , Sehung Hospital , Busan , Republic of Korea.
[Ti] Título:Estrogen receptor gene polymorphism in patients with degenerative lumbar scoliosis.
[So] Source:Br J Neurosurg;31(1):63-66, 2017 Feb.
[Is] ISSN:1360-046X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To examine the association between development of degenerative lumbar scoliosis (DLS) and sex hormones. METHODS: We investigated the association between DLS and estrogen receptor alpha (ERα) gene polymorphisms in 184 patients with a diagnosis of DLS, by determining the presences of the Pvu II and Xba I polymorphisms, measuring bone mineral densities at the lumbar spine (LSBMD) and femoral neck (FNBMD), and by investigating biochemical markers of bone turnover and comparing these results with those of 220 healthy normal controls. RESULTS: Genotype frequencies in DLS patients and controls revealed a significant difference for the Pvu II polymorphism only (p = 0.0287). No significant difference was found between the DLS and control groups with respect to the Xba I polymorphism, bone mineral density (BMD), or biochemical markers. Furthermore, no significant association was observed between the Pvu II polymorphism and BMD, lumbar scoliosis, lateral listhesis, or biochemical markers in patients with DLS. CONCLUSION: These results suggest that the ERα Pvu II polymorphism influences the prevalence of DLS.
[Mh] Termos MeSH primário: Receptor alfa de Estrogênio/genética
Degeneração do Disco Intervertebral/genética
Polimorfismo Genético/genética
Escoliose/genética
[Mh] Termos MeSH secundário: Absorciometria de Fóton
Idoso
Biomarcadores
Densidade Óssea/genética
DNA-Citosina Metilases/genética
Feminino
Frequência do Gene
Genótipo
Seres Humanos
Degeneração do Disco Intervertebral/epidemiologia
Masculino
Meia-Idade
Polimorfismo de Nucleotídeo Único/genética
Prevalência
Escoliose/epidemiologia
DNA Metiltransferases Sítio Específica (Adenina-Específica)/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Estrogen Receptor alpha); 0 (estrogen receptor alpha, human); EC 2.1.1.- (DNA modification methylase PvuII); EC 2.1.1.- (DNA modification methylase XbaI); EC 2.1.1.- (DNA-Cytosine Methylases); EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific))
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160712
[St] Status:MEDLINE
[do] DOI:10.1080/02688697.2016.1206186


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[PMID]:27997543
[Au] Autor:Ardissone S; Redder P; Russo G; Frandi A; Fumeaux C; Patrignani A; Schlapbach R; Falquet L; Viollier PH
[Ad] Endereço:Department of Microbiology and Molecular Medicine, Institute of Genetics & Genomics in Geneva (iGE3), Faculty of Medicine, University of Geneva, Geneva, Switzerland.
[Ti] Título:Cell Cycle Constraints and Environmental Control of Local DNA Hypomethylation in α-Proteobacteria.
[So] Source:PLoS Genet;12(12):e1006499, 2016 Dec.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heritable DNA methylation imprints are ubiquitous and underlie genetic variability from bacteria to humans. In microbial genomes, DNA methylation has been implicated in gene transcription, DNA replication and repair, nucleoid segregation, transposition and virulence of pathogenic strains. Despite the importance of local (hypo)methylation at specific loci, how and when these patterns are established during the cell cycle remains poorly characterized. Taking advantage of the small genomes and the synchronizability of α-proteobacteria, we discovered that conserved determinants of the cell cycle transcriptional circuitry establish specific hypomethylation patterns in the cell cycle model system Caulobacter crescentus. We used genome-wide methyl-N6-adenine (m6A-) analyses by restriction-enzyme-cleavage sequencing (REC-Seq) and single-molecule real-time (SMRT) sequencing to show that MucR, a transcriptional regulator that represses virulence and cell cycle genes in S-phase but no longer in G1-phase, occludes 5'-GANTC-3' sequence motifs that are methylated by the DNA adenine methyltransferase CcrM. Constitutive expression of CcrM or heterologous methylases in at least two different α-proteobacteria homogenizes m6A patterns even when MucR is present and affects promoter activity. Environmental stress (phosphate limitation) can override and reconfigure local hypomethylation patterns imposed by the cell cycle circuitry that dictate when and where local hypomethylation is instated.
[Mh] Termos MeSH primário: Caulobacter crescentus/genética
Ciclo Celular/genética
Metilação de DNA/genética
Transcrição Genética
[Mh] Termos MeSH secundário: Divisão Celular/genética
Replicação do DNA/efeitos dos fármacos
Replicação do DNA/genética
Regulação Bacteriana da Expressão Gênica
Genoma Microbiano
Metiltransferases/genética
Fosfatos/metabolismo
Regiões Promotoras Genéticas
DNA Metiltransferases Sítio Específica (Adenina-Específica)/genética
Inanição/genética
Inanição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphates); EC 2.1.1.- (Methyltransferases); EC 2.1.1.72 (Site-Specific DNA-Methyltransferase (Adenine-Specific))
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006499



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