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Pesquisa : B04.123.150.800.230 [Categoria DeCS]
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[PMID]:28456568
[Au] Autor:Yin J; Zhu F; Hao W; Xu Q; Chang J; Wang H; Guo B
[Ad] Endereço:Key Laboratory of Environmental Biotechnology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing 100085, China; University of Chinese Academy of Sciences, Beijing 100049, China.
[Ti] Título:Acylamino acid chiral fungicides on toxiciepigenetics in lambda DNA methylation.
[So] Source:Food Chem Toxicol;109(Pt 1):735-745, 2017 Nov.
[Is] ISSN:1873-6351
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Acylamino acid chiral fungicides (AACFs) are low-toxicity pesticides and considered as non-carcinogenic chemicals to laboratory animals. Though AACFs have potential toxicological effects on mammals by non-genotoxic mechanisms, the toxicoepigenomics of AACFs has not been documented. In this article, we explored toxiciepigenetics of metalaxyl, benalaxyl and furalaxyl through epigenetics research on lambda DNA under different concentration exposure. The toxicoepigenomic difference of stereoisomers was examined also. Our results showed that AACFs would affect methyltransferase activity resulting in modulating DNA methylation levels and pattern. The LOAEL of R-metalaxyl and S-metalaxyl were 30 mM and 0.3 mM, respectively. The LOAEL of (R, S)-benalaxyl and (R, S)-furalaxyl were 0.3 Mm and 30 mM, respectively. A significant dose-response effect between (R, S)-benalaxyl and global methylation level was observed. Global methylation level was more susceptible to S-enantiomer compared to R-enantiomer, which indicated enantiomers of AACFs have the enantioselectivity in toxiciepigenetics. Moreover, the dependence of the methylation inhibition on the chiral center of metalaxyl may suggest a considerable specificity of the compound of AACFs for DNA methyltransferases. The inhibition effect between R-enantiomer and S-enantiomer of AACFs on DNA methylation levels generated in this study is important for low-toxicity pesticides toxicoepigenomics evaluation.
[Mh] Termos MeSH primário: Bacteriófago lambda/efeitos dos fármacos
Fungicidas Industriais/toxicidade
[Mh] Termos MeSH secundário: Alanina/análogos & derivados
Alanina/toxicidade
Bacteriófago lambda/genética
Bacteriófago lambda/metabolismo
Metilação de DNA/efeitos dos fármacos
DNA Viral/genética
DNA Viral/metabolismo
Epigenômica
Furanos/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Fungicides, Industrial); 0 (Furans); 0 (furalaxyl); 16K4M187IF (metalaxyl); 18TH6NY90J (benalaxyl); OF5P57N2ZX (Alanine)
[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:170501
[St] Status:MEDLINE


  2 / 6585 MEDLINE  
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[PMID]:29188241
[Au] Autor:Mondal S; Chakraborty K; Bandyopadhyay S
[Ad] Endereço:Molecular Modeling Laboratory, Department of Chemistry, Indian Institute of Technology, Kharagpur-721302, India. sanjoy@chem.iitkgp.ernet.in.
[Ti] Título:Microscopic understanding of the conformational features of a protein-DNA complex.
[So] Source:Phys Chem Chem Phys;19(48):32459-32472, 2017 Dec 13.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Protein-DNA interactions play crucial roles in different biological processes. Binding of a protein to its target DNA is the key step at different stages of genetic activities. In this article, we have carried out atomistic molecular dynamics simulations to understand the microscopic conformational and dynamical features of the N-terminal domain of the λ-repressor protein and its operator DNA in their complexed state. The calculations revealed that the overall flexibility of the protein and the DNA components reduces due to complex formation. In particular, increased ordering of the DNA sugar rings bound to the protein is found to be associated with modified ring puckering. Attempts have been made to study the effect of complexation on the internal motions of the protein and the DNA components. It is demonstrated that the non-uniform ordering of the side chains of lysine residues in the consensus sequence leads to differential behavior of the two monomers of the homodimeric protein.
[Mh] Termos MeSH primário: DNA/metabolismo
Proteínas Repressoras/metabolismo
Proteínas Virais Reguladoras e Acessórias/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bacteriófago lambda/metabolismo
Sequência de Bases
Sítios de Ligação
DNA/química
Simulação de Dinâmica Molecular
Conformação de Ácido Nucleico
Ligação Proteica
Estrutura Terciária de Proteína
Proteínas Repressoras/química
Proteínas Virais Reguladoras e Acessórias/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Repressor Proteins); 0 (Viral Regulatory and Accessory Proteins); 0 (phage repressor proteins); 9007-49-2 (DNA)
[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:171201
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp05161a


  3 / 6585 MEDLINE  
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[PMID]:28468876
[Au] Autor:Cahill J; Rajaure M; Holt A; Moreland R; O'Leary C; Kulkarni A; Sloan J; Young R
[Ad] Endereço:Center of Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.
[Ti] Título:Suppressor Analysis of the Fusogenic Lambda Spanins.
[So] Source:J Virol;91(14), 2017 Jul 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The final step of lysis in phage λ infections of is mediated by the spanins Rz and Rz1. These proteins form a complex that bridges the cell envelope and that has been proposed to cause fusion of the inner and outer membranes. Accordingly, mutations that block spanin function are found within coiled-coil domains and the proline-rich region, motifs essential in other fusion systems. To gain insight into spanin function, pseudorevertant alleles that restored plaque formation for lysis-defective mutants of and were selected. Most second-site suppressors clustered within a coiled-coil domain of Rz near the outer leaflet of the cytoplasmic membrane and were not allele specific. Suppressors largely encoded polar insertions within the hydrophobic core of the coiled-coil interface. Such suppressor changes resulted in decreased proteolytic stability of the Rz double mutants Unlike the wild type, in which lysis occurs while the cells retain a rod shape, revertant alleles with second-site suppressor mutations supported lysis events that were preceded by spherical cell formation. This suggests that destabilization of the membrane-proximal coiled coil restores function for defective spanin alleles by increasing the conformational freedom of the complex at the cost of its normal, all-or-nothing functionality. encode cell envelope-spanning proteins called spanins, which are thought to fuse the inner and outer membranes during phage lysis. Recent genetic analysis identified the functional domains of the lambda spanins, which are similar to class I viral fusion proteins. While the pre- and postfusion structures of model fusion systems have been well characterized, the intermediate structure(s) formed during the fusion reaction remains elusive. Genetic analysis would be expected to identify functional connections between intermediates. Since most membrane fusion systems are not genetically tractable, only few such investigations have been reported. Here, we report a suppressor analysis of lambda spanin function. To our knowledge this is the first suppression analysis of a class I-like complex and also the first such analysis of a prokaryote membrane fusion system.
[Mh] Termos MeSH primário: Bacteriófago lambda/crescimento & desenvolvimento
Escherichia coli/virologia
Proteínas Mutantes/metabolismo
Supressão Genética
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Bacteriófago lambda/genética
Análise Mutacional de DNA
Modelos Biológicos
Proteínas Mutantes/genética
Conformação Proteica
Domínios Proteicos
Ensaio de Placa Viral
Proteínas Virais/química
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mutant Proteins); 0 (Viral Proteins); 150201-54-0 (Rz protein, bacteriophage lambda)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


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[PMID]:28445747
[Au] Autor:Yang TC; Ortiz D; Yang Q; De Angelis RW; Sanyal SJ; Catalano CE
[Ad] Endereço:Department of Medicinal Chemistry, School of Pharmacy, University of Washington, Seattle, Washington.
[Ti] Título:Physical and Functional Characterization of a Viral Genome Maturation Complex.
[So] Source:Biophys J;112(8):1551-1560, 2017 Apr 25.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genome packaging is strongly conserved in the complex double-stranded DNA viruses, including the herpesviruses and many bacteriophages. In these cases, viral DNA is packaged into a procapsid shell by a terminase enzyme. The packaging substrate is typically a concatemer composed of multiple genomes linked in a head-to-tail fashion, and terminase enzymes perform two essential functions: 1) excision of a unit length genome from the concatemer (genome maturation) and 2) translocation of the duplex into a procapsid (genome packaging). While the packaging motors have been described in some detail, the maturation complexes remain ill characterized. Here we describe the assembly, physical characteristics, and catalytic activity of the λ-genome maturation complex. The λ-terminase protomer is composed of one large catalytic subunit tightly associated with two DNA recognition subunits. The isolated protomer binds DNA weakly and does not discriminate between nonspecific DNA and duplexes that contain the packaging initiation sequence, cos. The Escherichia coli integration host factor protein (IHF) is required for efficient λ-development in vivo and a specific IHF recognition sequence is found within cos. We show that IHF and the terminase protomer cooperatively assemble at the cos site and that the small terminase subunit plays the dominant role in complex assembly. Analytical ultracentrifugation analysis reveals that the maturation complex is composed of four protomers and one IHF heterodimer bound at the cos site. Tetramer assembly activates the cos-cleavage nuclease activity of the enzyme, which matures the genome end in preparation for packaging. The stoichiometry and catalytic activity of the complex is reminiscent of the type IIE and IIF restriction endonucleases and the two systems may share mechanistic features. This study, to our knowledge, provides our first detailed glimpse into the structural and functional features of a viral genome maturation complex, an essential intermediate in the development of complex dsDNA viruses.
[Mh] Termos MeSH primário: Bacteriófago lambda/genética
Bacteriófago lambda/fisiologia
Empacotamento do DNA
Genoma Viral
Proteínas Virais/genética
Proteínas Virais/metabolismo
Montagem de Vírus
[Mh] Termos MeSH secundário: Área Sob a Curva
DNA Viral/genética
DNA Viral/metabolismo
Endodesoxirribonucleases/genética
Endodesoxirribonucleases/metabolismo
Fatores Hospedeiros de Integração/genética
Fatores Hospedeiros de Integração/metabolismo
Regiões Promotoras Genéticas
Multimerização Proteica
Ultracentrifugação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Integration Host Factors); 0 (Viral Proteins); EC 3.1.- (Endodeoxyribonucleases); EC 3.1.- (terminase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE


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[PMID]:28407231
[Au] Autor:Ohuchi S; Suess B
[Ad] Endereço:Department of Biology, Technische Universität Darmstadt, Germany.
[Ti] Título:An inhibitory RNA aptamer against the lambda cI repressor shows transcriptional activator activity in vivo.
[So] Source:FEBS Lett;591(10):1429-1436, 2017 May.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RNA aptamers are one of the promising components for constructing artificial genetic circuits. In this study, we developed a transcriptional activator based on an RNA aptamer against one of the most frequently applied repressor proteins, lambda phage cI. In vitro selection (Systematic Evolution of Ligands by EXponential enrichment) and following in vivo screening identified an RNA aptamer with the intended transcriptional activator activity from an RNA pool containing a 40-nucleotide long random region. Quantitative analysis showed a 35-fold elevation of reporter expression upon aptamer expression. These results suggest that the diversity of artificial transcriptional activators can be extended by employing RNA aptamers against repressor proteins to broaden the parts for constructing genetic circuits.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos/genética
Bacteriófago lambda/genética
Proteínas Repressoras/genética
Transcrição Genética
Proteínas Virais Reguladoras e Acessórias/genética
[Mh] Termos MeSH secundário: Aptâmeros de Nucleotídeos/síntese química
Aptâmeros de Nucleotídeos/química
Bacteriófago lambda/efeitos dos fármacos
Escherichia coli/genética
Escherichia coli/crescimento & desenvolvimento
Genes Reporter
Técnicas In Vitro
Estrutura Molecular
Técnica de Seleção de Aptâmeros
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Aptamers, Nucleotide); 0 (Repressor Proteins); 0 (Viral Regulatory and Accessory Proteins); 0 (phage repressor proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170919
[Lr] Data última revisão:
170919
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12653


  6 / 6585 MEDLINE  
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[PMID]:28338832
[Au] Autor:Goz E; Mioduser O; Diament A; Tuller T
[Ad] Endereço:Department of Biomedical Engineering, Tel-Aviv University, Ramat Aviv 69978, Israel.
[Ti] Título:Evidence of translation efficiency adaptation of the coding regions of the bacteriophage lambda.
[So] Source:DNA Res;24(4):333-342, 2017 Aug 01.
[Is] ISSN:1756-1663
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Deciphering the way gene expression regulatory aspects are encoded in viral genomes is a challenging mission with ramifications related to all biomedical disciplines. Here, we aimed to understand how the evolution shapes the bacteriophage lambda genes by performing a high resolution analysis of ribosomal profiling data and gene expression related synonymous/silent information encoded in bacteriophage coding regions.We demonstrated evidence of selection for distinct compositions of synonymous codons in early and late viral genes related to the adaptation of translation efficiency to different bacteriophage developmental stages. Specifically, we showed that evolution of viral coding regions is driven, among others, by selection for codons with higher decoding rates; during the initial/progressive stages of infection the decoding rates in early/late genes were found to be superior to those in late/early genes, respectively. Moreover, we argued that selection for translation efficiency could be partially explained by adaptation to Escherichia coli tRNA pool and the fact that it can change during the bacteriophage life cycle.An analysis of additional aspects related to the expression of viral genes, such as mRNA folding and more complex/longer regulatory signals in the coding regions, is also reported. The reported conclusions are likely to be relevant also to additional viruses.
[Mh] Termos MeSH primário: Adaptação Biológica
Bacteriófago lambda/genética
Regulação Viral da Expressão Gênica
Biossíntese de Proteínas
[Mh] Termos MeSH secundário: Bacteriófago lambda/crescimento & desenvolvimento
Escherichia coli/genética
Escherichia coli/metabolismo
Escherichia coli/virologia
Evolução Molecular
Perfilação da Expressão Gênica
Genes Virais
RNA Bacteriano/metabolismo
RNA de Transferência/metabolismo
Ribossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Bacterial); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE
[do] DOI:10.1093/dnares/dsx005


  7 / 6585 MEDLINE  
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[PMID]:28337073
[Au] Autor:Johnson SS; Zaikova E; Goerlitz DS; Bai Y; Tighe SW
[Ad] Endereço:Department of Biology, Georgetown University, Washington, DC 20057, USA;; Science, Technology, and International Affairs Program, Georgetown University, Washington, DC 20057, USA.
[Ti] Título:Real-Time DNA Sequencing in the Antarctic Dry Valleys Using the Oxford Nanopore Sequencer.
[So] Source:J Biomol Tech;28(1):2-7, 2017 04.
[Is] ISSN:1943-4731
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The ability to sequence DNA outside of the laboratory setting has enabled novel research questions to be addressed in the field in diverse areas, ranging from environmental microbiology to viral epidemics. Here, we demonstrate the application of offline DNA sequencing of environmental samples using a hand-held nanopore sequencer in a remote field location: the McMurdo Dry Valleys, Antarctica. Sequencing was performed using a MK1B MinION sequencer from Oxford Nanopore Technologies (ONT; Oxford, United Kingdom) that was equipped with software to operate without internet connectivity. One-direction (1D) genomic libraries were prepared using portable field techniques on DNA isolated from desiccated microbial mats. By adequately insulating the sequencer and laptop, it was possible to run the sequencing protocol for up to 2½ h under arduous conditions.
[Mh] Termos MeSH primário: Sequenciamento de Nucleotídeos em Larga Escala/instrumentação
Tipagem Molecular/instrumentação
Análise de Sequência de DNA/instrumentação
[Mh] Termos MeSH secundário: Regiões Antárticas
Bacteriófago lambda/genética
Clima Desértico
Microbiologia Ambiental
Padrões de Referência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE
[do] DOI:10.7171/jbt.17-2801-009


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[PMID]:28334870
[Au] Autor:Burnham DR; Nijholt B; De Vlaminck I; Quan J; Yusufzai T; Dekker C
[Ad] Endereço:Department of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Delft, 2629 HZ, The Netherlands.
[Ti] Título:Annealing helicase HARP closes RPA-stabilized DNA bubbles non-processively.
[So] Source:Nucleic Acids Res;45(8):4687-4695, 2017 May 05.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We investigate the mechanistic nature of the Snf2 family protein HARP, mutations of which are responsible for Schimke immuno-osseous dysplasia. Using a single-molecule magnetic tweezers assay, we construct RPA-stabilized DNA bubbles within torsionally constrained DNA to investigate the annealing action of HARP on a physiologically relevant substrate. We find that HARP closes RPA-stabilized bubbles in a slow reaction, taking on the order of tens of minutes for ∼600 bp of DNA to be re-annealed. The data indicate that DNA re-anneals through the removal of RPA, which is observed as clear steps in the bubble-closing traces. The dependence of the closing rate on both ionic strength and HARP concentration indicates that removal of RPA occurs via an association-dissociation mechanism where HARP does not remain associated with the DNA. The enzyme exhibits classical Michaelis-Menten kinetics and acts cooperatively with a Hill coefficient of 3 ± 1. Our work also allows the determination of some important features of RPA-bubble structures at low supercoiling, including the existence of multiple bubbles and that RPA molecules are mis-registered on the two strands.
[Mh] Termos MeSH primário: DNA Helicases/química
DNA Super-Helicoidal/química
Proteína de Replicação A/química
[Mh] Termos MeSH secundário: Bacteriófago lambda/genética
Bacteriófago lambda/metabolismo
Fenômenos Biomecânicos
DNA Helicases/genética
DNA Helicases/metabolismo
DNA Super-Helicoidal/genética
DNA Super-Helicoidal/metabolismo
Seres Humanos
Cinética
Campos Magnéticos
Pinças Ópticas
Concentração Osmolar
Plasmídeos/química
Plasmídeos/metabolismo
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteína de Replicação A/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Superhelical); 0 (Recombinant Proteins); 0 (Replication Protein A); EC 2.7.7.- (SMARCAL1 protein, human); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx147


  9 / 6585 MEDLINE  
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[PMID]:28130424
[Au] Autor:Strotskaya A; Savitskaya E; Metlitskaya A; Morozova N; Datsenko KA; Semenova E; Severinov K
[Ad] Endereço:Skolkovo Institute of Science and Technology, Moscow, Russia.
[Ti] Título:The action of Escherichia coli CRISPR-Cas system on lytic bacteriophages with different lifestyles and development strategies.
[So] Source:Nucleic Acids Res;45(4):1946-1957, 2017 Feb 28.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:CRISPR-Cas systems provide prokaryotes with adaptive defense against bacteriophage infections. Given an enormous variety of strategies used by phages to overcome their hosts, one can expect that the efficiency of protective action of CRISPR-Cas systems against different viruses should vary. Here, we created a collection of Escherichia coli strains with type I-E CRISPR-Cas system targeting various positions in the genomes of bacteriophages λ, T5, T7, T4 and R1-37 and investigated the ability of these strains to resist the infection and acquire additional CRISPR spacers from the infecting phage. We find that the efficiency of CRISPR-Cas targeting by the host is determined by phage life style, the positions of the targeted protospacer within the genome, and the state of phage DNA. The results also suggest that during infection by lytic phages that are susceptible to CRISPR interference, CRISPR-Cas does not act as a true immunity system that saves the infected cell but rather enforces an abortive infection pathway leading to infected cell death with no phage progeny release.
[Mh] Termos MeSH primário: Bacteriólise
Bacteriófagos/fisiologia
Sistemas CRISPR-Cas
Escherichia coli/fisiologia
Escherichia coli/virologia
[Mh] Termos MeSH secundário: Bacteriófago lambda/genética
Marcação de Genes
Variação Genética
Genoma Viral
Fagos T/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx042


  10 / 6585 MEDLINE  
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[PMID]:28124375
[Au] Autor:Reis LA; Rocha MS
[Ad] Endereço:Laboratório de Física Biológica, Departamento de Física, Universidade Federal de Viçosa, Minas Gerais, Brazil.
[Ti] Título:DNA interaction with DAPI fluorescent dye: Force spectroscopy decouples two different binding modes.
[So] Source:Biopolymers;107(5), 2017 May.
[Is] ISSN:1097-0282
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this work, we use force spectroscopy to investigate the interaction between the DAPI fluorescent dye and the λ-DNA molecule under high (174 mM) and low (34 mM) ionic strengths. Firstly, we have measured the changes on the mechanical properties (persistence and contour lengths) of the DNA-DAPI complexes as a function of the dye concentration in the sample. Then, we use recently developed models in order to connect the behavior of both mechanical properties to the physical chemistry of the interaction. Such analysis has allowed us to identify and to decouple two main binding modes, determining the relevant physicochemical (binding) parameters for each of these modes: minor groove binding, which saturates at very low DAPI concentrations ( CT ∼ 0.50 µM) and presents equilibrium binding constants of the order of ∼10 M for the two ionic strengths studied; and intercalation, which starts to play a significant role only after the saturation of the first mode, presenting much smaller equilibrium binding constants (∼10 M ).
[Mh] Termos MeSH primário: DNA/química
Corantes Fluorescentes/química
Indóis/química
[Mh] Termos MeSH secundário: Bacteriófago lambda/genética
DNA/metabolismo
Cinética
Concentração Osmolar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fluorescent Dyes); 0 (Indoles); 47165-04-8 (DAPI); 9007-49-2 (DNA)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170127
[St] Status:MEDLINE
[do] DOI:10.1002/bip.23015



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde