Base de dados : MEDLINE
Pesquisa : B04.123.150.500.260 [Categoria DeCS]
Referências encontradas : 662 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 67 ir para página                         

  1 / 662 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26847688
[Au] Autor:Pulkkinen E; Haapa-Paananen S; Savilahti H
[Ad] Endereço:Division of Genetics and Physiology, Department of Biology, University of Turku, 20520, Turku, Finland.
[Ti] Título:MuA-mediated in vitro cloning of circular DNA: transpositional autointegration and the effect of MuB.
[So] Source:Mol Genet Genomics;291(3):1181-91, 2016 Jun.
[Is] ISSN:1617-4623
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Transposons provide useful tools for genetics and genomics studies, as they can be modified easily for a variety of purposes. In this study, a strategy to clone circular DNA was developed on the basis of an efficient Mu in vitro transposition reaction catalyzed by MuA transposase. The transposon used contains a selectable marker as well as an origin of replication, and in vitro integration of the transposon into circular DNA generates a plasmid that can replicate in E. coli. We show that the substrate stoichiometry plays an important role in the profile of intermolecular versus intramolecular transposition reaction products. Increasing the relative amount of target DNA reduced the frequency of intramolecular products that are non-productive with regard to the developed cloning application. Such autointegration was also reduced in the reactions containing phage Mu-encoded MuB, indicating that this protein can be used for cloning in combination with MuA, and it is particularly useful with a limited amount of target DNA. The developed strategy can now be utilized to clone DNA circles regardless of their origin as long as their size is not prohibitive for transformation.
[Mh] Termos MeSH primário: Clonagem Molecular/métodos
Elementos de DNA Transponíveis
DNA Circular
Proteínas de Ligação a DNA/metabolismo
Escherichia coli/genética
Transposases/metabolismo
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Bacteriófago mu/enzimologia
Replicação do DNA
Técnicas In Vitro
Plasmídeos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (DNA, Circular); 0 (DNA-Binding Proteins); 0 (MuB protein, Enterobacteria phage Mu); 0 (Viral Proteins); EC 2.7.7.- (Transposases)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160206
[St] Status:MEDLINE
[do] DOI:10.1007/s00438-016-1175-2


  2 / 662 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26619078
[Au] Autor:Zhu D; Li R; Liu F; Xu H; Li B; Yuan Y; Saris PE; Qiao M
[Ad] Endereço:Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, Nankai University, Tianjin, China.
[Ti] Título:Mu insertion in feuD triggers the increase in nisin immunity in Lactococcus lactis subsp. lactis N8.
[So] Source:J Appl Microbiol;120(2):402-12, 2016 Feb.
[Is] ISSN:1365-2672
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: This study aims to explore how feuD mutation triggered the increase in nisin immunity of Lactococcus lactis L58, which was proven to be a feuD::Em-Mu mutant of Lc. lactis N8. METHODS AND RESULTS: The significant difference genes of Lc. lactis L58 and Lc. lactis N8 were compared at transcription and protein levels. Analysis revealed that the feuD mutation induced decrease in histidine-containing phosphocarrier protein PtsH (HPr) and increase in thioredoxin reductase TrxB (TR). Determination of iron concentration and cytoplasmic membrane potential (MP) showed the iron concentration decreased around 10% and the MP decreased approx. 14% in Lc. lactis L58. CONCLUSIONS: The increase in nisin immunity was dominated by TR up-expression by two main mechanisms in Lc. lactis L58. First, the TR-TRX (thioredoxin reductase) system changed the composition of cytoplasmic membrane by regulating the lipid metabolism to enhance the cells' resistance to nisin. Second, iron starvation stress induced decrease in MP; hence, the binding affinity of nisin to lipid II of Lc. lactis L58 decreased, which, in turn, increased the nisin immunity. SIGNIFICANCE AND IMPACT OF THE STUDY: The knowledge on regulation mechanism of nisin immunity was enriched, and the theoretical basis for improving nisin production in engineering strain could be provided.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Bacteriófago mu/genética
Lactococcus lactis/genética
Mutagênese Insercional
Nisina/imunologia
[Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo
Lactococcus lactis/imunologia
Nisina/genética
Sistema Fosfotransferase de Açúcar do Fosfoenolpiruvato/genética
Sistema Fosfotransferase de Açúcar do Fosfoenolpiruvato/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (nisin A); 1414-45-5 (Nisin); EC 2.7.1.- (Phosphoenolpyruvate Sugar Phosphotransferase System); EC 2.7.1.- (phosphocarrier protein HPr)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151201
[St] Status:MEDLINE
[do] DOI:10.1111/jam.13015


  3 / 662 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26070688
[Au] Autor:Li Y; Bai F; Xia H; Zhuang L; Xu H; Jin Y; Zhang X; Bai Y; Qiao M
[Ad] Endereço:College of Life Sciences, Nankai University, Tianjin 300071, China; School of Public Health, Chongqing Medical University, Chongqing 400016, China.
[Ti] Título:A novel regulator PA5022 (aefA) is involved in swimming motility, biofilm formation and elastase activity of Pseudomonas aeruginosa.
[So] Source:Microbiol Res;176:14-20, 2015 Jul.
[Is] ISSN:1618-0623
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Pseudomonas aeruginosa is an opportunistic pathogen contributing to a range of nosocomial infections. To identify new genes involved in P. aeruginosa swimming motility, an important mechanism of pathogenesis, mutants with altered swimming motility patterns from Mu transposon mutagenesis library of the P. aeruginosa clinical strain PA68 were isolated and characterized. We identified a mutant with transposon inactivation of PA5022 has completely abolished its swimming motility while still possesses a normal terminal flagellum according to electronic microscopy analysis. Microscopic examination revealed that the PA5022 mutant forms thicker biofilms compared to the PA68 wild-type strain and is impaired in its elastase activity. To exclude the possibility of genetic diversity in affecting gene functions among different strains, we constructed a PA5022 knock out mutant based on the PAK lab strain. The PAKΔPA5022 has similar phenotypes to the PA5022 (PA5022::Mu) mutant of PA68 strain. Furthermore, transcriptional fusion assays were carried out to investigate the regulatory mechanism of PA5022 by using the PlasI-lacZ, PrhlI-lacZ, PrpoN-lacZ, PrpoS-lacZ, PqscR-lacZ, PvqsR-lacZ fusions. ß-Galactosidase activity assays indicated that the expression of the vqsR, lasI and rhlI promotors was reduced in the PA5022 mutant compared to the PA68 wild-type. Our study showed that PA5022 links swimming motility and quorum sensing, which might be an important regulator for the pathogenesis of P. aeruginosa.
[Mh] Termos MeSH primário: Biofilmes/crescimento & desenvolvimento
Regulação Bacteriana da Expressão Gênica
Locomoção
Elastase Pancreática/biossíntese
Pseudomonas aeruginosa/fisiologia
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Bacteriófago mu
Flagelos/ultraestrutura
Deleção de Genes
Microscopia Eletrônica de Transmissão
Mutagênese Insercional
Pseudomonas aeruginosa/genética
Pseudomonas aeruginosa/ultraestrutura
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Transcription Factors); EC 3.4.21.36 (Pancreatic Elastase)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150613
[Lr] Data última revisão:
150613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150614
[St] Status:MEDLINE


  4 / 662 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26058069
[Au] Autor:Swapna G; Kumari V; Nagaraja V
[Ad] Endereço:Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, India.
[Ti] Título:Different Modes of Transactivation of Bacteriophage Mu Late Promoters by Transcription Factor C.
[So] Source:PLoS One;10(6):e0129504, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Transactivator protein C is required for the expression of bacteriophage Mu late genes from lys, I, P and mom promoters during lytic life cycle of the phage. The mechanism of transcription activation of mom gene by C protein is well understood. C activates transcription at Pmom by initial unwinding of the promoter DNA, thereby facilitating RNA polymerase (RNAP) recruitment. Subsequently, C interacts with the ß' subunit of RNAP to enhance promoter clearance. The mechanism by which C activates other late genes of the phage is not known. We carried out promoter-polymerase interaction studies with all the late gene promoters to determine the individual step of C mediated activation. Unlike at Pmom, at the other three promoters, RNAP recruitment and closed complex formation are not C dependent. Instead, the action of C at Plys, PI, and PP is during the isomerization from closed complex to open complex with no apparent effect at other steps of initiation pathway. The mechanism of transcription activation of mom and other late promoters by their common activator is different. This distinction in the mode of activation (promoter recruitment and escape versus isomerization) by the same activator at different promoters appears to be important for optimized expression of each of the late genes.
[Mh] Termos MeSH primário: Bacteriófago mu/genética
Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/genética
Regiões Promotoras Genéticas/genética
Transativadores/genética
Transcrição Genética/genética
Ativação Transcricional/genética
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Sítios de Ligação/genética
Proteínas de Ligação a DNA/genética
RNA Polimerases Dirigidas por DNA/genética
Regulação Viral da Expressão Gênica/genética
Ligação Proteica/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Leucine Zipper Transcription Factors); 0 (C protein, Bacteriophage Mu); 0 (DNA-Binding Proteins); 0 (Trans-Activators); 0 (Viral Proteins); EC 2.7.7.6 (DNA-Directed RNA Polymerases)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:150617
[Lr] Data última revisão:
150617
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150610
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0129504


  5 / 662 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25983038
[Au] Autor:Jang S; Harshey RM
[Ad] Endereço:Department of Molecular Biosciences, University of Texas at Austin, Austin, TX, 78712, USA.
[Ti] Título:Repair of transposable phage Mu DNA insertions begins only when the E. coli replisome collides with the transpososome.
[So] Source:Mol Microbiol;97(4):746-58, 2015 Aug.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We report a new cellular interaction between the infecting transposable phage Mu and the host Escherichia coli replication machinery during repair of Mu insertions, which involves filling-in of short target gaps on either side of the insertion, concomitant with degradation of extraneous long flanking DNA (FD) linked to Mu. Using the FD as a marker to follow repair, we find that after transposition into the chromosome, the unrepaired Mu is indefinitely stable until the replication fork arrives at the insertion site, whereupon the FD is rapidly degraded. When the fork runs into a Mu target gap, a double strand end (DSE) will result; we demonstrate fork-dependent DSEs proximal to Mu. These findings suggest that Pol III stalled at the transpososome is exploited for co-ordinated repair of both target gaps flanking Mu without replicating the intervening 37 kb of Mu, disassembling the stable transpososome in the process. This work is relevant to all transposable elements, including retroviral elements like HIV-1, which share with Mu the common problem of repair of their flanking target gaps.
[Mh] Termos MeSH primário: Bacteriófago mu/genética
Reparo do DNA
Elementos de DNA Transponíveis/genética
Escherichia coli/genética
Transposases/genética
[Mh] Termos MeSH secundário: DNA Polimerase III/genética
DNA Polimerase III/metabolismo
Replicação do DNA
DNA Viral/genética
Escherichia coli/metabolismo
Recombinação Genética
Transposases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (DNA, Viral); EC 2.7.7.- (DNA Polymerase III); EC 2.7.7.- (Transposases)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150519
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13061


  6 / 662 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25902138
[Au] Autor:Jakhetia R; Verma NK
[Ad] Endereço:Division of Biomedical Science and Biochemistry, Research School of Biology, The Australian National University, Canberra, ACT 0200, Australia.
[Ti] Título:Identification and Molecular Characterisation of a Novel Mu-Like Bacteriophage, SfMu, of Shigella flexneri.
[So] Source:PLoS One;10(4):e0124053, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:S. flexneri is the leading cause of bacillary dysentery in the developing countries. Several temperate phages originating from this host have been characterised. However, all S. flexneri phages known to date are lambdoid phages, which have the ability to confer the O-antigen modification of their host. In this study, we report the isolation and characterisation of a novel Mu-like phage from a serotype 4a strain of S. flexneri. The genome of phage SfMu is composed of 37,146 bp and is predicted to contain 55 open reading frames (orfs). Comparative genome analysis of phage SfMu with Mu and other Mu-like phages revealed that SfMu is closely related to phage Mu, sharing >90% identity with majority of its proteins. Moreover, investigation of phage SfMu receptor on the surface of the host cell revealed that the O-antigen of the host serves as the receptor for the adsorption of phage SfMu. This study also demonstrates pervasiveness of SfMu phage in S. flexneri, by identifying complete SfMu prophage strains of serotype X and Y, and remnants of SfMu in strains belonging to 4 other serotypes, thereby indicating that transposable phages in S. flexneri are not uncommon. The findings of this study contribute an advance in our current knowledge of S. flexneri phages and will also play a key role in understanding the evolution of S. flexneri.
[Mh] Termos MeSH primário: Bacteriófago mu/genética
DNA Viral/genética
Genoma Viral
Shigella flexneri/virologia
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Bacteriófago mu/metabolismo
Mapeamento Cromossômico
DNA Viral/metabolismo
Tamanho do Genoma
Antígenos O/química
Antígenos O/metabolismo
Fases de Leitura Aberta
Receptores Virais/química
Receptores Virais/metabolismo
Análise de Sequência de DNA
Sorotipagem
Shigella flexneri/metabolismo
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (O Antigens); 0 (Receptors, Virus); 0 (Viral Proteins)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150423
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0124053


  7 / 662 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25645531
[Au] Autor:Ma J; Howe MM
[Ad] Endereço:Department of Microbiology, Immunology & Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163.
[Ti] Título:The phage Mu middle promoter Pm contains a partial UP element.
[So] Source:G3 (Bethesda);5(4):507-16, 2015 Feb 02.
[Is] ISSN:2160-1836
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:There are three phases of transcription during lytic development of bacteriophage Mu: early, middle, and late. Transcription from the middle phase promoter Pm requires the activator protein Mor. In the presence of Mor, transcription from Pm is carried out by the Escherichia coli RNA polymerase holoenzyme containing σ(70). A Mor dimer binds to two 5-bp inverted repeats within a 16-bp element centered at -43.5 in Pm, replacing the normal -35 element contacted by RNA polymerase (RNAP). In this study random and targeted mutagenesis of the sequence upstream (-88 to -52) of the Mor binding site was performed to determine whether Pm also contains an UP element for binding of the RNAP α subunit, thereby stimulating transcription. The results demonstrated that mutations upstream of -57 had no effect on Pm activity in vivo, assayed by expression of lacZ fused downstream of a wild-type or mutant Pm. Mutations at positions -57 through -52 led to decreased transcription from Pm, consistent with the presence of an UP element. In DNase I footprinting and gel mobility shift assays, paired mutations at positions -55 and -54 did not affect Mor binding but decreased the synergistic binding of Mor with histidine tagged α (His-α), indicating that His-α binds to Pm in a sequence- and/or structure-specific manner. Taken together, these results demonstrate that Pm has a strong proximal UP element subsite, but lacks a distal subsite.
[Mh] Termos MeSH primário: Bacteriófago mu/genética
Regiões Promotoras Genéticas
[Mh] Termos MeSH secundário: Sequência de Bases
Sítios de Ligação
RNA Polimerases Dirigidas por DNA/química
RNA Polimerases Dirigidas por DNA/metabolismo
Desoxirribonuclease I/metabolismo
Ensaio de Desvio de Mobilidade Eletroforética
Mutagênese
Plasmídeos/genética
Plasmídeos/metabolismo
Transativadores/genética
Transativadores/metabolismo
Transcrição Genética
Proteínas Virais/química
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Mor protein, Enterobacteria phage Mu); 0 (Trans-Activators); 0 (Viral Proteins); EC 2.7.7.6 (DNA-Directed RNA Polymerases); EC 2.7.7.6 (RNA polymerase alpha subunit); EC 3.1.21.1 (Deoxyribonuclease I)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:150411
[Lr] Data última revisão:
150411
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150204
[St] Status:MEDLINE
[do] DOI:10.1534/g3.114.013607


  8 / 662 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26104374
[Au] Autor:Harshey RM
[Ti] Título:Transposable Phage Mu.
[So] Source:Microbiol Spectr;2(5), 2014 Oct.
[Is] ISSN:2165-0497
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Transposable phage Mu has played a major role in elucidating the mechanism of movement of mobile DNA elements. The high efficiency of Mu transposition has facilitated a detailed biochemical dissection of the reaction mechanism, as well as of protein and DNA elements that regulate transpososome assembly and function. The deduced phosphotransfer mechanism involves in-line orientation of metal ion-activated hydroxyl groups for nucleophilic attack on reactive diester bonds, a mechanism that appears to be used by all transposable elements examined to date. A crystal structure of the Mu transpososome is available. Mu differs from all other transposable elements in encoding unique adaptations that promote its viral lifestyle. These adaptations include multiple DNA (enhancer, SGS) and protein (MuB, HU, IHF) elements that enable efficient Mu end synapsis, efficient target capture, low target specificity, immunity to transposition near or into itself, and efficient mechanisms for recruiting host repair and replication machineries to resolve transposition intermediates. MuB has multiple functions, including target capture and immunity. The SGS element promotes gyrase-mediated Mu end synapsis, and the enhancer, aided by HU and IHF, participates in directing a unique topological architecture of the Mu synapse. The function of these DNA and protein elements is important during both lysogenic and lytic phases. Enhancer properties have been exploited in the design of mini-Mu vectors for genetic engineering. Mu ends assembled into active transpososomes have been delivered directly into bacterial, yeast, and human genomes, where they integrate efficiently, and may prove useful for gene therapy.
[Mh] Termos MeSH primário: Bacteriófago mu/fisiologia
Elementos de DNA Transponíveis
DNA Viral/metabolismo
Proteínas Virais/metabolismo
Integração Viral
[Mh] Termos MeSH secundário: Bacteriófago mu/genética
Recombinação Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (DNA, Viral); 0 (Viral Proteins)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150625
[St] Status:MEDLINE
[do] DOI:10.1128/microbiolspec.MDNA3-0007-2014


  9 / 662 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25256747
[Au] Autor:Choi W; Saha RP; Jang S; Harshey RM
[Ad] Endereço:Department of Molecular Biosciences & Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, TX, 78712, USA.
[Ti] Título:Controlling DNA degradation from a distance: a new role for the Mu transposition enhancer.
[So] Source:Mol Microbiol;94(3):595-608, 2014 Nov.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phage Mu is unique among transposable elements in employing a transposition enhancer. The enhancer DNA segment is the site where the transposase MuA binds and makes bridging interactions with the two Mu ends, interwrapping the ends with the enhancer in a complex topology essential for assembling a catalytically active transpososome. The enhancer is also the site at which regulatory proteins control divergent transcription of genes that determine the phage lysis-lysogeny decision. Here we report a third function for the enhancer - that of regulating degradation of extraneous DNA attached to both ends of infecting Mu. This DNA is protected from nucleases by a phage protein until Mu integrates into the host chromosome, after which it is rapidly degraded. We find that leftward transcription at the enhancer, expected to disrupt its topology within the transpososome, blocks degradation of this DNA. Disruption of the enhancer would lead to the loss or dislocation of two non-catalytic MuA subunits positioned in the transpososome by the enhancer. We provide several lines of support for this inference, and conclude that these subunits are important for activating degradation of the flanking DNA. This work also reveals a role for enhancer topology in phage development.
[Mh] Termos MeSH primário: Bacteriófago mu/enzimologia
Bacteriófago mu/genética
Elementos de DNA Transponíveis
DNA/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Evolução Molecular
Hidrólise
Ligação Proteica
Recombinação Genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (Viral Proteins); 9007-49-2 (DNA)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140927
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.12781


  10 / 662 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25197059
[Au] Autor:Choi W; Jang S; Harshey RM
[Ad] Endereço:Department of Molecular Biosciences and Institute of Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712.
[Ti] Título:Mu transpososome and RecBCD nuclease collaborate in the repair of simple Mu insertions.
[So] Source:Proc Natl Acad Sci U S A;111(39):14112-7, 2014 Sep 30.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The genome of transposable phage Mu is packaged as a linear segment, flanked by several hundred base pairs of non-Mu DNA. The linear ends are held together and protected from nucleases by the phage N protein. After transposition into the Escherichia coli chromosome, the flanking DNA (FD) is degraded, and the 5-bp gaps left in the target are repaired to generate a simple Mu insertion. Our study provides insights into this repair pathway. The data suggest that the first event in repair is removal of the FD by the RecBCD exonuclease, whose entry past the N-protein block is licensed by the transpososome. In vitro experiments reveal that, when RecBCD is allowed entry into the FD, it degrades this DNA until it arrives at the transpososome, which presents a barrier for further RecBCD movement. RecBCD action is required for stimulating endonucleolytic cleavage within the transpososome-protected DNA, leaving 4-nt flanks outside both Mu ends. This end product of collaboration between the transpososome and RecBCD resembles the intermediate products of Tn7 and retroviral and retrotransposon transposition, and may hint at a common gap-repair mechanism in these diverse transposons.
[Mh] Termos MeSH primário: Bacteriófago mu/genética
Bacteriófago mu/metabolismo
Elementos de DNA Transponíveis/genética
Exodesoxirribonuclease V/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Reparo do DNA
DNA Viral/genética
DNA Viral/metabolismo
Escherichia coli K12/genética
Escherichia coli K12/metabolismo
Escherichia coli K12/virologia
Células HEK293
Seres Humanos
Modelos Biológicos
Mutagênese Sítio-Dirigida
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Especificidade da Espécie
Transposases/química
Transposases/genética
Transposases/metabolismo
Proteínas Virais/química
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Transposable Elements); 0 (DNA, Viral); 0 (Viral Proteins); EC 2.7.- (mu transposase); EC 2.7.7.- (Transposases); EC 3.1.11.5 (Exodeoxyribonuclease V)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140909
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1407562111



página 1 de 67 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

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