Search results for " Homology"

showing 10 items of 633 documents

New enveloped dsRNA phage from freshwater habitat.

2015

Cystoviridae is a family of bacteriophages with a tri-segmented dsRNA genome enclosed in a tri-layered virion structure. Here, we present a new putative member of the Cystoviridae family, bacteriophage ϕNN. ϕNN was isolated from a Finnish lake in contrast to the previously identified cystoviruses, which originate from various legume samples collected in the USA. The nucleotide sequence of the virus reveals a strong genetic similarity (~80 % for the L-segments, ~55 % for the M-segments and ~84 % for the S-segments) to Pseudomonas phage ϕ6, the type member of the virus family. However, the relationship between ϕNN and other cystoviruses is more distant. In general, proteins located in the int…

CystoviridaevirusesMolecular Sequence DataFresh Waterfreshwater habitatsGenomeVirusBacteriophage03 medical and health sciencesVirologyPseudomonasSequence Homology Nucleic AcidCluster AnalysisBacteriophagesFinlandPhylogeny030304 developmental biologyGenetics0303 health sciencesbiology030306 microbiologyta1183ta1182Bacteriophage phi 6Nucleic acid sequenceSequence Analysis DNAbiology.organism_classificationVirologyRNA silencingLakesMolecular virologyRNA ViralRecombinationThe Journal of general virology
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Study of the Evolutionary Relationships among Limonium Species (Plumbaginaceae) Using Nuclear and Cytoplasmic Molecular Markers

2000

The genus Limonium, due to the patchiness of the natural habitats of its species as well as the high frequency of hybridization and polyploidy and the possibility of reproduction by apomixis, provides an example of all the principal mechanisms of rapid speciation of plants. As an initial study of evolution in this genus, we have analyzed intra- and interspecific variability in 17 species from section Limonium, the largest in the genus, based on RFLPs of cpDNA and nuclear rDNA ITS sequences. In the cpDNA analysis, 21 restriction enzymes were used, resulting in 779 fragments, 490 of which were variable and 339 parsimony informative. L. furfuraceum exhibited two relatively divergent cpDNA hapl…

CytoplasmChloroplastsLimoniumMolecular Sequence DataBiologyDNA RibosomalPhylogeneticsSequence Homology Nucleic AcidApomixisPolyphylyBotanyGeneticsMolecular BiologyPhylogenyPlant Physiological PhenomenaEcology Evolution Behavior and SystematicsCell NucleusBase SequencePhylogenetic treeMediterranean RegionReproductionGenetic VariationPlantsbiology.organism_classificationBiological EvolutionReticulate evolutionChloroplast DNARestriction fragment length polymorphismPolymorphism Restriction Fragment LengthMolecular Phylogenetics and Evolution
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Establishment and functional validation of a structural homology model for human DNA methyltransferase 1

2003

Changes in DNA methylation patterns play an important role in tumorigenesis. The DNA methyltransferase 1 (DNMT1) protein represents a major DNA methyltransferase activity in human cells and is therefore a prominent target for experimental cancer therapies. However, there are only few available inhibitors and their high toxicity and low specificity have so far precluded their broad use in chemotherapy. Based on the strong conservation of catalytic DNA methyltransferase domains we have used a homology modeling approach to determine the three-dimensional structure of the DNMT1 catalytic domain. Our results suggest an overall structural conservation with other DNA methyltransferases but also in…

DNA (Cytosine-5-)-Methyltransferase 1Models MolecularMethyltransferaseMolecular Sequence DataBiophysicsDNA Methyltransferase InhibitorComputational biologyBiologymedicine.disease_causeModels BiologicalBiochemistryDNA methyltransferasechemistry.chemical_compoundCatalytic DomainTumor Cells CulturedmedicineHumansAmino Acid SequenceDNA (Cytosine-5-)-MethyltransferasesHomology modelingEnzyme InhibitorsMolecular BiologyGeneticsSequence Homology Amino AcidCell BiologyDNA MethylationModels ChemicalchemistryDNA methylationAzacitidineDNMT1Nucleic Acid ConformationCarcinogenesisDNABiochemical and Biophysical Research Communications
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Induction of DNA strand breaks and expression of HSP70 and GRP78 homolog by cadmium in the marine sponge Suberites domuncula

1998

The marine sponge Suberites domuncula was used as a bioindicator to study the effects of cadmium on the occurrence of DNA strand breakage and on the induction of the expression of the stress biomarkers, heat shock protein 70 (HSP70) and glucose-regulated protein 78 (GRP78) homolog. The cDNA encoding GRP78 homolog from S. domuncula was isolated and characterized. The GRP78 cDNA has a length of 2.1 kb and displays characteristic features of the HSP70 family ; it encodes an aa sequence of M-r 72, 000. Exposure of S. domuncula to 1 mg/L of cadmium chloride for 24 h caused a strong(16.6-fold) increase in cadmium content to 7.7 mu g/g wet weight of sponge tissue ; after an incubation period of 6 …

DNA damageHealth Toxicology and MutagenesisMolecular Sequence Datachemistry.chemical_elementCadmium chlorideToxicologyIncubation periodchemistry.chemical_compoundCadmium ChlorideGlucose-regulated protein. Heat-shock proteins. Geodia-cydonium.Mediterranean SeaAnimalsHSP70 Heat-Shock ProteinsAmino Acid SequenceNorthern blotIncubationHeat-Shock ProteinsCadmiumGreeceSequence Homology Amino AcidbiologyEcologyDNAGeneral Medicinebiology.organism_classificationPollutionMolecular biologyPoriferaHsp70Suberites domunculaZincchemistryWater Pollutants ChemicalDNA DamageMutagens
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Comprehensive DNA methylation analysis of the Aedes aegypti genome

2016

AbstractAedes aegypti mosquitoes are important vectors of viral diseases. Mosquito host factors play key roles in virus control and it has been suggested that dengue virus replication is regulated by Dnmt2-mediated DNA methylation. However, recent studies have shown that Dnmt2 is a tRNA methyltransferase and that Dnmt2-dependent methylomes lack defined DNA methylation patterns, thus necessitating a systematic re-evaluation of the mosquito genome methylation status. We have now searched the Ae. aegypti genome for candidate DNA modification enzymes. This failed to reveal any known (cytosine-5) DNA methyltransferases, but identified homologues for the Dnmt2 tRNA methyltransferase, the Mettl4 (…

DNA Bacterial0301 basic medicineBisulfite sequencingDNA methyltransferaseArticleMass Spectrometry03 medical and health sciences0302 clinical medicineRNA TransferAedesAnimalsAmino Acid SequenceDNA (Cytosine-5-)-MethyltransferasesEpigeneticsGeneticsGenomeMultidisciplinaryTRNA methylationSequence Homology Amino AcidWhole Genome SequencingbiologyTRNA MethyltransferaseSequence Analysis DNAMethylationDNA Methylation030104 developmental biology030220 oncology & carcinogenesisDNA methylationbiology.proteinInsect ProteinsDemethylaseSequence AlignmentScientific Reports
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Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster

1998

ABSTRACT A citrate lyase (EC 4.1.3.6 ) was purified 25-fold from Leuconostoc mesenteroides and was shown to contain three subunits. The first 42 amino acids of the β subunit were identified, as well as an internal peptide sequence spanning some 20 amino acids into the α subunit. Using degenerated primers from these sequences, we amplified a 1.2-kb DNA fragment by PCR from Leuconostoc mesenteroides subsp. cremoris . This fragment was used as a probe for screening a Leuconostoc genomic bank to identify the structural genes. The 2.7-kb gene cluster encoding citrate lyase of L. mesenteroides is organized in three open reading frames, citD , citE , and citF , encoding, respectively, the three ci…

DNA BacterialATP citrate lyaseMolecular Sequence DataGene ExpressionBiologymedicine.disease_causeMicrobiologyBacterial ProteinsCarbon-Sulfur LigasesMultienzyme ComplexesGene clusterAcyl Carrier ProteinEscherichia colimedicineLeuconostocAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliBase SequenceSequence Homology Amino AcidStructural geneOxo-Acid-LyasesSequence Analysis DNALyasebiology.organism_classificationEnzymes and ProteinsMolecular biologyOxaloacetate decarboxylaseBiochemistryGenes BacterialLeuconostoc mesenteroidesMultigene FamilyCoenzyme A-TransferasesLeuconostoc
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Geographical and temporal structures of Legionella pneumophila sequence types in comunitat valenciana (Spain), 1998 to 2013

2015

ABSTRACT Legionella pneumophila is an accidental human pathogen associated with aerosol formation in water-related sources. High recombination rates make Legionella populations genetically diverse, and nearly 2,000 different sequence types (STs) have been described to date for this environmental pathogen. The spatial distribution of STs is extremely heterogeneous, with some variants being present worldwide and others being detected at only a local scale. Similarly, some STs have been associated with disease outbreaks, such as ST578 or ST23. Spain is among the European countries with the highest incidences of reported legionellosis cases, and specifically, Comunitat Valenciana (CV) is the se…

DNA BacterialBIOFILMS[SDV.BIO]Life Sciences [q-bio]/BiotechnologyGenotypeLegionellaOUTBREAKSequence HomologyZoologyRECOMBINATIONHuman pathogenLEGIONNAIRES-DISEASESOFTWAREBiologySpatial distributionApplied Microbiology and BiotechnologyLegionella pneumophilaLegionella pneumophilaMicrobiology03 medical and health sciencesSpatio-Temporal AnalysisEnvironmental MicrobiologyCluster AnalysisHumansTypingPOPULATION-STRUCTUREPhylogeny030304 developmental biology0303 health sciencesEcologyPublic and Environmental Health Microbiology030306 microbiologySTRAINSSCHEMELocal scaleGenetic VariationOutbreakSequence Analysis DNASequence typesbiology.organism_classification3. Good healthMolecular TypingLIFE[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologySpainLegionnaires' DiseaseFood ScienceBiotechnology
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Vip3C, a novel class of vegetative insectidal proteins from Bacillus thuringiensis

2012

Three vip3 genes were identified in two Bacillus thuringiensis Spanish collections. Sequence analysis revealed a novel Vip3 protein class (Vip3C). Preliminary bioassays of larvae from 10 different lepidopteran species indicated that Vip3Ca3 caused more than 70% mortality in four species after 10 days at 4 οg/cm 2. © 2012, American Society for Microbiology.

DNA BacterialBioquímicaSequence analysisMolecular Sequence DataBiotecnologia agrícolaBacillus thuringiensisBiologyApplied Microbiology and BiotechnologyLepidoptera genitaliaBacterial proteinPlagues ControlBacterial ProteinsPhylogeneticsBacillus thuringiensisBotanyPlaguicidesInvertebrate MicrobiologyAnimalsBioassayGenePhylogenyLarvaSequence Homology Amino AcidEcologyfungiSequence Analysis DNAbiology.organism_classificationSurvival AnalysisVip3 genesLepidopteraSpainLarvaProteïnesFood ScienceBiotechnology
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Cloning and sequencing of the gene encoding α-acetolactate decarboxylase fromLeuconostoc oenos

1996

The alsD gene encoding alpha-acetolactate decarboxylase was isolated from a genomic library of Leuconostoc oenos, using a screening procedure developed on microtiter plates. The nucleotide sequence of alsD encodes a putative protein of 239 amino acids showing significant similarity with other bacterial alpha-acetolactate decarboxylases. Upstream from alsD lies an open reading frame (alsS) which is highly similar to bacterial genes coding for catabolic alpha-acetolactate synthases. Northern (RNA) blotting analyses indicated the presence of a 2.4-kb dicistronic transcript of alsS and alsD. This suggests that the alsS and alsD genes are organized in a single operon.

DNA BacterialCarboxy-LyasesOperonMolecular Sequence DataRestriction MappingBiologyMicrobiologyGene Expression Regulation EnzymologicGeneticsLeuconostocGenomic libraryCloning MolecularMolecular BiologyGeneGeneticsCloningSequence Homology Amino AcidNucleic acid sequenceGene Expression Regulation BacterialSequence Analysis DNABlotting Northernbiology.organism_classificationAcetolactate decarboxylaseAcetolactate SynthaseRNA BacterialOpen reading framePhenotypeBiochemistryGenes BacterialLactatesLeuconostocFEMS Microbiology Letters
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Gene Cloning, Transcriptional Analysis, Purification, and Characterization of Phenolic Acid Decarboxylase from Bacillus subtilis

1998

Phenolic acids, also called substituted cinnamic acids, are important lignin-related aromatic acids and natural constituents of plant cell walls. These acids (particularly ferulic, p-coumaric, and caffeic acids) bind the complex lignin polymer to the hemicellulose and cellulose in plants (1) or are generally esterified with tartaric acid (for example, in grape must, wine, and cider) and can be released as free acids during wine making by some cinnamoyl esterase activities (9). Most often, free phenolic acids are metabolized by different microorganisms into 4-vinyl derivatives and then are eventually reduced into 4-ethyl derivatives (5, 6). Some of these volatile phenols, particularly vinyl …

DNA BacterialCarboxy-lyasesCarboxy-LyasesMolecular Sequence DataGenetics and Molecular BiologyBacillus subtilisBiologyApplied Microbiology and BiotechnologyEsteraseGene Expression Regulation EnzymologicSubstrate SpecificityFerulic acidchemistry.chemical_compoundCaffeic acidEscherichia coliPhenolsAmino Acid SequenceCloning MolecularDNA Primerschemistry.chemical_classificationEcologyBase SequenceSequence Homology Amino Acidfood and beveragesChromosome MappingPhenolic acidGene Expression Regulation Bacterialbiology.organism_classificationRecombinant ProteinsAmino acidchemistryBiochemistryGenes BacterialbacteriaFood ScienceBiotechnologyBacillus subtilis
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