Search results for "sequence data"

showing 10 items of 1952 documents

A DNA region ofTorulaspora delbrueckii containing theHIS3 gene: sequence, gene order and evolution

2003

We cloned a genomic DNA fragment of the yeast Torulaspora delbrueckii by complementation of a Saccharomyces cerevisiae his3 mutant strain. DNA sequence analysis revealed that the fragment contained two complete ORFs, which share a high similarity with S. cerevisiae His3p and Mrp51p, respectively. The cloned TdHIS3 gene fully complemented the his3 mutation of S. cerevisiae, confirming that it encodes for the imidazoleglycerol-phosphate dehydrate of T. delbrueckii. Two additional ORFs, with a high homology to S. cerevisiae PET56 and DED1 genes, were mapped upstream and downstream from TdHIS3 and TdMRP51, respectively. This genetic organization is analogous to that previously found in Saccharo…

Saccharomyces cerevisiae ProteinsTranscription GeneticSequence analysisMolecular Sequence DataSaccharomyces cerevisiaeCell Cycle ProteinsBioengineeringBiologyApplied Microbiology and BiotechnologyBiochemistryHomology (biology)DEAD-box RNA HelicasesEvolution MolecularFungal ProteinsOpen Reading FramesTorulaspora delbrueckiiGeneticsAmino Acid SequenceCloning MolecularORFSDNA FungalGeneHydro-LyasesPhylogenyGeneticsBase SequenceMethyltransferasesbiology.organism_classificationMolecular biologygenomic DNASaccharomycetalesChromosomal regionSequence AlignmentRNA HelicasesBiotechnologyYeast
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Molecular cloning and characterization of a Candida albicans gene coding for cytochrome c haem lyase and a cell wall-related protein.

1998

Immunoscreening of a Candida albicans cDNA library with a monoclonal antibody (mAb 4C12) recognizing an epitope present in high-molecular-weight mannoprotein (HMWM) components specific for the mycelial cell walls (a 180 kDa component and a polydispersed 260 kDa species) resulted in the isolation of the gene CaCYC3 encoding for cytochrome c haem lyase (CCHL). The CaCYC3 gene was transcribed preferentially in mycelial cells in which two mRNA transcripts of 0.8 and 1 kb were found. The nucleotide and the deduced amino acid sequences of this gene displayed 45% homology and 46% identity, respectively, to the Saccharomyces cerevisiae CYC3 gene and shared common features with other reported genes …

Saccharomyces cerevisiaeBlotting WesternGenes FungalMolecular Sequence DataFluorescent Antibody TechniqueLyasesSaccharomyces cerevisiaeMolecular cloningMicrobiologyHomology (biology)Fungal ProteinsCell WallImmunoscreeningSequence Homology Nucleic AcidCandida albicansAmino Acid SequenceRNA MessengerCloning MolecularCandida albicansMolecular BiologyGeneMembrane GlycoproteinsbiologyBase SequencecDNA libraryRNA FungalSequence Analysis DNALyasebiology.organism_classificationBlotting NorthernMolecular biologyMitochondriaBiochemistrySequence AlignmentMolecular microbiology
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A natural A/T-rich sequence from the yeast FBP1 gene exists as a cruciform in Escherichia coli cells.

1993

Abstract Palindromic or semipalindromic sequences can adopt cruciform structures in DNA in vitro. It has been demonstrated in some cases that A/T-rich cruciforms exist also in vivo in Escherichia coli. The biological function of those structures is not understood although putative cruciforms have been found in interesting locations on replication origins, operators, or transcriptional termination regions. Here we show by means of the use of structure-dependent nucleases that the 3′ end of the yeast FBP1 gene contains a stable cruciform both in vitro and in E. coli cells and that in both cases, its extrusion depends on the DNA supercoiling state.

Saccharomyces cerevisiaeGenes FungalMolecular Sequence DataDNA RecombinantSaccharomyces cerevisiaeOrigin of replicationmedicine.disease_causechemistry.chemical_compoundmedicineEscherichia coliMolecular BiologyGeneEscherichia coliPalindromic sequenceGeneticsEndodeoxyribonucleasesbiologyBase SequenceDNA Superhelicalbiology.organism_classificationCell biologychemistryCruciformDNA supercoilNucleic Acid ConformationDNAPlasmid
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Salinity and Bacterial Diversity: To What Extent Does the Concentration of Salt Affect the Bacterial Community in a Saline Soil?

2014

In this study, the evaluation of soil characteristics was coupled with a pyrosequencing analysis of the V2-V3 16S rRNA gene region in order to investigate the bacterial community structure and diversity in the A horizon of a natural saline soil located in Sicily (Italy). The main aim of the research was to assess the organisation and diversity of microbial taxa using a spatial scale that revealed physical and chemical heterogeneity of the habitat under investigation. The results provided information on the type of distribution of different bacterial groups as a function of spatial gradients of soil salinity and pH. The analysis of bacterial 16S rRNA showed differences in bacterial compositi…

SalinitySoil salinitylcsh:MedicineSoil ScienceBiologyMicrobiologyEcosystemsMicrobial EcologyCoastal EcosystemsBacteria; Phylogeny; RNA Ribosomal 16S; Salinity; Salts; Soil MicrobiologyRNA Ribosomal 16SBacteria Community ecology Community structure DNA sequence analysis Soil Salinity Sequence databasesSoil ecologylcsh:ScienceMolecular BiologyPhylogenySoil MicrobiologyMultidisciplinaryCommunityBacteriaEcologyEcologylcsh:REcology and Environmental SciencesCommunity structureSoil chemistryBiology and Life SciencesBiodiversitySoil EcologySalinitySettore AGR/14 - PedologiaSoil horizonlcsh:QSpatial variabilitySaltsCoastal EcologyResearch Article
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Sulfur cycling and methanogenesis primarily drive microbial colonization of the highly sulfidic Urania deep hypersaline basin

2009

Urania basin in the deep Mediterranean Sea houses a lake that is >100 m deep, devoid of oxygen, 6 times more saline than seawater, and has very high levels of methane and particularly sulfide (up to 16 mM), making it among the most sulfidic water bodies on Earth. Along the depth profile there are 2 chemoclines, a steep one with the overlying oxic seawater, and another between anoxic brines of different density, where gradients of salinity, electron donors and acceptors occur. To identify and differentiate the microbes and processes contributing to the turnover of organic matter and sulfide along the water column, these chemoclines were sampled at a high resolution. Bacterial cell numbers…

SalinitySulfideMethanogenesisMolecular Sequence Datageosphere-biosphere interactionchemistry.chemical_elementGEO/01 - PALEONTOLOGIA E PALEOECOLOGIA03 medical and health sciencesWater columnelement cyclingMediterranean SeaSeawater14. Life underwaterEcosystemComputingMilieux_MISCELLANEOUS030304 developmental biology2. Zero hungerchemistry.chemical_classification[SDU.OCEAN]Sciences of the Universe [physics]/Ocean AtmosphereManganese0303 health sciencesNitratesMultidisciplinaryBacteriabiology030306 microbiologyEcologyWaterdeep anoxic hypersaline lake15. Life on landbiology.organism_classificationArchaeaSulfurAnoxic waters6. Clean waterOxygenRedox gradientchemistryDeep anoxic hypersaline lake; Element cycling; Geosphere-biosphere interaction; Mediterranean Sea; Microbial diversityEnvironmental chemistrymicrobial diversityPhysical SciencesSeawaterdeep anoxic hypersaline lake element cycling geosphere–biosphere interaction Mediterranean Sea microbial diversitySulfurArchaea
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Centromeric heterochromatin and satellite DNA in the Chironomus plumosus species group

1994

Species of the Chironomus plumosus group display significant differences in their amount of centromeric heterochromatin. A tandem-repetitive satellite-like DNA has been isolated from C. plumosus. This DNA accounts for a major part of the centromeric heterochromatin. The DNA element has a Sau3AI restriction site ("Sau elements") and a monomer length of 165 or 166 bp. It is A-T rich (73%) and reveals a moderate DNA curvature, as shown by gel migration and computer analysis. The chromosomal localization and genomic organization of Sau elements were studied in 24 Chironomus species by in situ hybridization and (or) Southern analysis. The DNA is predominantly located in the centromeric regions …

Satellite DNACentromereMolecular Sequence DataIn situ hybridizationDNA SatelliteChironomidaechemistry.chemical_compoundSpecies SpecificityHeterochromatinCentromereGeneticsAnimalsChironomus plumosusCloning MolecularDeoxyribonucleases Type II Site-SpecificMolecular BiologyIn Situ HybridizationPhylogenyGenomic organizationGeneticsBase SequencebiologySequence Analysis DNAGeneral Medicinebiology.organism_classificationMolecular biologyRestriction sitechemistryNucleic Acid ConformationChironomusDNABiotechnologyGenome
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Phosphorylation of the Usher syndrome 1G protein SANS controls Magi2-mediated endocytosis.

2014

Item does not contain fulltext The human Usher syndrome (USH) is a complex ciliopathy with at least 12 chromosomal loci assigned to three clinical subtypes, USH1-3. The heterogeneous USH proteins are organized into protein networks. Here, we identified Magi2 (membrane-associated guanylate kinase inverted-2) as a new component of the USH protein interactome, binding to the multifunctional scaffold protein SANS (USH1G). We showed that the SANS-Magi2 complex assembly is regulated by the phosphorylation of an internal PDZ-binding motif in the sterile alpha motif domain of SANS by the protein kinase CK2. We affirmed Magi2's role in receptor-mediated, clathrin-dependent endocytosis and showed tha…

Scaffold proteinGuanylate kinaseMolecular Sequence DataPrimary Cell CultureNerve Tissue ProteinsBiologyEndocytosisPhotoreceptor cellExocytosisMiceCiliogenesisGeneticsmedicineAnimalsHumansProtein Interaction Domains and MotifsAmino Acid SequencePhosphorylationRNA Small InterferingSensory disorders Radboud Institute for Molecular Life Sciences [Radboudumc 12]Molecular BiologyGenetics (clinical)Adaptor Proteins Signal TransducingBinding SitesGeneral MedicineClathrinEndocytosisCell biologyMice Inbred C57BLRenal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]medicine.anatomical_structureHEK293 CellsGene Expression RegulationCiliary pocketCarrier ProteinsSterile alpha motifGuanylate KinasesSequence AlignmentUsher SyndromesPhotoreceptor Cells VertebrateProtein BindingSignal TransductionHuman molecular genetics
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Isolation of the silicatein-α interactor silintaphin-2 by a novel solid-phase pull-down assay.

2011

The skeleton of siliceous sponges consists of amorphous biogenous silica (biosilica). Biosilica formation is driven enzymatically by means of silicatein(s). During this unique process of enzymatic polycondensation, skeletal elements (spicules) that enfold a central proteinaceous structure (axial filament), mainly comprising silicatein, are formed. However, only the concerted action of silicatein and other proteins can explain the genetically controlled diversity of spicular morphotypes, from simple rods with pointed ends to intricate structures with up to six rays. With the scaffold protein silintaphin-1, a first silicatein interactor that facilitates the formation of the axial filament and…

Scaffold proteinSpiculeImmunoprecipitationMolecular Sequence DataNanotechnologyBiologyFlagellumBiochemistry03 medical and health sciencesSponge spiculePhase (matter)Two-Hybrid System TechniquesProtein Interaction MappingAnimalsInteractorAmino Acid Sequence030304 developmental biology0303 health sciences030302 biochemistry & molecular biologySilicon DioxideCathepsinsYeastProtein TransportSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationBiophysicsAutoradiographyCalciumSuberitesProtein BindingBiochemistry
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MPP1 links the Usher protein network and the Crumbs protein complex in the retina.

2007

Contains fulltext : 53571.pdf (Publisher’s version ) (Closed access) The highly ordered distribution of neurons is an essential feature of a functional mammalian retina. Disruptions in the apico-basal polarity complexes at the outer limiting membrane (OLM) of the retina are associated with retinal patterning defects in vertebrates. We have analyzed the binding repertoire of MPP5/Pals1, a key member of the apico-basal Crumbs polarity complex, that has functionally conserved counterparts in zebrafish (nagie oko) and Drosophila (Stardust). We show that MPP5 interacts with its MAGUK family member MPP1/p55 at the OLM. Mechanistically, this interaction involves heterodimerization of both MAGUK mo…

Scaffold proteinanimal structuresGenetics and epigenetic pathways of disease [NCMLS 6]BioinformaticsPDZ domainMolecular Sequence DataMice TransgenicNerve Tissue ProteinsNeuroinformatics [DCN 3]Models BiologicalRetinaMiceTwo-Hybrid System TechniquesCell polarityPerception and Action [DCN 1]GeneticsNeurosensory disorders [UMCN 3.3]Basal bodyAnimalsHumansAmino Acid SequenceRats WistarEye ProteinsMolecular BiologyZebrafishGenetics (clinical)ActinRenal disorder [IGMD 9]GeneticsExtracellular Matrix ProteinsBinding SitesbiologyModels GeneticCell MembraneMembrane ProteinsGeneral MedicineBlood Proteinsbiology.organism_classificationEmbryo MammalianCell biologyProtein Structure TertiaryRatsGenetic defects of metabolism [UMCN 5.1]Eye disordersense organsCellular energy metabolism [UMCN 5.3]Nucleoside-Phosphate KinaseFunctional Neurogenomics [DCN 2]Neural developmentHuman Molecular Genetics
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Cystic Fibrosis Transmembrane Conductance Regulator Interacts with Multiple Immunoglobulin Domains of Filamin A

2010

Mutations of the chloride channel cystic fibrosis transmembrane conductance regulator (CFTR) that impair its apical localization and function cause cystic fibrosis. A previous report has shown that filamin A (FLNa), an actin-cross-linking and -scaffolding protein, interacts directly with the cytoplasmic N terminus of CFTR and that this interaction is necessary for stability and confinement of the channel to apical membranes. Here, we report that the CFTR N terminus has sequence similarity to known FLNa-binding partner-binding sites. FLNa has 24 Ig (IgFLNa) repeats, and a CFTR peptide pulled down repeats 9, 12, 17, 19, 21, and 23, which share sequence similarity yet differ from the other FLN…

Scaffold proteincongenital hereditary and neonatal diseases and abnormalitiesFilaminsMolecular Sequence DataCystic Fibrosis Transmembrane Conductance RegulatorImmunoglobulinsBiologymedicine.disease_causeFilaminBiochemistryContractile ProteinsProtein structureCricetinaemedicineAnimalsHumansFLNAAmino Acid SequenceMolecular BiologyPeptide sequenceMutationSequence Homology Amino AcidCell MembraneMicrofilament ProteinsCell Biologyrespiratory systemMolecular biologyActinsCystic fibrosis transmembrane conductance regulatorProtein Structure Tertiaryrespiratory tract diseasesCell biologySolubilityMutationProtein Structure and FoldingChloride channelbiology.proteinPeptidesDimerizationProtein BindingJournal of Biological Chemistry
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