Search results for " assembly"

showing 10 items of 289 documents

Conserved chromosomal clustering of genes governed by chromatin regulators in Drosophila

2008

Transcriptional analysis of chromatin regulator mutants in Drosophila melanogaster identified clusters of functionally related genes conserved in other insect species.

Model organismsanimal structuresTranscription GeneticEvolutionChromosomal Proteins Non-HistoneDrosòfila melanogasterGenome studiesDevelopmentBiologyNon-histone proteinAnimalsDrosophila ProteinsDrosòfila -- GenèticaTranscription factorGeneGeneticsMicroarray analysis techniquesResearchGene Expression ProfilingMutació (Biologia)fungiNuclear Proteinsbiology.organism_classificationChromatin Assembly and DisassemblyChromatinHistoneDrosophila melanogasterDrosofila melanogasterGene Expression RegulationMultigene Familybiology.proteinDrosophila melanogasterDrosophila ProteinGenètica del desenvolupamentTranscription FactorsGenome Biology
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Effective stiffening of DNA due to nematic ordering causes DNA molecules packed in phage capsids to preferentially form torus knots.

2012

Observation that DNA molecules in bacteriophage capsids preferentially form torus type of knots provided a sensitive gauge to evaluate various models of DNA arrangement in phage heads. Only models resulting in a preponderance of torus knots could be considered as close to reality. Recent studies revealed that experimentally observed enrichment of torus knots can be qualitatively reproduced in numerical simulations that include a potential inducing nematic arrangement of tightly packed DNA molecules within phage capsids. Here, we investigate what aspects of the nematic arrangement are crucial for inducing formation of torus knots. Our results indicate that the effective stiffening of DNA by …

Models MolecularBacteriophages/genetics; Capsid/chemistry; DNA Viral/chemistry; Models Molecular; Virus AssemblyvirusesBacteriophageQuantitative Biology::Subcellular Processeschemistry.chemical_compoundCapsidstomatognathic systemLiquid crystalStructural BiologyGeneticsMoleculeBacteriophagesDna viralQuantitative Biology::BiomoleculesbiologyVirus Assemblyfood and beveragesTorusbiology.organism_classificationVirologyQuantitative Biology::GenomicsMathematics::Geometric TopologyStiffeningsurgical procedures operativechemistryCapsidDNA ViralBiophysicsDNANucleic acids research
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Molecular and structural characterization of fluorescent human parvovirus B19 virus-like particles

2005

Although sharing a T = 1 icosahedral symmetry with other members of the Parvoviridae family, it has been suggested that the fivefold channel of the human parvovirus B19 VP2 capsids is closed at its outside end. To investigate the possibility of placing a relatively large protein moiety at this site of B19, fluorescent virus-like particles (fVLPs) of B19 were developed. The enhanced green fluorescent protein (EGFP) was inserted at the N-terminus of the structural protein VP2 and assembly of fVLPs from this fusion protein was obtained. Electron microscopy revealed that these fluorescent protein complexes were very similar in size when compared to wild-type B19 virus. Further, fluorescence cor…

Models MolecularImmunoprecipitationRecombinant Fusion ProteinsvirusesGreen Fluorescent ProteinsBiophysicsFluorescence correlation spectroscopyEndosomesSpodopteraBiologyMicroscopy Atomic ForceBiochemistryFluorescenceCell LineGreen fluorescent proteinParvoviridae InfectionsBimolecular fluorescence complementationCell Line Tumorhemic and lymphatic diseasesParvovirus B19 HumanAnimalsHumansImmunoprecipitationMolecular BiologyParvoviridaeImmune SeraVirus AssemblyVirionvirus diseasesCell Biologybiology.organism_classificationFusion proteinMolecular biologyNanostructuresCell biologyTransport proteinProtein TransportCapsidCapsid Proteins
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A Short Caspase-3 Isoform Inhibits Chemotherapy-Induced Apoptosis by Blocking Apoptosome Assembly

2011

Alternative splicing of caspase-3 produces a short isoform caspase-3s that antagonizes caspase-3 apoptotic activity. However, the mechanism of apoptosis inhibition by caspase-3s remains unknown. Here we show that exogenous caspase-3 sensitizes MCF-7 and HBL100 breast cancers cells to chemotherapeutic treatments such as etoposide and methotrexate whereas co-transfection with caspase-3s strongly inhibits etoposide and methotrexate-induced apoptosis underlying thus the anti-apoptotic role of caspase-3s. In caspase-3 transfected cells, lamin-A and α-fodrin were cleaved when caspase-3 was activated by etoposide or methotrexate. When caspase-3s was co-transfected, this cleavage was strongly reduc…

Models MolecularImmunoprecipitationScienceBlotting WesternMolecular Sequence DataGene ExpressionApoptosisBreast NeoplasmsCaspase 3BiologyReal-Time Polymerase Chain ReactionBiochemistryRNA interferenceApoptosomesCell Line TumorMolecular Cell BiologyBreast CancermedicineHumansAmino Acid SequenceBiologyEtoposideDNA PrimersMultidisciplinaryCell DeathBase SequenceSequence Homology Amino AcidCaspase 3QRObstetrics and GynecologyTransfectionApoptosome assemblyMolecular biologyEnzymesEnzyme ActivationIsoenzymesApoptosisCancer researchMedicineApoptosomeResearch Articlemedicine.drugPLoS ONE
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Sizzled Is Unique among Secreted Frizzled-related Proteins for Its Ability to Specifically Inhibit Bone Morphogenetic Protein-1 (BMP-1)/Tolloid-like …

2012

BMP-1/tolloid-like proteinases (BTPs) are major enzymes involved in extracellular matrix assembly and activation of bioactive molecules, both growth factors and anti-angiogenic molecules. Although the control of BTP activity by several enhancing molecules is well established, the possibility that regulation also occurs through endogenous inhibitors is still debated. Secreted frizzled-related proteins (sFRPs) have been studied as possible candidates, with highly contradictory results, after the demonstration that sizzled, a sFRP found in Xenopus and zebrafish, was a potent inhibitor of Xenopus and zebrafish tolloid-like proteases. In this study, we demonstrate that mammalian sFRP-1, -2, and …

Models MolecularProteasesFrizzledanimal structuresMolecular Sequence DataXenopusXenopus ProteinsBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 1MiceXenopus laevismedicineAnimalsHumansProtease InhibitorsAmino Acid SequenceMolecular BiologyZebrafishGlycoproteinsSequence Homology Amino AcidbiologyExtracellular matrix assemblyfungiIntracellular Signaling Peptides and ProteinsTissue Inhibitor of MetalloproteinasesCell BiologySurface Plasmon Resonancebiology.organism_classificationMatrix MetalloproteinasesRecombinant ProteinsExtracellular MatrixWnt ProteinsBiochemistryMechanism of actionembryonic structuresEnzymologySignal transductionmedicine.symptomPeptide HydrolasesSignal TransductionJournal of Biological Chemistry
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Bacteriophage P23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage.

2013

Summary It has proved difficult to classify viruses unless they are closely related since their rapid evolution hinders detection of remote evolutionary relationships in their genetic sequences. However, structure varies more slowly than sequence, allowing deeper evolutionary relationships to be detected. Bacteriophage P23-77 is an example of a newly identified viral lineage, with members inhabiting extreme environments. We have solved multiple crystal structures of the major capsid proteins VP16 and VP17 of bacteriophage P23-77. They fit the 14 Å resolution cryo-electron microscopy reconstruction of the entire virus exquisitely well, allowing us to propose a model for both the capsid archi…

Models MolecularProtein ConformationViral proteinLineage (evolution)virusesCrystallography X-Raymedicine.disease_causeArticleVirusViral AssemblyBacteriophage03 medical and health sciencesProtein structureStructural BiologymedicineBacteriophagesMolecular Biology030304 developmental biologySequence (medicine)0303 health sciencesbiology030306 microbiologyCryoelectron Microscopyta1183ta1182biology.organism_classificationVirology3. Good healthCapsidEvolutionary biologyCapsid ProteinsCrystallizationStructure (London, England : 1993)
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Identification of SNARE complex modulators that inhibit exocytosis from an alpha-helix-constrained combinatorial library.

2003

Synthetic peptides patterned after the proteins involved in vesicle fusion [the so-called SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) proteins] are potent inhibitors of SNARE complex assembly and neuronal exocytosis. It is noteworthy that the identification of peptide sequences not related to the SNARE proteins has not been accomplished yet; this is due, in part, to the structural constraints and the specificity of the protein interactions that govern the formation of the SNARE complex. Here we have addressed this question and used a combinatorial approach to identify peptides that modulate the assembly of the SNARE core complex and inhibit neuronal…

Models MolecularVesicle fusionMacromolecular SubstancesChromaffin CellsMolecular Sequence DataVesicular Transport ProteinsBiologyBiochemistryExocytosisExocytosisProtein Structure SecondaryPeptide LibraryAnimalsAmino Acid SequencePeptide libraryMolecular BiologyCells CulturedSNARE complex assemblyNeuronsSTX1AMembrane ProteinsMunc-18Cell BiologyFusion proteinCell biologyRatsCattleSNARE complexPeptidesSNARE ProteinsResearch ArticleThe Biochemical journal
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The Minor Capsid Protein VP11 of Thermophilic Bacteriophage P23-77 Facilitates Virus Assembly by Using Lipid-Protein Interactions

2015

ABSTRACT Thermus thermophilus bacteriophage P23-77 is the type member of a new virus family of icosahedral, tailless, inner-membrane-containing double-stranded DNA (dsDNA) viruses infecting thermophilic bacteria and halophilic archaea. The viruses have a unique capsid architecture consisting of two major capsid proteins assembled in various building blocks. We analyzed the function of the minor capsid protein VP11, which is the third known capsid component in bacteriophage P23-77. Our findings show that VP11 is a dynamically elongated dimer with a predominantly α-helical secondary structure and high thermal stability. The high proportion of basic amino acids in the protein enables electrost…

Models MolecularvirusesMolecular Sequence DataStatic ElectricityImmunologyMicrobiologyProtein–protein interactionBacteriophagechemistry.chemical_compoundCapsidVirologyBacteriophagesAmino Acid SequenceThermusPeptide sequenceProtein secondary structureprotein-lipid systemsbiologyVirus AssemblyStructure and AssemblyCapsomereVirionThermus thermophilusLipid Metabolismbiology.organism_classificationLipidsMolecular biologychemistryCapsidInsect Sciencethermophilic virusesBiophysicsCapsid ProteinsDNAkapsidiJournal of Virology
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The Modular X- and Gamma-Ray Sensor (MXGS)of the ASIM Payload on the International Space Station

2019

The Modular X- and Gamma-ray Sensor (MXGS) is an imaging and spectral X- and Gamma-ray instrument mounted on the starboard side of the Columbus module on the International Space Station. Together with the Modular Multi-Spectral Imaging Assembly (MMIA) (Chanrion et al. this issue) MXGS constitutes the instruments of the Atmosphere-Space Interactions Monitor (ASIM) (Neubert et al. this issue). The main objectives of MXGS are to image and measure the spectrum of X- and γ-rays from lightning discharges, known as Terrestrial Gamma-ray Flashes (TGFs), and for MMIA to image and perform high speed photometry of Transient Luminous Events (TLEs) and lightning discharges. With these two instruments sp…

Modular Multi-Spectral Imaging AssemblyPhysics - Instrumentation and Detectors010504 meteorology & atmospheric sciencesModular X- and Gamma-ray SensorFOS: Physical sciencesTerrestrial Gamma-ray FlashesInternational Space Station01 natural sciencesPhysics - Space Physics0103 physical sciencesInternational Space Station010303 astronomy & astrophysicsInstrumentation and Methods for Astrophysics (astro-ph.IM)Atmosphere-Space Interaction Monitor0105 earth and related environmental sciencesRemote sensingPhysicsbusiness.industryPayloadGamma rayX- and Gamma-ray detector for spaceAstronomy and AstrophysicsInstrumentation and Detectors (physics.ins-det)Modular designLightningSpace Physics (physics.space-ph)Photometry (astronomy)Space and Planetary ScienceTransient (oscillation)Astrophysics - Instrumentation and Methods for Astrophysicsbusiness
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Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone.

1997

Abstract Histones are thought to play a key role in regulating gene expression at the level of DNA packaging. Recent evidence suggests that transcriptional activation requires competition of transcription factors with histones for binding to regulatory regions and that there may be several mechanisms by which this is achieved. We have characterized a human nucleosome assembly protein, NAP-2, previously identified by positional cloning at 11p15.5, a region implicated in several disease processes including Wilms tumor (WT) etiology. The deduced amino acid sequence of NAP-2 indicates that it encodes a protein with a potential nuclear localization motif and two clusters of highly acidic residue…

NAP1L4DNA ComplementaryNucleosome assemblyPositional cloningMolecular Sequence DataMice NudeWilms TumorHistonesMicemental disordersGeneticsNucleosomeAnimalsHumansAmino Acid SequenceCloning MolecularRegulation of gene expressionbiologyBase Sequencemusculoskeletal neural and ocular physiologyfungiGene Transfer TechniquesNuclear ProteinsMolecular biologyRecombinant ProteinsChromatinCell biologyNucleosomesDNA-Binding ProteinsHistoneChaperone (protein)biology.proteinpsychological phenomena and processesMolecular ChaperonesProtein BindingSubcellular FractionsGenomics
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