Search results for "Cell Nucleus"

showing 9 items of 379 documents

Molecular Effects of the CTG Repeats in Mutant Dystrophia Myotonica Protein Kinase Gene

2008

Myotonic Dystrophy type 1 (DM1) is a multi-system disorder characterized by muscle wasting, myotonia, cardiac conduction defects, cataracts, and neuropsychological dysfunction. DM1 is caused by expansion of a CTG repeat in the 3 untranslated region (UTR) of the Dystrophia Myotonica Protein Kinase (DMPK) gene. A body of work demonstrates that DMPK mRNAs containing abnormally expanded CUG repeats are toxic to several cell types. A core mechanism underlying symptoms of DM1 is that mutant DMPK RNA interferes with the developmentally regulated alternative splicing of defined pre-mRNAs. Expanded CUG repeats fold into ds(CUG) hairpins that sequester nuclear proteins including human Muscleblind-lik…

musculoskeletal diseasescongenital hereditary and neonatal diseases and abnormalitiesThree prime untranslated regionAlternative splicingBiologyMolecular biologyArticleExonchemistry.chemical_compoundCell nucleusmedicine.anatomical_structurechemistryGene expressionGeneticsmedicineGene silencingMBNL1Nuclear proteinGenetics (clinical)Current Genomics
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Early evolutionary colocalization of the nuclear ribosomal 5S and 45S gene families in seed plants: evidence from the living fossil gymnosperm Ginkgo…

2012

In seed plants, the colocalization of the 5S loci within the intergenic spacer (IGS) of the nuclear 45S tandem units is restricted to the phylogenetically derived Asteraceae family. However, fluorescent in situ hybridization (FISH) colocalization of both multigene families has also been observed in other unrelated seed plant lineages. Previous work has identified colocalization of 45S and 5S loci in Ginkgo biloba using FISH, but these observations have not been confirmed recently by sequencing a 1.8 kb IGS. In this work, we report the presence of the 45S–5S linkage in G. biloba, suggesting that in seed plants the molecular events leading to the restructuring of the ribosomal loci are much o…

phylogenetic relictDNA PlantPseudogeneMolecular Sequence Dataintergenic spacerrDNAEvolution MolecularGymnospermTranscription (biology)GeneticsGene family45S–5S unitGeneGenetics (clinical)In Situ Hybridization FluorescenceGeneticsCell NucleusbiologyFossilsGinkgoRNA Ribosomal 5SColocalizationChromosome MappingGinkgo bilobaGenes rRNARibosomal RNAbiology.organism_classificationribosomal pseudogenes gymnospermSeedsOriginal Article
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Infection-induced chromatin modifications facilitate translocation of herpes simplex virus capsids to the inner nuclear membrane

2021

Herpes simplex virus capsids are assembled and packaged in the nucleus and move by diffusion through the nucleoplasm to the nuclear envelope for egress. Analyzing their motion provides conclusions not only on capsid transport but also on the properties of the nuclear environment during infection. We utilized live-cell imaging and single-particle tracking to characterize capsid motion relative to the host chromatin. The data indicate that as the chromatin was marginalized toward the nuclear envelope it presented a restrictive barrier to the capsids. However, later in infection this barrier became more permissive and the probability of capsids to enter the chromatin increased. Thus, although …

virusesGene ExpressionVirus ReplicationPathology and Laboratory Medicineherpes simplex -virusChlorocebus aethiopsCapsidsMedicine and Health SciencesSimplexvirusBiology (General)Mass DiffusivityStainingChromosome BiologyPhysicsChromatinChemistryMedical MicrobiologyViral PathogensPhysical SciencesVirusesHerpes Simplex Virus-1EpigeneticsCellular Structures and OrganellesPathogenskapsidiResearch ArticleHerpesvirusesNuclear EnvelopeQH301-705.5Biological Transport ActiveViral StructureResearch and Analysis MethodsinfektiotMicrobiologydiffuusio (fysikaaliset ilmiöt)CapsidNuclear MembraneVirologyGeneticsAnimalsherpesviruksetVero CellsMicrobial PathogensCell NucleusChemical PhysicsOrganismsBiology and Life SciencesHerpes SimplexCell Biologybiochemical phenomena metabolism and nutritionRC581-607Viral ReplicationHerpes Simplex VirusNuclear StainingSpecimen Preparation and TreatmentImmunologic diseases. AllergyDNA viruses
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Assembly and Translocation of Papillomavirus Capsid Proteins

2002

ABSTRACT The major and minor capsid proteins of polyomavirus are preassembled in the cytoplasm and translocated to the nucleus only as a VP1-VP2/VP3 complex. In this study, we describe independent nuclear translocation of the L1 major protein and the L2 minor capsid protein of human papillomavirus type 33 by several approaches. First, we observed that expression and nuclear translocation of L2 in natural lesions precede expression of L1. Second, using a cell culture system for coexpression, we found that accumulation of L2 in nuclear domain 10 (ND10) subnuclear structures precedes L1 by several hours. In contrast, complexes of L2 and mutants of L1 forced to assemble in the cytoplasm are tra…

virusesImmunologyActive Transport Cell NucleusChromosomal translocationBiologyMicrobiologychemistry.chemical_compoundCapsidVirologyMG132medicineAnimalsHumansPapillomaviridaeCOS cellsStructure and AssemblyVirus AssemblyOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologymedicine.anatomical_structureCapsidchemistryCytoplasmCell cultureInsect ScienceCOS CellsProteasome inhibitorCapsid ProteinsFemaleNucleusmedicine.drug
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Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles.

2004

ABSTRACT Recent reports suggest that nuclear domain(s) 10 (ND10) is the site of papillomavirus morphogenesis. The viral genome replicates in or close to ND10. In addition, the minor capsid protein, L2, accumulates in these subnuclear structures and recruits the major capsid protein, L1. We have now used cell lines deficient for promyelocytic leukemia (PML) protein, the main structural component of ND10, to study the role of this nuclear protein for L2 incorporation into virus-like particles (VLPs). L2 expressed in PML protein knockout (PML −/− ) cells accumulated in nuclear dots, which resemble L2 aggregates forming at ND10 in PML protein-containing cells. These L2 assemblies also attracted…

virusesImmunologyActive Transport Cell NucleusNuclear dotsBiologyPromyelocytic Leukemia ProteinMicrobiologyCell LinePromyelocytic leukemia proteinMiceDeath-associated protein 6Virus-like particleVirologymedicineAnimalsHumansNuclear proteinPapillomaviridaeAdaptor Proteins Signal TransducingCell NucleusTumor Suppressor ProteinsStructure and AssemblyIntracellular Signaling Peptides and ProteinsVirionvirus diseasesNuclear ProteinsOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologyCell biologyNeoplasm ProteinsCell nucleusMicroscopy Electronmedicine.anatomical_structureInsect ScienceMutationbiology.proteinCapsid ProteinsNuclear transportCarrier ProteinsCo-Repressor ProteinsNuclear localization sequenceMolecular ChaperonesTranscription FactorsJournal of virology
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Translocation of the nuclear autoantigen La to the cell surface of herpes simplex virus type 1 infected cells.

1992

Recently we developed a procedure to translocalize one of the extractable nuclear antigens (ENAs), the La protein, to the cell surface of CV-1 cells. Here we report that herpes simplex virus type 1 infection can also induce a translocation of the autoantigen to the cell surface. On the cell surface we detected La protein assembled with large protrusions. Within these protrusions La protein colocalized with virus particles. These protrusions are known to be released from the cell after virus infections. Such complexes consisting of self and virus could provide helper determinants for an anti-self response, and therefore be important in generation of autoimmunity.

virusesImmunologyCellmedicine.disease_causeAutoantigensVirusHerpesviridaeSingle-stranded binding proteinAntigenAlphaherpesvirinaeCricetinaemedicineImmunology and AllergyAnimalsNuclear proteinCells CulturedCell NucleusbiologyAntibodies MonoclonalBiological TransportHerpes Simplexbiology.organism_classificationBlood Physiological PhenomenaVirologymedicine.anatomical_structureHerpes simplex virusRibonucleoproteinsbiology.proteinAutoimmunity
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Baculovirus-mediated immediate-early gene expression and nuclear reorganization in human cells

2007

Baculovirus, Autographa californica multiple nucleopolyhedrovirus (AcMNPV), has the ability to transduce mammalian cell lines without replication. The general objective of this study was to detect the transcription and expression of viral immediate-early genes in human cells and to examine the interactions between viral components and subnuclear structures. Viral capsids were seen in large, discrete foci in nuclei of both dividing and non-dividing human cells. Concurrently, the transcription of viral immediate-early transregulator genes (ie-1, ie-2) and translation of IE-2 protein were detected. Quantitative microscopy imaging and analysis showed that virus transduction altered the size of …

virusesImmunologyGene ExpressionAnthraquinonesMicrobiologyCell LineHistonesMiceViral ProteinsTransduction (genetics)CapsidViral entryTranscription (biology)VirologyAnimalsHumansInsect virusGenes Immediate-EarlyGeneCell NucleusMicroscopy ConfocalbiologyChromatin Assembly and DisassemblyMolecular biologyNucleopolyhedrovirusesChromatinHistoneMicroscopy Fluorescencebiology.proteinImmediate early geneCellular Microbiology
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Impact of VP1-Specific Protein Sequence Motifs on Adeno-Associated Virus Type 2 Intracellular Trafficking and Nuclear Entry

2012

ABSTRACT Adeno-associated virus type 2 (AAV2) has gained much interest as a gene delivery vector. A hallmark of AAV2-mediated gene transfer is an intracellular conformational change of the virus capsid, leading to the exposure of infection-relevant protein domains. These protein domains, which are located on the N-terminal portion of the structural proteins VP1 and VP2, include a catalytic phospholipase A 2 domain and three clusters of basic amino acids. We have identified additional protein sequence motifs located on the VP1/2 N terminus that also proved to be obligatory for virus infectivity. These motifs include signals that are known to be involved in protein interaction, endosomal sort…

virusesImmunologyProtein domainAmino Acid MotifsMolecular Sequence DataSequence alignmentBiologyMicrobiologyVirusCell LineParvoviridae InfectionsVirologyHumansAmino Acid SequenceAdeno-Associated Virus Type 2Peptide sequenceCell NucleusDependovirusMolecular biologyTransport proteinCell biologyVirus-Cell InteractionsProtein TransportCapsidInsect ScienceCapsid ProteinsSequence motifSequence Alignment
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Quantitative microscopy reveals stepwise alteration of chromatin structure during herpesvirus infection

2019

During lytic herpes simplex virus 1 (HSV-1) infection, the expansion of the viral replication compartments leads to an enrichment of the host chromatin in the peripheral nucleoplasm. We have shown previously that HSV-1 infection induces the formation of channels through the compacted peripheral chromatin. Here, we used three-dimensional confocal and expansion microscopy, soft X-ray tomography, electron microscopy, and random walk simulations to analyze the kinetics of host chromatin redistribution and capsid localization relative to their egress site at the nuclear envelope. Our data demonstrated a gradual increase in chromatin marginalization, and the kinetics of chromatin smoothening arou…

viruseslcsh:QR1-502Herpesvirus 1 HumanmikroskopiaVirus ReplicationinfektiotElectronMicrobiologylcsh:MicrobiologyArticleFluorescenceCell LineBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biologyherpes simplex -virustumaChlorocebus aethiopsAnimalsHumansherpesviruksetVero CellsTomographyVirus ReleaseCell NucleusMicroscopyTomography X-RayHerpesvirus 1nuclear egressHerpesviridae InfectionsHSV-1ChromatinMicroscopy ElectronInfectious DiseasesMicroscopy FluorescencetumaegressKasvibiologia mikrobiologia virologia - Plant biology microbiology virologyX-RaykromatiiniSexually Transmitted InfectionschromatinInfectionHuman
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