Search results for "Membrane virus"

showing 3 items of 3 documents

Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli

2014

Bacteria possess an intricate internal organization resembling that of the eukaryotes. The complexity is especially prominent at the bacterial cell poles, which are also known to be the preferable sites for some bacteriophages to infect. Bacteriophage PRD1 is a well-known model serving as an ideal system to study structures and functions of icosahedral internal membrane-containing viruses. Our aim was to analyze the localization and interactions of individual PRD1 proteins in its native host Escherichia coli. This was accomplished by constructing a vector library for production of fluorescent fusion proteins. Analysis of solubility and multimericity of the fusion proteins, as well as their …

Cancer ResearchViral proteinvirusesIntracellular SpaceBiologymedicine.disease_causeBacterial cell structureProtein–protein interactionViral Proteins03 medical and health sciencesVirologyEscherichia colimedicineBacteriophage PRD1Escherichia coli030304 developmental biology0303 health sciencesBacteria030302 biochemistry & molecular biologyDNA replicationta1182Protein interactionsFusion proteinVirus assemblyCell biologyConfocal microscopyProtein TransportInfectious DiseasesMembrane proteinVirion assemblyMembrane virusVirus Research
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Non-structural proteins P17 and P33 are involved in the assembly of the internal membrane-containing virus PRD1.

2015

AbstractBacteriophage PRD1, which has been studied intensively at the structural and functional levels, still has some gene products with unknown functions and certain aspects of the PRD1 assembly process have remained unsolved. In this study, we demonstrate that the phage-encoded non-structural proteins P17 and P33, either individually or together, complement the defect in a temperature-sensitive GroES mutant of Escherichia coli for host growth and PRD1 propagation. Confocal microscopy of fluorescent fusion proteins revealed co-localisation between P33 and P17 as well as between P33 and the host chaperonin GroEL. A fluorescence recovery after photobleaching assay demonstrated that the diff…

assemblychaperoninvirusesMutantfluorescence recovery after photobleachingViral Nonstructural Proteinsmedicine.disease_causeVirus ReplicationChaperoninHost-Parasite InteractionsBacteriophagebacteriophageVirologymedicineEscherichia colifluorescent proteinBacteriophage PRD1Escherichia colimembrane virusMicroscopy Confocalbiologyprotein localisationVirus Assemblyta1182Fluorescence recovery after photobleachingGroESChaperonin 60biology.organism_classificationFusion proteinGroEL3. Good healthCell biologyVirology
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Subcellular localization of bacteriophage PRD1 proteins in Escherichia coli

2014

Bacteria possess an intricate internal organization resembling that of the eukaryotes. The complexity is especially prominent at the bacterial cell poles, which are also known to be the preferable sites for some bacteriophages to infect. Bacteriophage PRD1 is a well-known model serving as an ideal system to study structures and functions of icosahedral internal membrane-containing viruses. Our aim was to analyze the localization and interactions of individual PRD1 proteins in its native host Escherichia coli. This was accomplished by constructing a vector library for production of fluorescent fusion proteins. Analysis of solubility and multimericity of the fusion proteins, as well as their …

Confocal microscopykonfokaalimikroskopiabakteeriMembrane virusvirusesproteiinien vuorovaikutuksetKalvollinen virusProtein interactionsVirus assemblybakteerit
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