6533b82bfe1ef96bd128e21d
RESEARCH PRODUCT
Non-structural proteins P17 and P33 are involved in the assembly of the internal membrane-containing virus PRD1.
Teemu O. IhalainenSari MäntynenHanna M. OksanenJaana K. H. BamfordJenni Karttunensubject
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 biologydescription
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 diffusion of the P33 fluorescent fusion protein was substantially slower in E. coli than theoretically calculated, presumably resulting from intermolecular interactions. Our results indicate that P33 and P17 function in procapsid assembly, possibly in association with the host chaperonin complex GroEL/GroES.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2015-08-01 | Virology |