title: Assembly of membrane-containing bacteriophage PRD1 is dependent on GroEL and GroES.
abstract: Assembly of the broad-host-range bacteriophage PRD1 involves translocation of the virus-specific membrane to the inside of the icosahedral protein shell formed of trimeric coat proteins. The formation of PRD1 particles is, in addition to the virus-encoded assembly factors P10 and P17, dependent on GroEL/GroES chaperonins. The chaperonins assist in the folding of the capsid proteins P3 and P5 and in the assembly of viral membrane proteins.
authors.affiliation: Division of Genetics, University of Helsinki, 00014, Finland.
authors.forename: A L
authors.initials: AL
authors.lastname: Hänninen
authors.forename: D H
authors.initials: DH
authors.lastname: Bamford
authors.forename: J K
authors.initials: JK
authors.lastname: Bamford
mesh_terms: D018835:Chaperonin 10 / Q000502:physiology*; D018834:Chaperonin 60 / Q000502:physiology*; D004926:Escherichia coli / Q000235:genetics / Q000821:virology; D009154:Mutation; D017510:Protein Folding; D017916:Tectiviridae / Q000502:physiology*; D014764:Viral Proteins / Q000378:metabolism; D019065:Virus Assembly
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D014764:Viral Proteins