title: The N-terminal part of bacteriophage P2 capsid protein is essential for postassembly maturation of P2 and P4 capsids.
abstract: During capsid assembly of bacteriophage P2 and its satellite phage P4, gpN undergoes proteolytic cleavage with the removal of the first 31 amino acids. The truncated protein gpN* is unable to support formation of viable phages in complementation tests. A c-myc antigenic epitope (EQKLISEEDL) exchanged for eleven amino acids in the amino terminal part of gpN results in both proteolytic processing of gpN::c-myc as well as assembly of P2 and P4 procapsid-like structures, but gpN::c-myc failed, like N*, to support the production of infectious P2 and P4 particles.
authors.affiliation: Institute of Biology, University of Oslo, Norway.
authors.forename: K
authors.initials: K
authors.lastname: Bjerve
authors.forename: B H
authors.initials: BH
authors.lastname: Lindqvist
mesh_terms: D017901:Bacteriophage P2 / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D002213:Capsid / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism; D013329:Structure-Activity Relationship; D019065:Virus Assembly
chemical_list: D016271:Proto-Oncogene Proteins c-myc