The N-terminal part of bacteriophage P2 capsid protein is essential for postassembly maturation of P2 and P4 capsids.
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.
Bjerve
K
K
Institute of Biology, University of Oslo, Norway.
Lindqvist
B H
BH
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
D016271:Proto-Oncogene Proteins c-myc