The major capsid protein of the lipid-containing bacteriophage PR4 is the precursor of two other capsid proteins.

We report that capsid proteins P16 and P18 of bacteriophage PR4 are synthesized by post-translational processing of a portion of the major capsid protein, P2. A polyclonal antibody raised against purified P2 reacted with P16 and P18 as well as with P2. A monoclonal antibody reacted with both P2 and P18. The amino acid sequences of the N-termini of P2 and P18 exactly matched, indicating that P18 is derived from the N-terminal segment of P2. These data were confirmed by the analysis of the proteins encoded by various nonsense and missense P2 mutants. The 3129-bp MnlI-C fragment of the PR4 genome was shown to encode P2. The nucleotide sequence of this fragment was obtained and a single continuous ORF was found to encode P2, thus excluding introns and transcript processing in the production of P16 and P18. The DNA segment contained eight ORFs sized > 200 bp and the genes encoding proteins P6 and P6A as well as P2 were mapped by marker rescue analysis. We also report the isolation and characterization of a new class of P2 missense mutants.