Structure and synthesis of a lipid-containing bacteriophage : VI. The spectrum of cytoplasmic and membrane-associated proteins in Pseudomonas BAL 31 during replication of bacteriophage PM2

Abstract

After infection of Pseudomonas BAL-31 with the lipid-containing bacteriophage PM2, the rate of incorporation of amino acids into membrane-associated polypeptides increases and the incorporation into cytoplasm decreases, when compared to uninfected cells. When examined by SDS-acrylamide gel electrophoresis, at least 13 distinct newly synthesized membrane-associated viral-specific polypeptides can be demonstrated, while only one new polypeptide was observed in the cytoplasmic fraction after infection. Prelabeling experiments indicate that the membrane-associated peptides present in uninfected cells are conserved during infection, and thus the newly synthesized proteins probably do not displace membrane-associated proteins present prior to infection. In the presence of nalidixic acid, which inhibits both cellular and viral DNA synthesis, at least two viral specific membrane-associated polypeptides are not synthesized, and these probably correspond to two of the viral structural proteins.