Abstract
The bacteriophage P22 late operon contains 2 genes whose products are required for cell lysis and 13 genes whose products are involved in the morphogenesis of the phage particle. This operon is under the positive control of the phage gene 23 product and is thought to have a single promoter. The expression of one of these late genes, the scaffolding protein gene, is autogenously modulated independently from the remainder of the late genes. When unassembled, scaffolding protein turns down the rate of synthesis of additional scaffolding protein, and when it is assembled into phage precursor structures, it does not. Experiments presented here show (i) that the mRNA from the scaffolding protein gene is functionally threefold more stable when most of the scaffolding protein is assembled than when it is unassembled and (ii) that no new promoter near the scaffolding protein gene is activated at the high level of synthesis. These data support the model that this autogenous modulation occurs at a posttranscriptional level. We also observed that another message, that of coat protein, appears to become increasingly stable with time after phage infection.