Deoxyribonucleic acid isolated from bacteriophage lambda can infect Escherichia coli K12 in the presence of adsorbed helper phage (Kaiser and Hogness, 1960; Kaiser, 1962). The manner in which lambda DNA enters the cell and the possible role of helper phage in the penetration process is still not clear. Kinetic studies conducted in this laboratory during the initial stages of infection by lambda DNA demonstrate a requirement for helper function during the penetration of an infectious molecule. Further investigation into this problem is needed and was the major objective of this study.

Staphylococcus aureus pathogenicity island SaPI1 is a genomic element that is mobilized and transduced at high frequency by helper phage 80α. SaPI1 encodes a small terminase protein that belongs to the phage small terminase subunit family. The presence of SaPI1-encoded small terminase suggests that it plays a role in SaPI1-specific packaging into transducing particles by complexing with the 80α large terminase subunit and redirecting recognition to a pac site on SaPI1 DNA from 80α DNA. The effects of deleting the small terminase genes in SaPI1 and in a prophage copy of 80α are consistent with this hypothesis. Induction of the 80α small terminase deletion mutant produces wild type levels of SaPI1 transducing particles, demonstrating that SaPI1 small terminase can replace that of 80a in SaPI1 packaging. Southern blot analysis of virion DNAs isolated from the deletion mutants confirms that SaPI1 redirects packaging of its DNA into SaPI1-sized capsids.