Abstract
Using E. coli lysogens carrying heat inducible λ defective in R or S or both R and S genes (called R, S and RS cells respectively), it has been found that induced β-galactosidase synthesis by host continued in S cells beyond the normal time of lysis. S function affected the permeability of host cell membrane. When radioactive labelled host membrane was incubated in vitro with extracts prepared from phage induced R and RS cells, R cell extract solubilized labelled lipid mostly in the undegraded form. This indicated that S gene product may be a lipophilic protein rather than a phospholipase.