Protein O of bacteriophage lambda is a short-lived protein which has a
key role in the replication of the phage DNA in Escherichia coli. Her
e we present evidence that lambda O degradation is energy dependent: i
t is impaired by cyanide and alpha-methylglucoside, both of which inhi
bit cellular energy metabolism. Removal of these inhibitors restored t
he degradation of lambda O. Our experiments suggest that limited amoun
ts of cellular energy are sufficient to support lambda O degradation.
In addition, degradation of lambda O protein is prevented by a mutatio
n in the E. coli clpP gene, but not by a mutation in the clpA gene. Th
ese results suggest that the ClpP protease is involved in the energy-d
ependent degradation of the lambda O protein.