Energy-dependent degradation of lambda O protein in Escherichia coli.
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. Here we present evidence that lambda O degradation is energy dependent: it is impaired by cyanide and alpha-methylglucoside, both of which inhibit cellular energy metabolism. Removal of these inhibitors restored the degradation of lambda O. Our experiments suggest that limited amounts of cellular energy are sufficient to support lambda O degradation. In addition, degradation of lambda O protein is prevented by a mutation in the E. coli clpP gene, but not by a mutation in the clpA gene. These results suggest that the ClpP protease is involved in the energy-dependent degradation of the lambda O protein.
Bejarano
I
I
Department of Molecular Biology, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Klemes
Y
Y
Schoulaker-Schwarz
R
R
Engelberg-Kulka
H
H
D049069:ATP-Dependent Proteases; D010582:Bacteriophage lambda / Q000378:metabolism*; D004734:Energy Metabolism / Q000187:drug effects; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D006360:Heat-Shock Proteins / Q000235:genetics*; D009154:Mutation; D012697:Serine Endopeptidases / Q000235:genetics*; D014764:Viral Proteins / Q000378:metabolism*
D006360:Heat-Shock Proteins; C027812:O protein, Bacteriophage lambda; D014764:Viral Proteins; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases