Localization of the Basic Aminopeptidases in Escherichia coli

Abstract

The basic aminopeptidase activity was found in both the 30 S and 50 S ribosomal subunit of Escherichia coli B; the specific activity of the enzyme in the 30 S particle was about six times that found in the 50 S particle. Although about 50% of the enzyme was released from E. coli B ribosomes on dissociation into the subunits, this was not observed with E. coli Q-13, a ribonuclease I-less strain. The partition of the basic aminopeptidase activity between the soluble and ribosomal fractions (isolated in 60 mM KCl) of E. coli was determined by the strain of E. coli used, as well as the stage and temperature of growth. Under similar growth conditions, a significantly greater amount of enzyme was found in the ribosomal fraction of E. coli B than in the corresponding fraction of E. coli K-12. When E. coli B cells were disrupted in 300 mM KCl, over 90% of the enzyme was found in the soluble fraction. The remaining 10% on the ribosomal particle had enriched activity towards methionyl peptides suggesting that more than one enzyme is present in the basic aminopeptidase fraction.