Abstract

The relative levels of protein L12 and its α- N-acetylated form L7 in ribosomes of Escherichia coli have previously been shown to markedly vary during the growth cycle. The present labeling study shows preferential utilization of L12 in early logarithmic phase and of L7 in late logarithmic phase. Both forms are, however, simultaneously used throughout the growth cycle. After assembly into ribosomes, L7 and L12 are conserved without net interconversion. It is therefore concluded that the variation in L12 to L7 ratio takes place through changes in the relative flow of L7 and L12 species into ribosome assembly rather than by modification in pre-existing ribosomes. During this study, we have also measured the surprisingly large difference in the binding of Coomassie Blue to these proteins.

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