Relationship between Methylation of Adenine Near the 3′ End of 16‐S Ribosomal RNA and the Activity of 30‐S Ribosomal Subunits

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Abstract
The relationship between methylation of adenine near the 3′ end of 16‐S ribosomal RNA and the activity of 30‐S ribosomal subunits has been studied using 30‐S subunits from kasugamycin‐sensitive and kasugamycin‐resistant bacteria. Analysis of the proteins of 30‐S subunits by gel electrophoresis showed that the content of protein S1 in 30‐S subunits from a kasugamycin‐resistant strain was smaller than that in 30‐S subunits from the parent strain. Although polyphenylalanine‐synthetic activity of 30‐S subunits from a kasugamycin‐resistant strain previously methylated by a methylase purified from Escherichia coli Q13 was nearly equal to that of untreated 30‐S subunits, both phenylalanine‐synthetic activity and the content of protein S1 in the 30‐S particles reconstituted from 23‐S core particles and split proteins from the kasugamycin‐resistant strain increased by prior methylation of 23‐S core particles by the methylase. These results suggest that methylation of adenine near the 3′ end of 16‐S rRNA induces an increase of polypeptide‐synthetic activity by the acceleration of binding of protein S1 to S1‐depleted 30‐S subunits.