Relationship between methylation of adenine near the 3' end of 16-S ribosomal RNA and the activity of 30-S ribosomal subunits.

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 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.