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The properties of 30S ribosomal subunits from untreated and from colicin E3-treated (E3-30S) bacteria have been compared. Polyacrylamide gel electrophoresis of ribosomal proteins revealed no difference, but several studies indicated that the 16S RNA from E3-30S particles was modified. E3-16S RNA showed slightly increased resistance to heat-induced degradation and had a reduced (15 S) sedimentation coefficient on sucrose gradients. Fingerprint analyses of E3-16S RNA revealed that the 3'-terminus of the molecule had been deleted. It was concluded that a primary effect of colicin E3 is the activation of a highly specific RNase that degrades 30S ribosomal RNA in situ, and that the resulting fragment(s) are probably retained within the 30S particle.

Effect of Colicin E3 upon the 30S Ribosomal Subunit of Escherichia coli