Abstract
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.
MeSH Terms
Autoradiography
Bacterial Proteins/analysis
Centrifugation, Density Gradient
Colicins/pharmacology
Densitometry
Electrophoresis, Disc
Escherichia coli/cytology
Nucleoproteins/analysis
RNA, Ribosomal/metabolism
Ribonucleases/metabolism
Ribosomes/analysis,drug effects
Chemicals
Bacterial Proteins
Colicins
Nucleoproteins
RNA, Ribosomal
Ribonucleases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Senior B W
Holland I B
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21 references, click to expand
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