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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Holland, I. B. Senior, B. W. |
| 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 5 |
| Volume Number | 68 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1971-07-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Colicins Pharmacology Escherichia Coli Cytology Ribosomes Drug Effects Autoradiography Bacterial Proteins Centrifugation, Density Gradient Densitometry Electrophoresis, Disc Nucleoproteins RNA, Ribosomal Metabolism Ribonucleases Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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