Abstract
At Mg2+ concentrations optimal for protein synthesis on natural messenger UNA, initiation factor IF-3† effectively inhibits the association of 30 s and 50 s ribosomal subunits but does not cause the dissociation of single ribosomes. The rate of exchange between single ribosomes and ribosomal subunits is very slow at these concentrations of Mg2+, but increases markedly at lesser concentrations of Mg2+. The net dissociation of single ribosomes observed at low concentrations of Mg2+ in the presence of IF-3 is not stimulated by this factor, but proceeds only to the extent of spontaneous dissociation of single ribosomes, with IF-3 subsequently intercepting the ribosomal subunits. The inhibition of ribosomal subunit association is displayed by highly purified IF-3, but not by IF-1 or IF-2. It can be overcome in the presence of 0.01 mspermidine, but not by putrescine. Ribosomal subunit association also is inhibited by tetracycline; this inhibition likewise is overcome by spermidine.
| Original language | English |
|---|---|
| Pages (from-to) | 583-598 |
| Number of pages | 16 |
| Journal | Journal of Molecular Biology |
| Volume | 71 |
| Issue number | 3 |
| DOIs | |
| State | Published - 28 Nov 1972 |
| Externally published | Yes |
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