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- W2010248876 abstract "1 The binding of washed 30-S ribosomal subunits of Escherichia coli to MS2 RNA in the absence of fMet-tRNA requires the presence of the initiation factor IF-3. No binding is observed with IF-1, IF-2 or a combination of these two initiation factors. 2 The IF-3-dependent binding is stimulated about two-fold by IF-2. IF-1 has no effect in this respect. Optimal binding occurs at about 7 mM Mg2+. 3 Upon incubation of [35S]IF-3, MS2 [3H]RNA and 30-S subunits, complexes are formed which contain the three components in a 1:1:1 ratio. These ternary complexes have a sedimentation coefficient of about 40 S and a buoyant density in CsCl of about 1.74 g/ml. 4 The ternary complexes formed in the absence of IF-2 and IF-1 are rather labile and readily dissociate into MS2 RNA and IF-3-containing ribosomes. Their half-life at 0°C is about 40 min. In the presence of IF-2 and IF-1, complexes are formed which remain stable for at least 6 h. Unwashed native 30-S subunits also form stable complexes with MS2 RNA. 5 Binding of washed 30-S subunits to unfolded MS2 RNA (MS2 RNA treated with formaldehyde) does not require initiation factors. Complexes containing more than one ribosomal particle per messenger can be formed. Attachment of fMet-tRNA to these complexes requires IF-2 and IF-1, but is optimal in the presence of all three initiation factors. 6 Release of [35S]IF-3 from the MS2 RNA · 30-S subunit complexes occurs upon attachment of fMet-tRNA. In the case of unwashed native 30-S ribosomal subunits, recycling of IF-3 occurs at the same stage as was demonstrated by a direct determination of the stoichiometry of unlabeled IF-3 on the ribosomal complexes." @default.
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- W2010248876 date "1973-12-01" @default.
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- W2010248876 title "Initiation Factor-Dependent Binding of MS2 RNA to 30-S Ribosomes and the Recycling of IF-3" @default.
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- W2010248876 doi "https://doi.org/10.1111/j.1432-1033.1973.tb03197.x" @default.
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