Abstract
The activity of the chain initiation factor F2 in promoting the messenger-dependent binding of formylmethionyl-transfer RNA (fMet∼tRNAf) to purified E. coli ribosomes is inhibited by sulfhydryl-binding reagents, such as N-ethylmaleimide or p-hydroxymercuribenzoate, but prior incubation with guanosine triphosphate (GTP) or with ribosomes largely prevents this inhibition. The effect of GTP suggests that it forms a complex with F2 whereby “active” sulfhydryl groups become sheltered. Experiments on the time course of the binding reaction, with and without preincubation of F2 with GTP, and gel filtration experiments with 3H-labeled GTP lend support to this suggestion.
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Selected References
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