Abstract
The interaction of translational elongation factor EF-G with the ribosome in the posttranslocational state has been mapped by directed hydroxyl radical probing. Localized hydroxyl radicals were generated from Fe(II) tethered to 18 different sites on the surface of EF-G bound to the ribosome. Cleavages in ribosomal RNA were mapped, providing proximity relationships between specific sites of EF-G and rRNA elements of the ribosome. Collectively, these data provide a set of constraints by which EF-G can be positioned unambiguously in the ribosome at low resolution. The proximities of different domains of EF-G to well-characterized elements of rRNA have additional implications for the mechanism of protein synthesis.
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