Interaction of ribosome recycling factor and elongation factor EF‐G with E. coli ribosomes studied by the surface plasmon resonance technique

Ribosome recycling factor (RRF), in concert with elongation factor EF‐G, is required for disassembly of the post‐termination complex of a ribosome after the release of polypeptides. How RRF dissociates the complex has long been puzzling. Crystal structures of RRF molecules have been solved recently and shown to mimic a transfer RNA (tRNA) shape, which prompted us to examine whether RRF binds to the ribosome as tRNA does.

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