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Significance Recruitment of messenger RNA (mRNA) into the decoding site of the eukaryotic 40S ribosomal subunit is a critical step in the process of mRNA selection for translation. This step is known to require an open conformation of the decoding site to be induced, but the opening mechanism has not yet been determined. We generated a quantitative assay to monitor conformation changes that occur during mRNA recruitment using a reconstituted system. We show that, unexpectedly, mRNA recruitment is dependent on both the eukaryotic initiation factor (eIF) 4A DEAD-box helicase and ATP. This function of eIF4A is completely independent of its unwinding activity and thus functions as a regulator of translation initiation regardless of mRNA secondary structure content.

A helicase-independent activity of eIF4A in promoting mRNA recruitment to the human ribosome