The ATPase Fap7 Tests the Ability to Carry Out Translocation-like Conformational Changes and Releases Dim1 during 40S Ribosome Maturation

Late in their maturation, nascent small (40S) ribosomal subunits bind 60S subunits to produce 80Slike ribosomes. Because of the analogy of this translation- like cycle to actual translation, and because 80S-like ribosomes do not produce any protein, it has been suggested that this represents a quality control mechanism for subunit functionality. Here we use genetic and biochemical experiments to show that the essential ATPase Fap7 promotes formation of the rotated state, a key intermediate in translocation, thereby releasing the essential assembly factor Dim1 from pre-40S subunits. Bypassing this quality control step produces defects in reading frame maintenance. These results show how progress in the maturation cascade is linked to a test for a key functionality of 40S ribosomes: their ability to translocate the mRNA, tRNA pair. Furthermore, our data demonstrate for the first time that the translation- like cycle is a quality control mechanismthat ensures the fidelity of the cellular ribosome pool.