Structural basis for the final steps of human 40S ribosome maturation.

Nature
Michael AmeismeierRoland Beckmann

Abstract

Eukaryotic ribosomes consist of a small 40S and a large 60S subunit that are assembled in a highly coordinated manner. More than 200 factors ensure correct modification, processing and folding of ribosomal RNA and the timely incorporation of ribosomal proteins1,2. Small subunit maturation ends in the cytosol, when the final rRNA precursor, 18S-E, is cleaved at site 3 by the endonuclease NOB13. Previous structures of human 40S precursors have shown that NOB1 is kept in an inactive state by its partner PNO14. The final maturation events, including the activation of NOB1 for the decisive rRNA-cleavage step and the mechanisms driving the dissociation of the last biogenesis factors have, however, remained unresolved. Here we report five cryo-electron microscopy structures of human 40S subunit precursors, which describe the compositional and conformational progression during the final steps of 40S assembly. Our structures explain the central role of RIOK1 in the displacement and dissociation of PNO1, which in turn allows conformational changes and activation of the endonuclease NOB1. In addition, we observe two factors, eukaryotic translation initiation factor 1A domain-containing protein (EIF1AD) and leucine-rich repeat-containing p...Continue Reading

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Citations

Mar 22, 2021·The Journal of Biological Chemistry·Eric Westhof, Neocles B Leontis
Apr 29, 2021·ELife·Laura PlassartCelia Plisson-Chastang
Jun 3, 2021·International Journal of Molecular Sciences·Annalisa PecoraroAnnapina Russo
Jul 3, 2021·International Journal of Molecular Sciences·Xiao LiLasse Lindahl

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BETA
GTPase
Fluorescence
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electrophoresis
NMR
transfection

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Relion
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PyMOL Molecular Graphics System
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