RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes

Lukas Brüning, Philipp Hackert, Roman Martin, Jimena Davila Gallesio, Gerald Ryan R. Aquino, Henning Urlaub, Katherine E. Sloan () and Markus T. Bohnsack ()
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Lukas Brüning: University Medical Center Göttingen
Philipp Hackert: University Medical Center Göttingen
Roman Martin: University Medical Center Göttingen
Jimena Davila Gallesio: University Medical Center Göttingen
Gerald Ryan R. Aquino: University Medical Center Göttingen
Henning Urlaub: Bioanalytical Mass Spectrometry
Katherine E. Sloan: University Medical Center Göttingen
Markus T. Bohnsack: University Medical Center Göttingen

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: Abstract Production of eukaryotic ribosomal subunits is a highly dynamic process; pre-ribosomes undergo numerous structural rearrangements that establish the architecture present in mature complexes and serve as key checkpoints, ensuring the fidelity of ribosome assembly. Using in vivo crosslinking, we here identify the pre-ribosomal binding sites of three RNA helicases. Our data support roles for Has1 in triggering release of the U14 snoRNP, a critical event during early 40S maturation, and in driving assembly of domain I of pre-60S complexes. Binding of Mak5 to domain II of pre-60S complexes promotes recruitment of the ribosomal protein Rpl10, which is necessary for subunit joining and ribosome function. Spb4 binds to a molecular hinge at the base of ES27 facilitating binding of the export factor Arx1, thereby promoting pre-60S export competence. Our data provide important insights into the driving forces behind key structural remodelling events during ribosomal subunit assembly.

Date: 2018
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DOI: 10.1038/s41467-018-07783-w

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