The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly

Gerald Ryan R. Aquino, Philipp Hackert, Nicolai Krogh, Kuan-Ting Pan, Mariam Jaafar, Anthony K. Henras, Henrik Nielsen, Henning Urlaub, Katherine E. Bohnsack () and Markus T. Bohnsack ()
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Gerald Ryan R. Aquino: University Medical Center Göttingen
Philipp Hackert: University Medical Center Göttingen
Nicolai Krogh: University of Copenhagen
Kuan-Ting Pan: Max Planck Institute for Biophysical Chemistry, Bioanalytical Mass Spectrometry
Mariam Jaafar: Université de Toulouse, CNRS, UPS
Anthony K. Henras: Université de Toulouse, CNRS, UPS
Henrik Nielsen: University of Copenhagen
Henning Urlaub: Max Planck Institute for Biophysical Chemistry, Bioanalytical Mass Spectrometry
Katherine E. Bohnsack: University Medical Center Göttingen
Markus T. Bohnsack: University Medical Center Göttingen

Nature Communications, 2021, vol. 12, issue 1, 1-16

Abstract: Abstract Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center (PTC) and is responsible for stabilizing interactions between the 5′ and 3′ ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation.

Date: 2021
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DOI: 10.1038/s41467-021-26208-9

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