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

Brüning, L., Hackert, P., Martin, R., Gallesio, J. D., Aquino, G. R. R., Urlaub, H., et al. (2018). RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes. Nature Communications, 9: 5383. doi:10.1038/s41467-018-07783-w.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-B64E-A Version Permalink: http://hdl.handle.net/21.11116/0000-0003-39AD-B
Genre: Journal Article

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 Creators:
Brüning, L., Author
Hackert, P., Author
Martin, R., Author
Gallesio, J. D., Author
Aquino, G. R. R., Author
Urlaub, H.1, Author              
Sloan, K. E., Author
Bohnsack, M. T., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 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.

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Language(s): eng - English
 Dates: 2018-12-19
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41467-018-07783-w
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Title: Nature Communications
Source Genre: Journal
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Pages: 14 Volume / Issue: 9 Sequence Number: 5383 Start / End Page: - Identifier: -