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

Aquino, G. R. R., Hackert, P., Krogh, N., Pan, K. T., Jaafar, M., Henras, A. K., et al. (2021). The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly. Nature Communications, 12: 6152. doi:10.1038/s41467-021-26208-9.

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Aquino, G. R. R., Author
Hackert, P., Author
Krogh, N., Author
Pan, K. T.1, Author           
Jaafar, M., Author
Henras, A. K., Author
Nielsen, H., Author
Urlaub, H.1, Author           
Bohnsack, K. E., Author
Bohnsack, M. T., Author
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1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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 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 interac- tions 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.

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Language(s): eng - English
 Dates: 2021-10-22
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-021-26208-9
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Title: Nature Communications
Source Genre: Journal
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Pages: 16 Volume / Issue: 12 Sequence Number: 6152 Start / End Page: - Identifier: ISSN: 2041-1723