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.; Nielsen, H.; Urlaub, H.; Bohnsack, K. E.; Bohnsack, M. T.

doi:10.1038/s41467-021-26208-9

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

/persons/resource/persons185577

Pan, K. T.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons15947

Urlaub, H.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

3385384.pdf
(Publisher version), 4MB

Supplementary Material (public)

There is no public supplementary material available

Citation

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.

Cite as: https://hdl.handle.net/21.11116/0000-000A-8186-C

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.