MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments

Klemens Wild, Milan Aleksić, Karine Lapouge, Keven D. Juaire, Dirk Flemming, Stefan Pfeffer () and Irmgard Sinning ()
Additional contact information
Klemens Wild: Biochemiezentrum der Universität Heidelberg (BZH), INF 328
Milan Aleksić: Zentrum für Molekulare Biologie der Universität Heidelberg, INF282
Karine Lapouge: Biochemiezentrum der Universität Heidelberg (BZH), INF 328
Keven D. Juaire: Biochemiezentrum der Universität Heidelberg (BZH), INF 328
Dirk Flemming: Biochemiezentrum der Universität Heidelberg (BZH), INF 328
Stefan Pfeffer: Zentrum für Molekulare Biologie der Universität Heidelberg, INF282
Irmgard Sinning: Biochemiezentrum der Universität Heidelberg (BZH), INF 328

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract Human Ebp1 is a member of the proliferation-associated 2G4 (PA2G4) family and plays an important role in cancer regulation. Ebp1 shares the methionine aminopeptidase (MetAP) fold and binds to mature 80S ribosomes for translational control. Here, we present a cryo-EM single particle analysis reconstruction of Ebp1 bound to non-translating human 80S ribosomes at a resolution range from 3.3 to ~8 Å. Ebp1 blocks the tunnel exit with major interactions to the general uL23/uL29 docking site for nascent chain-associated factors complemented by eukaryote-specific eL19 and rRNA helix H59. H59 is defined as dynamic adaptor undergoing significant remodeling upon Ebp1 binding. Ebp1 recruits rRNA expansion segment ES27L to the tunnel exit via specific interactions with rRNA consensus sequences. The Ebp1-ribosome complex serves as a template for MetAP binding and provides insights into the structural principles for spatial coordination of co-translational events and molecular triage at the ribosomal tunnel exit.

Date: 2020
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-020-14603-7 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14603-7

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-020-14603-7

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().