Molecular analysis of the ribosome recycling factor ABCE1 bound to the 30S post-splitting complex

  • Ribosome recycling by the twin-ATPase ABCE1 is a key regulatory process in mRNA translation and surveillance and in ribosome-associated protein quality control in Eukarya and Archaea. Here, we captured the archaeal 30S ribosome post-splitting complex at 2.8 Å resolution by cryo-electron microscopy. The structure reveals the dynamic behavior of structural motifs unique to ABCE1, which ultimately leads to ribosome splitting. More specifically, we provide molecular details on how conformational rearrangements of the iron–sulfur cluster domain and hinge regions of ABCE1 are linked to closure of its nucleotide-binding sites. The combination of mutational and functional analyses uncovers an intricate allosteric network between the ribosome, regulatory domains of ABCE1, and its two structurally and functionally asymmetric ATP-binding sites. Based on these data, we propose a refined model of how signals from the ribosome are integrated into the ATPase cycle of ABCE1 to orchestrate ribosome recycling.
Metadaten
Author:Elina Nürenberg-GoloubORCiDGND, Hanna Kratzat, Holger Heinemann, André Heuer, Peter Kötter, Otto Berninghausen, Thomas Becker, Robert TampéORCiDGND, Roland Beckmann
URN:urn:nbn:de:hebis:30:3-638262
DOI:https://doi.org/10.15252/embj.2019103788
ISSN:1460-2075
Parent Title (English):The EMBO journal
Publisher:EMBO Press; Wiley
Place of publication:Heidelberg; Hoboken, NJ [u.a.]
Document Type:Article
Language:English
Date of Publication (online):2020/02/17
Date of first Publication:2020/02/17
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2022/03/08
Tag:ABC proteins, ribosome recycling; mRNA surveillance; molecular machines; ribosome-associated quality control
Volume:39
Issue:9, art. e103788
Page Number:13
First Page:1
Last Page:13
Note:
E.N.G. was supported by the Christiane Nüsslein-Volhard Foundation, L'Oréal, and the United Nations Educational, Scientific and Cultural Organization (UNESCO). H.K. is supported by a DFG fellowship through the Graduate School of Quantitative Bioscience Munich (QBM). The German Research Foundation (DFG) SFB 902 “Molecular mechanisms of RNA-based regulation” (to R.T.), TRR174 “Spatiotemporal dynamics of bacterial cells” (to R.B.) and FOR 1805 (to R.B.) funded this work.
HeBIS-PPN:49374620X
Institutes:Biochemie, Chemie und Pharmazie
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - Namensnennung 4.0