Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry

Kristin Kiosze-Becker, Alessandro Ori, Milan Gerovac, André Heuer, Elina Nürenberg-Goloub, Umar Jan Rashid, Thomas Becker, Roland Beckmann, Martin Beck and Robert Tampé ()
Additional contact information
Kristin Kiosze-Becker: Institute of Biochemistry, Biocenter, Goethe University Frankfurt
Alessandro Ori: Structural and Computational Biology Unit, EMBL Heidelberg
Milan Gerovac: Institute of Biochemistry, Biocenter, Goethe University Frankfurt
André Heuer: Gene Center and Center for Integrated Protein Science Munich (CiPSM), University of Munich
Elina Nürenberg-Goloub: Institute of Biochemistry, Biocenter, Goethe University Frankfurt
Umar Jan Rashid: Institute of Biochemistry, Biocenter, Goethe University Frankfurt
Thomas Becker: Gene Center and Center for Integrated Protein Science Munich (CiPSM), University of Munich
Roland Beckmann: Gene Center and Center for Integrated Protein Science Munich (CiPSM), University of Munich
Martin Beck: Structural and Computational Biology Unit, EMBL Heidelberg
Robert Tampé: Institute of Biochemistry, Biocenter, Goethe University Frankfurt

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: Abstract Ribosome recycling orchestrated by the ATP binding cassette (ABC) protein ABCE1 can be considered as the final—or the first—step within the cyclic process of protein synthesis, connecting translation termination and mRNA surveillance with re-initiation. An ATP-dependent tweezer-like motion of the nucleotide-binding domains in ABCE1 transfers mechanical energy to the ribosome and tears the ribosome subunits apart. The post-recycling complex (PRC) then re-initiates mRNA translation. Here, we probed the so far unknown architecture of the 1-MDa PRC (40S/30S·ABCE1) by chemical cross-linking and mass spectrometry (XL-MS). Our study reveals ABCE1 bound to the translational factor-binding (GTPase) site with multiple cross-link contacts of the helix–loop–helix motif to the S24e ribosomal protein. Cross-linking of the FeS cluster domain to the ribosomal protein S12 substantiates an extreme lever-arm movement of the FeS cluster domain during ribosome recycling. We were thus able to reconstitute and structurally analyse a key complex in the translational cycle, resembling the link between translation initiation and ribosome recycling.

Date: 2016
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms13248 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:7:y:2016:i:1:d:10.1038_ncomms13248

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

DOI: 10.1038/ncomms13248

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 ().