TY - JOUR A1 - Kiosze-Becker, Kristin A1 - Ori, Alessandro A1 - Gerovac, Milan A1 - Heuer, André A1 - Nürenberg-Goloub, Elina A1 - Rashid, Umar Jan A1 - Becker, Thomas A1 - Beckmann, Roland A1 - Beck, Martin A1 - Tampé, Robert T1 - Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry T2 - Nature Communications N2 - 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. KW - Cryoelectron microscopy KW - Mass spectrometry KW - Ribosome Y1 - 2016 UR - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/48370 UR - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-483708 SN - 2041-1723 N1 - Rights and permissions: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ VL - 7 IS - Art. 13248 SP - 1 EP - 9 PB - Nature Publishing Group UK CY - [London] ER -