TY - JOUR A1 - Nürenberg-Goloub, Elina A1 - Heinemann, Holger A1 - Gerovac, Milan A1 - Tampé, Robert T1 - Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1 T2 - Life science alliance N2 - Ribosome recycling orchestrated by ABCE1 is a fundamental process in protein translation and mRNA surveillance, connecting termination with initiation. Beyond the plenitude of well-studied translational GTPases, ABCE1 is the only essential factor energized by ATP, delivering the energy for ribosome splitting via two nucleotide-binding sites by a yet unknown mechanism. Here, we define how allosterically coupled ATP binding and hydrolysis events in ABCE1 empower ribosome recycling. ATP occlusion in the low-turnover control site II promotes formation of the pre-splitting complex and facilitates ATP engagement in the high-turnover site I, which in turn drives the structural reorganization required for ribosome splitting. ATP hydrolysis and ensuing release of ABCE1 from the small subunit terminate the post-splitting complex. Thus, ABCE1 runs through an allosterically coupled cycle of closure and opening at both sites, consistent with a processive clamp model. This study delineates the inner mechanics of ABCE1 and reveals why various ABCE1 mutants lead to defects in cell homeostasis, growth, and differentiation. KW - ABC proteins KW - ATPases KW - conformational dynamics KW - mRNA translation KW - macromolecular complexes KW - molecular motors KW - ribosome quality control Y1 - 2018 UR - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/47108 UR - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-471082 SN - 2575-1077 N1 - Copyright & Usage : © 2018 Nürenberg-Goloub et al. https://creativecommons.org/licenses/by/4.0/ This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/). VL - 1 IS - 3, e201800095 SP - 1 EP - 12 PB - Life Science Alliance, LLC CY - [Woodbury, NY] ER -