ArticleLife science alliance2018
Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1.
Article in Life science alliance, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Genetic dissection of human ABCE1 in yeast reveals separable requirements for ribosome recycling and suppression of aberrant reinitiation.FEBS open bio · 2026Article
- Braess' Paradox in Enzyme Kinetics: Asymmetry from Population Balance without Direct Cooperativity.Journal of chemical theory and computation · 2026Article
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- Human ABCE1 exhibits temperature-dependent heterologous co-functionality in S. cerevisiae.FEBS open bio · 2022Article
- Rebirth of the translational machinery: The importance of recycling ribosomes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Article
- The Arabidopsis ATP-Binding Cassette E protein ABCE2 is a conserved component of the translation machinery.Frontiers in plant science · 2022Article
- Iron in Translation: From the Beginning to the End.Microorganisms · 2021Review
- ABC-F translation factors: from antibiotic resistance to immune response.FEBS letters · 2021Review
- A structural inventory of native ribosomal ABCE1-43S pre-initiation complexes.The EMBO journal · 2021Article
- Mutational analysis of Arabidopsis thaliana ABCE2 identifies important motifs for its RNA silencing suppressor function.Plant biology (Stuttgart, Germany) · 2021Article
- Article
- Molecular analysis of the ribosome recycling factor ABCE1 bound to the 30S post-splitting complex.The EMBO journal · 2020Article
- Omnipresent Maxwell's demons orchestrate information management in living cells.Microbial biotechnology · 2019Article
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Authors and funding
4 authors.
Funding
Abstract
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 re-organization 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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.