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Molecular analysis of the ribosome recycling factor ABCE 1 bound to the 30S post‐splitting complex
Author(s) -
NürenbergGoloub Elina,
Kratzat Hanna,
Heinemann Holger,
Heuer André,
Kötter Peter,
Berninghausen Otto,
Becker Thomas,
Tampé Robert,
Beckmann Roland
Publication year - 2020
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2019103788
Subject(s) - biology , ribosome , genetics , 30s , microbiology and biotechnology , computational biology , rna , gene
Ribosome recycling by the twin‐ ATP ase ABCE 1 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 ABCE 1, 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 ABCE 1 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 ABCE 1, 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 ATP ase cycle of ABCE 1 to orchestrate ribosome recycling.