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TitleMechanism of ribosome stalling by the AMD1 C-terminal tail arrest peptide.
Journal, issue, pagesSci Adv, Vol. 12, Issue 13, Page eaec5067, Year 2026
Publish dateMar 27, 2026
AuthorsEmir Maldosevic / Fabio S Boiocchi / Michal I Swirski / Kyle A Meiklejohn / Martina M Yordanova / Pavel V Baranov / Ahmad Jomaa /
PubMed Abstract encodes adenosylmethionine decarboxylase 1 (AMD1), a key enzyme in polyamine biosynthesis. A subset of ribosomes translating the coding sequence read through the stop codon and pause at a second in- ... encodes adenosylmethionine decarboxylase 1 (AMD1), a key enzyme in polyamine biosynthesis. A subset of ribosomes translating the coding sequence read through the stop codon and pause at a second in-frame stop 384 nucleotides downstream, producing a conserved C-terminal extension (C-tail). Despite growing evidence that such cis-acting elements regulate translation of their genes, the molecular mechanism by which the C-tail mediates ribosome stalling remains unclear. Here, we determined the structure of the ribosome nascent chain complex paused by the AMD1 C-tail which traps eukaryotic release factor 1 (eRF1) with the ATP-binding cassette subfamily E member 1 (ABCE1). The nascent chain forms a molecular clamp that positions an arginine hook in the peptidyl-transferase center, occluding the accommodation of the eRF1 GGQ motif thereby hampering translation termination. Analysis of aggregated ribosome profiling data revealed several genes with a pattern of stop codon readthrough followed by ribosome stalling at a specific location, suggesting that regulatory readthrough-stall mechanisms may not be limited to .
External linksSci Adv / PubMed:41894501 / PubMed Central
MethodsEM (single particle)
Resolution2.86 Å
Structure data

EMDB-72314, PDB-9q7q:
ABCE1-eRF1-RNC-AMD1C
Method: EM (single particle) / Resolution: 2.86 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • oryctolagus cuniculus (rabbit)
KeywordsRIBOSOME / AMD1 / ribosome stalling / arresting peptide / eRF1 / ABCE1

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