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-Structure paper
| Title | Mechanism of ribosome stalling by the AMD1 C-terminal tail arrest peptide. |
|---|---|
| Journal, issue, pages | Sci Adv, Vol. 12, Issue 13, Page eaec5067, Year 2026 |
| Publish date | Mar 27, 2026 |
Authors | Emir 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 links | Sci Adv / PubMed:41894501 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.86 Å |
| Structure data | EMDB-72314, PDB-9q7q: |
| Chemicals | ![]() ChemComp-MG: ![]() ChemComp-ZN: |
| Source |
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Keywords | RIBOSOME / AMD1 / ribosome stalling / arresting peptide / eRF1 / ABCE1 |
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