Overview
- Experiments show pantetheine‑derived thioesters form in neutral water and transfer activated amino acids to RNA without enzymes.
- Attachment occurs selectively at the 2',3' diol on the 3' end of double‑stranded RNA, with thioesters remaining stable and suppressing unwanted free‑peptide formation.
- Aminoacylation was observed across all four nucleotides and a wide range of amino acids, including charged residues such as arginine and lysine.
- Thioesters convert to reactive thioacids in the presence of hydrogen sulfide, enabling activation for peptide bond formation from RNA‑bound amino acids.
- Researchers argue the chemistry is most plausible in concentrated freshwater pools rather than oceans, and they note open questions about sequence specificity and integration with later translation machinery.