NatA engages in multi-factor complexes at the ribosomal polypeptide tunnel exit
N-terminal acetylation shapes protein fate during protein biosynthesis at the ribosome. Here the authors show that the NatA enzyme forms dynamic multi-factor complexes at the ribosome, acting as an interaction hub that coordinates cotranslational protein maturation.
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| Hauptverfasser: | , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
23 January 2026
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| In: |
Nature Communications
Year: 2026, Jahrgang: 17, Pages: 1-14 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-026-68787-5 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: https://doi.org/10.1038/s41467-026-68787-5 Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41467-026-68787-5 
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| Verfasserangaben: | Marius Klein, Klemens Wild, Nina McTiernan, Thomas Arnesen & Irmgard Sinning |
| Zusammenfassung: | N-terminal acetylation shapes protein fate during protein biosynthesis at the ribosome. Here the authors show that the NatA enzyme forms dynamic multi-factor complexes at the ribosome, acting as an interaction hub that coordinates cotranslational protein maturation. |
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| Beschreibung: | Gesehen am 23.03.2026 |
| Beschreibung: | Online Resource |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-026-68787-5 |