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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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Bibliographic Details
Main Authors: Klein, Marius (Author) , Wild, Klemens (Author) , McTiernan, Nina (Author) , Arnesen, Thomas (Author) , Sinning, Irmgard (Author)
Format: Article (Journal)
Language:English
Published: 23 January 2026
In: Nature Communications
Year: 2026, Volume: 17, Pages: 1-14
ISSN:2041-1723
DOI:10.1038/s41467-026-68787-5
Online Access: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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Author Notes:Marius Klein, Klemens Wild, Nina McTiernan, Thomas Arnesen & Irmgard Sinning
Description
Summary: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.
Item Description:Gesehen am 23.03.2026
Physical Description:Online Resource
ISSN:2041-1723
DOI:10.1038/s41467-026-68787-5

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