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| Title | NatA engages in multi-factor complexes at the ribosomal polypeptide tunnel exit. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 17, Issue 1, Page 884, Year 2026 |
| Publish date | Jan 23, 2026 |
 Authors | Marius Klein / Klemens Wild / Nina McTiernan / Thomas Arnesen / Irmgard Sinning /   |
| PubMed Abstract | N-terminal acetylation (NTA) is the most common protein modification in eukaryotes, playing a crucial role in proteostasis. Almost 40% of the human proteome is acetylated co-translationally by the ...N-terminal acetylation (NTA) is the most common protein modification in eukaryotes, playing a crucial role in proteostasis. Almost 40% of the human proteome is acetylated co-translationally by the NatA complex, which requires prior N-terminal methionine excision (NME). Recently, NatA was shown to form multi-enzyme complexes with MAP1/NAC or MAP2, combining the capabilities of NME and NTA into a single complex. Here, we show that NatA can also form ribosome-independent assemblies with several ribosome associated factors (RAFs). At the ribosome, NatA can form a ternary complex with the abundant pseudoenzyme Ebp1 or a second copy of NatA, which can be coordinated from a different binding site with closer access to a potential substrate. Further, we identify a conserved binding site on NatA, which can be accessed by four RAFs - Ebp1, NAC, Naa10 and HypK, allowing the formation of different multi-factor complexes at the ribosomal tunnel exit. Therefore, our data suggest that NatA constitutes an interaction hub, and contributes to the coordination of co-translational protein maturation. |
 External links | Nat Commun / PubMed:41577663 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.91 - 4.61 Å |
| Structure data | EMDB-51382, PDB-9gj5: EMDB-51383, PDB-9gj6: |
| Chemicals |  ChemComp-KGN:  ChemComp-IHP: |
| Source |
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 Keywords | TRANSLATION / human 80S ribosome / N-terminal acetylation (NTA) / N-acety-transferase A (NatA) / Ebp1 / PA2G4 / N-acety-transferase A (NatA) in proximal and distal position |
homo sapiens (human)