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Updated: Oct 1, 2025

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
Published on: February 27, 2020
A stable start: cotranslational Nt-acetylation promotes proteome stability across kingdoms
Daniel J Gibbs1, Mark Bailey2, Ross D Etherington1
1School of Biosciences, University of Birmingham, Edgbaston, B15 2TT, UK.
Cotranslational N-terminal protein acetylation (NTA) stabilizes proteins in humans and plants by blocking degradation signals. This finding contrasts with prior research, highlighting NTA
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- N-terminal protein acetylation (NTA) is a widespread post-translational modification.
- Previous studies suggested a role for NTA in protein degradation.
- The precise function of NTA in regulating protein stability remained unclear.
Purpose of the Study:
- To investigate the role of cotranslational N-terminal protein acetylation (NTA) in proteome stability.
- To reconcile conflicting findings regarding NTA's function in protein turnover.
Main Methods:
- Analysis of proteome stability in human and plant systems.
- Investigating the impact of NTA on N-degron accessibility.
Main Results:
- Cotranslational NTA was shown to promote proteome stability in both humans and plants.
- NTA masks specific N-terminal degradation signals (N-degrons).
- This masking prevents premature protein destabilization.
Conclusions:
- NTA plays a crucial role in maintaining proteome stability by preventing degradation.
- The function of NTA is context-specific and more complex than previously thought.
- These findings revise the understanding of NTA's role in protein homeostasis.
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