Cotranslational N-degron masking by acetylation promotes proteome stability in plants
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N-terminal protein acetylation (NTA) is a prevalent protein modification essential for viability in animals and plants. The dominant executor of NTA is the ribosome tethered Nα-acetyltransferase A (NatA) complex. However, the impact of NatA on protein fate is still enigmatic. Here, we demonstrate that depletion of NatA activity leads to a 4-fold increase in global protein turnover via the ubiquitin-proteasome system in Arabidopsis. Surprisingly, a concomitant increase in translation, actioned via enhanced Target-of-Rapamycin activity, is also observed, implying that defective NTA triggers feedback mechanisms to maintain steady-state protein abundance. Quantitative analysis of the proteome, the translatome, and the ubiquitome reveals that NatA substrates account for the bulk of this enhanced turnover. A targeted analysis of NatA substrate stability uncovers that NTA absence triggers protein destabilization via a previously undescribed and widely conserved nonAc/N-degron in plants. Hence, the imprinting of the proteome with acetylation marks is essential for coordinating proteome stability.
Originalsprog | Engelsk |
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Tidsskrift | Nature Communications |
Vol/bind | 13 |
Udgave nummer | 1 |
Sider (fra-til) | 810 |
ISSN | 2041-1723 |
DOI | |
Status | Udgivet - 2022 |
Eksternt udgivet | Ja |
Bibliografisk note
© 2022. The Author(s).
ID: 292144066