Cotranslational N-degron masking by acetylation promotes proteome stability in plants
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Nature Communications |
Volume | 13 |
Issue number | 1 |
Pages (from-to) | 810 |
ISSN | 2041-1723 |
DOIs | |
Publication status | Published - 2022 |
Externally published | Yes |
Bibliographical note
© 2022. The Author(s).
ID: 292144066