Cotranslational N-degron masking by acetylation promotes proteome stability in plants
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 th...
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| Hauptverfasser: | , , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
10 February 2022
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| In: |
Nature Communications
Year: 2022, Jahrgang: 13, Pages: 1-12 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-022-28414-5 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: https://doi.org/10.1038/s41467-022-28414-5 Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41467-022-28414-5 
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| Verfasserangaben: | Eric Linster, Francy L. Forero Ruiz, Pavlina Miklankova, Thomas Ruppert, Johannes Mueller, Laura Armbruster, Xiaodi Gong, Giovanna Serino, Matthias Mann, Rüdiger Hell & Markus Wirtz |
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| 245 | 1 | 0 | |a Cotranslational N-degron masking by acetylation promotes proteome stability in plants |c Eric Linster, Francy L. Forero Ruiz, Pavlina Miklankova, Thomas Ruppert, Johannes Mueller, Laura Armbruster, Xiaodi Gong, Giovanna Serino, Matthias Mann, Rüdiger Hell & Markus Wirtz |
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| 520 | |a 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. | ||
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