Cotranslational N-degron masking by acetylation promotes proteome stability in plants
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Cotranslational N-degron masking by acetylation promotes proteome stability in plants. / Linster, Eric; Forero Ruiz, Francy L; Miklankova, Pavlina; Ruppert, Thomas; Mueller, Johannes; Armbruster, Laura; Gong, Xiaodi; Serino, Giovanna; Mann, Matthias; Hell, Rüdiger; Wirtz, Markus.
I: Nature Communications, Bind 13, Nr. 1, 2022, s. 810.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Cotranslational N-degron masking by acetylation promotes proteome stability in plants
AU - Linster, Eric
AU - Forero Ruiz, Francy L
AU - Miklankova, Pavlina
AU - Ruppert, Thomas
AU - Mueller, Johannes
AU - Armbruster, Laura
AU - Gong, Xiaodi
AU - Serino, Giovanna
AU - Mann, Matthias
AU - Hell, Rüdiger
AU - Wirtz, Markus
N1 - © 2022. The Author(s).
PY - 2022
Y1 - 2022
N2 - 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.
AB - 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.
U2 - 10.1038/s41467-022-28414-5
DO - 10.1038/s41467-022-28414-5
M3 - Journal article
C2 - 35145090
VL - 13
SP - 810
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
ER -
ID: 292144066